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Conserved domains on  [gi|1820002560|emb|CAA9959473|]
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AMP-binding enzyme [Pyrenophora teres f. maculata]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK12316 super family cl36106
peptide synthase; Provisional
366-4096 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12316:

Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1459.40  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  366 DIFRHPTLAALASLETNQYNITIE---ETPPLSLLGENADVAQVRDEAAAMCSVDGSAIEDMYLCSPLQEGLM--SLTTK 440
Cdd:PRK12316  1495 EMFAEATVQRLADDYARELQALIEhccDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIADIYPLSPMQQGMLfhSLYEQ 1574
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  441 RAGDYIMQdvleLRADV---DEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQVVVEEKMQ-------WTESESLEEYLN 510
Cdd:PRK12316  1575 EAGDYINQ----LRVDVqglDPDRFRAAWQATVDRHEILRSGFLWQDGLEQPLQVIHKQVElpfaeldWRGREDLGQALD 1650
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  511 EDKAASMGLGDRLARYALIKESC---GGKRW-FVWTIHHALYDGWSLPLVLDAVKQVYSG----AALERqpsFNTFIQYV 582
Cdd:PRK12316  1651 ALAQAERQKGFDLTRAPLLRLVLvrtGEGRHhLIYTNHHILMDGWSNAQLLGEVLQRYAGqpvaAPGGR---YRDYIAWL 1727
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  583 SQQDVKAAAAYWQTALADCEAvlfpplPSTVTQPVA-----DTTVKYQCPPSPEVTSS--------NITTSTLIRAAWAI 649
Cdd:PRK12316  1728 QRQDAAASEAFWKEQLAALEE------PTRLAQAARtedgqVGYGDHQQLLDPAQTRAlaefaraqKVTLNTLVQAAWLL 1801
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  650 IASRYTSSEDIVFGTTVTGRNAPITGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTGLQRIMKMGp 729
Cdd:PRK12316  1802 LLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWA- 1880
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  730 GPQHACGFQTLLVV--HPTDDVLS----SDDTLGEWHSRSDselqyfTTYALTIQCTLAvEGVQITASFDARVVEHWVVE 803
Cdd:PRK12316  1881 GQGGEALFDSLLVFenYPVAEALKqgapAGLVFGRVSNHEQ------TNYPLTLAVTLG-ETLSLQYSYDRGHFDAAAIE 1953
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  804 KMLGQFSFVMQQLAE----AGVEKKVADIEtttlEDRQQLWVWNADMPPA-VDRCIHDLFAEQARARPDASAVCAWDGEL 878
Cdd:PRK12316  1954 RLDRHLLHLLEQMAEdaqaALGELALLDAG----ERQRILADWDRTPEAYpRGPGVHQRIAEQAARAPEAIAVVFGDQHL 2029
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  879 TYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSQ 958
Cdd:PRK12316  2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRH 2109
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  959 hamlfaSSERHQVTVSKVSTSqLPTVVNFAKSP-------VDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAF 1031
Cdd:PRK12316  2110 ------LLERLPLPAGVARLP-LDRDAEWADYPdtapavqLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY 2182
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1032 GYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRR-NNLAKAISTMDVNCALLTPSVARLLEPSA-----VPS 1105
Cdd:PRK12316  2183 ELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDpEQLYDEMERHGVTILDFPPVYLQQLAEHAerdgrPPA 2262
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1106 LKRLVLQGEQVSFADWNRWPGSVQT---INGYGPTECSV------CCNTYSGkqGFKSGIIGTSVASLS-WVVDAGNHnr 1175
Cdd:PRK12316  2263 VRVYCFGGEAVPAASLRLAWEALRPvylFNGYGPTEAVVtpllwkCRPQDPC--GAAYVPIGRALGNRRaYILDADLN-- 2338
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1176 LAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAwllegyeGHAGrrGRLYKTGDLVRCDADGNLVCLGRKDSQVKV 1255
Cdd:PRK12316  2339 LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG--ERLYRTGDLARYRADGVVEYLGRIDHQVKI 2409
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1256 RGQRVELGEIEHHVR--ECLPEARQLAVEVilPSGQKehalLAAFIqldkgnhnalfeekaSGEDsmAQVVFLTGVEEEL 1333
Cdd:PRK12316  2410 RGFRIELGEIEARLQahPAVREAVVVAQDG--ASGKQ----LVAYV---------------VPDD--AAEDLLAELRAWL 2466
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1334 AKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDIGASftvqqlaemrtSSQGPKRQPSTEVEQTMQQLWAQVLSIEpnS 1413
Cdd:PRK12316  2467 AARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVS-----------QLRQAYVAPQEGLEQRLAAIWQAVLKVE--Q 2533
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1414 IGLDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADIFRHPRLVDLARVQNSQFSSAAeevpafsllgedVNAVQLSQDA 1492
Cdd:PRK12316  2534 VGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTSRA------------PVLQKVTRVQ 2601
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1493 AAMCSVAagivediypcSPLQEGLMSLTAKRAGdYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSE----- 1567
Cdd:PRK12316  2602 PLPLSHA----------QQRQWFLWQLEPESAA-YHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEqtrqv 2670
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1568 ---LGLLQVVIEENIQWTEPKSLEEYLSEDKAVSVGLGDPLARyAFVKEACGGKRWFVWTIHHAVYDGWSLPLILHAVKQ 1644
Cdd:PRK12316  2671 ilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLR-VRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQ 2749
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1645 VYSGGVLQWQPSFNAFI-----------QYLGQQDLEATVAYWQTALADCEAVLFPTL--PPTVTQPVADATVEYQCP-P 1710
Cdd:PRK12316  2750 AYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLGGEQPVLELPLdrPRPALQSHRGARLDVALDvA 2829
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1711 LSKA------TSDTTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNTPvtGVEAMVGPTIATVPVRLRVQRDQTVFAFL 1784
Cdd:PRK12316  2830 LSREllalarREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQVLRAQVDAQLAFRDLL 2907
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1785 QGLQQQATDMIAHEQT-------GLQRIAKMGQGP--QHACSFQTLLVVQPVDDVLDNTLGEWRDHSelqefTTYTLMLQ 1855
Cdd:PRK12316  2908 GQVKEQALGAQAHQDLpfeqlveALQPERSLSHSPlfQVMYNHQSGERAAAQLPGLHIESFAWDGAA-----TQFDLALD 2982
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1856 CMLAAEGVQITASFDTRVIEKWVVEKMLRQFSFIMQQLAEaGAEKTVSDIETTTPEDRQQ-LWAWNQ-EVPPAIERCVHD 1933
Cdd:PRK12316  2983 TWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVE-NPQRSVDELAMLDAEERGQlLEAWNAtAAEYPLERGVHR 3061
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1934 LFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 2013
Cdd:PRK12316  3062 LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2014 PASRHEDIFRQTGAQVVVTSaQHSARWIGTNHQVVTVSAGSlEQFSTLVNPVDLpaKPENAAYVMFTSGSTGTPKGVVLE 2093
Cdd:PRK12316  3142 PEERLAYMLEDSGAQLLLSQ-SHLRLPLAQGVQVLDLDRGD-ENYAEANPAIRT--MPENLAYVIYTSGSTGKPKGVGIR 3217
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2094 HRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRDNLA-------KAITDMQVNWGY 2166
Cdd:PRK12316  3218 HSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALlvelinsEGVDVLHAYPSM 3297
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2167 LTSSVARLlDPCLVPSLKVLVLGGEQVNSTDWGKWPSSVQTINGYGPTECCVFCTGYTGIQGFQSG-NIGTSIASVSWVV 2245
Cdd:PRK12316  3298 LQAFLEEE-DAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvPIGRPIANRACYI 3376
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2246 DPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegYPGhegrqGRLYKTGDLVRYSSDGNLVCLGR 2325
Cdd:PRK12316  3377 LDGS-LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF-----VPG-----ERLYRTGDLARYRADGVIEYIGR 3445
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2326 KDSQVKVRGQRVELGEVEhhmrKCLPEANQLAVEVVPPSGERDhamLAAFIRLDDETRNSPLIIKyaednstaqivfltg 2405
Cdd:PRK12316  3446 VDHQVKIRGFRIELGEIE----ARLLEHPWVREAVVLAVDGRQ---LVAYVVPEDEAGDLREALK--------------- 3503
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2406 ieEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssegpkrQPSTEAERTMQQLWAQVLG 2485
Cdd:PRK12316  3504 --AHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVNELERRLAAIWADVLK 3570
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2486 ieLESIGLDDSFFRLGGDSITAMQISSSARALHLSVSTGDILKKKTIALIAREILPSTSTfsrSVWRDPVNNAFDLTPIQ 2565
Cdd:PRK12316  3571 --LEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGV---AVDQGPVSGETLLLPIQ 3645
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2566 HLYLTLDPSGRSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFQRQTGGRWQQYISEHDSSSLIVNHiHTRDTT 2645
Cdd:PRK12316  3646 QQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRA-ELDDAE 3724
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2646 EIVEALRQSRGSLDIERGPVLAAVLCD-AGERQSLFVAIHHLVVDLVSWRIL----LEELEDLLLGQTLP-PALSTPFQA 2719
Cdd:PRK12316  3725 ELERLGEEAQRSLDLADGPLLRALLATlADGSQRLLLVIHHLVVDGVSWRILledlQQAYQQLLQGEAPRlPAKTSSFKA 3804
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2720 WhaaqAKYIEEHVPPSAVAQveldpdQLSYW-----GVSPD--------DVLSSYAISEEFVLDRKTTSTLLGSCNDAFS 2786
Cdd:PRK12316  3805 W----AERLQEHARGEALKA------ELAYWqeqlqGVSSElpcdhpqgALQNRHAASVQTRLDRELTRRLLQQAPAAYR 3874
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2787 TRPLELMVAALSySFATIFSDRKPAAIFNEIHGREAWDSSIDLTRTVGWFTSMCPVQAANGAGLLDAIRETKDCIRSFQD 2866
Cdd:PRK12316  3875 TQVNDLLLTALA-RVVCRWTGEASALVQLEGHGREDLFADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPN 3953
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2867 NGWSYFASQFASASAADAFASLFPM-EVLFNYQGLYQ-QLERKDSLFknLPMPDSCEPALAALCPRFALFDVSFVVEQGC 2944
Cdd:PRK12316  3954 KGIGFGLLRYLGDEESRRTLAGLPVpRITFNYLGQFDgSFDEEMALF--VPAGESAGAEQSPDAPLDNWLSLNGRVYGGE 4031
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2945 AKVSFVSDKRARHQYRIRQWIQKYK---VTLIDMSALLPNRSAewTLSDLPLAfssyiDLDRFRHKTLPgleVPPEDVED 3021
Cdd:PRK12316  4032 LSLDWTFSREMFEEATIQRLADDYAaelTALVEHCCDAERHGV--TPSDFPLA-----GLDQARLDALP---LPLGEIED 4101
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3022 VFPCTPMQEGILTSQGKDPDA--YWVCFIYEVipnqeTSISLARLQQAWKGVVHQHSLLRTLLVDNvpGSTGT-TNVVLK 3098
Cdd:PRK12316  4102 IYPLSPMQQGMLFHSLYEQEAgdYINQMRVDV-----QGLDVERFRAAWQAALDRHDVLRSGFVWQ--GELGRpLQVVHK 4174
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3099 DPQPSISVFSSEGTATIELFRSRYNPAAQRSIGQLQH----HLSICQLNNGKVYLCLDINHAIIDAHSRGILMHDLQEAY 3174
Cdd:PRK12316  4175 QVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRapllRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY 4254
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3175 DANLNPQSTS-FRDFASYIKQQSQEEAGRYWAEYLDGV-EPCFF------PSLGDSGGANTIPRtvEVPSIDSSAVHMFC 3246
Cdd:PRK12316  4255 SGRPPAQPGGrYRDYIAWLQRQDAAASEAFWREQLAALdEPTRLaqaiarADLRSANGYGEHVR--ELDATATARLREFA 4332
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3247 KIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPLISILPCRIHLHKQLTVLEALKTVQENYAS 3326
Cdd:PRK12316  4333 RTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLA 4412
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3327 SLSFQTFPLASMHSFLGLGTSALFNTAL---------SLQRIddigpcSASEITLKMKEGLDPTEYNITLSAGYSkDAID 3397
Cdd:PRK12316  4413 LREHEHTPLYEIQRWAGQGGEALFDSLLvfenypvseALQQG------APGGLRFGEVTNHEQTNYPLTLAVGLG-ETLS 4485
                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3398 ISMTFRAGCMDLVQAKRLASNFSQAIKAVTTEPHSRIYSLDILTYNESKKI---WGWNADVPPAiERCVHDLFTEQAKAR 3474
Cdd:PRK12316  4486 LQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIvalWNRTDAGYPA-TRCVHQLVAERARMT 4564
                         3290      3300      3310      3320      3330      3340      3350      3360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:PRK12316  4565 PDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMM 4644
                         3370      3380      3390      3400      3410      3420      3430      3440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVASAQYSARwtssschvVTVSKALSSqlpAVVD---------STNTSVR--PENAAYIIFTSGSTGVPKGVV 3623
Cdd:PRK12316  4645 EDSGAALLLTQSHLLQR--------LPIPDGLAS---LALDrdedwegfpAHDPAVRlhPDNLAYVIYTSGSTGRPKGVA 4713
                         3450      3460      3470      3480      3490      3500      3510      3520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3624 LEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDS-DRRNSLAKAISTMDVNWAFLTPS 3702
Cdd:PRK12316  4714 VSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSlWDPERLYAEIHEHRVTVLVFPPV 4793
                         3530      3540      3550      3560      3570      3580      3590      3600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3703 VARLL-----DPGLIPSLKILAIGGEQSSSADWNRWPGSVQKI---HVYGPTECCIFCTGYTTKQGFEPST----IGTSV 3770
Cdd:PRK12316  4794 YLQQLaehaeRDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVylfNGYGPTETTVTVLLWKARDGDACGAaympIGTPL 4873
                         3610      3620      3630      3640      3650      3660      3670      3680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3771 ASVS-WVVDpeNHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNAD 3849
Cdd:PRK12316  4874 GNRSgYVLD--GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF-------GAPG--GRLYRTGDLARYRAD 4942
                         3690      3700      3710      3720      3730      3740      3750      3760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3850 GNLVYLGRKDSQVKVRGQRVELGEVEHHVRE--CLPEARQLAVEVilPSGQKdhamLAAFVqleegtqnaLLDKEAGGED 3927
Cdd:PRK12316  4943 GVIDYLGRVDHQVKIRGFRIELGEIEARLREhpAVREAVVIAQEG--AVGKQ----LVGYV---------VPQDPALADA 5007
                         3770      3780      3790      3800      3810      3820      3830      3840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3928 SMAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssqgpkrQPSTEAEQT 4007
Cdd:PRK12316  5008 DEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYV-----------APRSELEQQ 5076
                         3850      3860      3870      3880      3890      3900      3910      3920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4008 MQQLWAQVLSLgaDIIGLDDSFFRLGGDSIAAMKLVGEAR-RMGLHLSVADIFRHPKLADFAGIQITQCSSGTEEvpays 4086
Cdd:PRK12316  5077 VAAIWAEVLQL--ERVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTLAAFVELAAAAGSGDDEK----- 5149
                         3930
                   ....*....|
gi 1820002560 4087 lLGEDEDVMQ 4096
Cdd:PRK12316  5150 -FDDLEELLS 5158
PRK12316 super family cl36106
peptide synthase; Provisional
4106-6543 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12316:

Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 892.77  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4106 SVDASAITDVYPCSPLQEGLM--SLTAKRAGDYIMQtvleLRADV---NEDAFRAAWELVVQLTAVLRTRIVQHSELGLL 4180
Cdd:PRK12316  1547 PLPAGEIADIYPLSPMQQGMLfhSLYEQEAGDYINQ----LRVDVqglDPDRFRAAWQATVDRHEILRSGFLWQDGLEQP 1622
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4181 QVVVEERIQ--WTESESLEEYPREDKAVSMGVGDRLARYALIKEPY-------DGGKRW-FVWTMHHALYDGWSLPRILH 4250
Cdd:PRK12316  1623 LQVIHKQVElpFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLlrlvlvrTGEGRHhLIYTNHHILMDGWSNAQLLG 1702
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4251 AVKQAYSG-VVLERQPSFNAFIQYLSQQDPEAAAAYWqtalvdcKAALFPTLPPTVTQPVADTTVE-------YQCPPPS 4322
Cdd:PRK12316  1703 EVLQRYAGqPVAAPGGRYRDYIAWLQRQDAAASEAFW-------KEQLAALEEPTRLAQAARTEDGqvgygdhQQLLDPA 1775
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4323 QSAT--------DITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQTVFAFL 4394
Cdd:PRK12316  1776 QTRAlaefaraqKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWL 1855
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4395 QGVQQQATDMIAHEQTGLQRIAKMSpGARHACGFQTLLVVQ--PTDDVL--GSDDMLGEWRSYSEMQdfTTYALMVqCVL 4470
Cdd:PRK12316  1856 QEVQALNLALREHEHTPLYDIQRWA-GQGGEALFDSLLVFEnyPVAEALkqGAPAGLVFGRVSNHEQ--TNYPLTL-AVT 1931
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4471 VKDRVGVTASFDARVIEQWVVEKMLRQFGFVMQQLADAGEeKKVAGIETTTTGDRQQLWA-WNQDVPPA-IERCVHDQFA 4548
Cdd:PRK12316  1932 LGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQ-AALGELALLDAGERQRILAdWDRTPEAYpRGPGVHQRIA 2010
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4549 EQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 4628
Cdd:PRK12316  2011 EQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE 2090
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4629 RHEHIFRQTGAQVVLA-SAQYATLWTSLG-RSVVIVSEASTSQLPvvTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEH 4706
Cdd:PRK12316  2091 RLAYMLEDSGAALLLTqRHLLERLPLPAGvARLPLDRDAEWADYP--DTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSH 2168
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4707 KAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRR-NNLAKAINAMDVNWALLTPSVAR 4785
Cdd:PRK12316  2169 GALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDpEQLYDEMERHGVTILDFPPVYLQ 2248
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4786 ML------DPCVVqSLKILVLGGEQVNSADWDRWPKSIQT---INAYGPTECSICCTTYSGKQGFKSGT----IGTSIVS 4852
Cdd:PRK12316  2249 QLaehaerDGRPP-AVRVYCFGGEAVPAASLRLAWEALRPvylFNGYGPTEAVVTPLLWKCRPQDPCGAayvpIGRALGN 2327
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4853 VS-WVVDPENHnrLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygGHSGrqGRLYKTGDLVRYDADGN 4931
Cdd:PRK12316  2328 RRaYILDADLN--LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG--ERLYRTGDLARYRADGV 2396
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4932 LVYLGRKDSQVKLRGQRVELGEVEHHVR--ECLTEAKqlaveVIVPEGEGGyAMLAAFVqLGDDtyntlvkekaggdslt 5009
Cdd:PRK12316  2397 VEYLGRIDHQVKIRGFRIELGEIEARLQahPAVREAV-----VVAQDGASG-KQLVAYV-VPDD---------------- 2453
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5010 VQVVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREIGASFTAQQLAEmrtssqgpkrqPSTEAERTMQ 5089
Cdd:PRK12316  2454 AAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVA-----------PQEGLEQRLA 2522
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5090 QLWTRVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRT-GLQLSVADVFRHPRLVDLAYVQNSECSSAAEEVPAFSLL 5168
Cdd:PRK12316  2523 AIWQAVLKVE--QVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRV 2600
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5169 GGRAADTAQVSQdaaamcsvdassvedmypcsplqEGLMSLTAKRAGdYIMQSVLELRVDVDEDAFRAAWEHVVQLTAAL 5248
Cdd:PRK12316  2601 QPLPLSHAQQRQ-----------------------WFLWQLEPESAA-YHLPSALHLRGVLDQAALEQAFDALVLRHETL 2656
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5249 RTRIVQHSE--------LGLLQVVVEEKIQWTESKRLEEYLREDKAVSMGLGDRLARYALIKepYDGGKRWFVWTIHHAL 5320
Cdd:PRK12316  2657 RTRFVEVGEqtrqvilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLA--LDGQEHVLVITQHHIV 2734
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5321 YDGWSLPRILQAVKQIYSGAVPERQPSFNAFI-----------QYLGQQDLEAATLYWQTAL--ADCKAALFPTLPPTVT 5387
Cdd:PRK12316  2735 SDGWSMQVMVDELVQAYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLggEQPVLELPLDRPRPAL 2814
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5388 QPVADTTVEYQCPPP-------SQSATDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGVEAMVGPTIATVP 5460
Cdd:PRK12316  2815 QSHRGARLDVALDVAlsrellaLARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQV 2892
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5461 LRVCLQKDQTVSTLLECLQQQSTDMIAHEQTGL-QRIAKMSP--GARHACGFQTLLVVQPTD----DVLGSDDMLGEWRS 5533
Cdd:PRK12316  2893 LRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFeQLVEALQPerSLSHSPLFQVMYNHQSGEraaaQLPGLHIESFAWDG 2972
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5534 YSEMQDFTTYALMVQCTLAKDRVEVTASFDARVIEQwvvekMLRQFGFVMQQLAEaGAEKTVSDIETTTLEDRQQ-LWAW 5612
Cdd:PRK12316  2973 AATQFDLALDTWESAEGLGASLTYATDLFDARTVER-----LARHWQNLLRGMVE-NPQRSVDELAMLDAEERGQlLEAW 3046
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5613 NQN-VPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLA 5691
Cdd:PRK12316  3047 NATaAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLA 3126
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5692 VLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSaQHSARWIGTNHQVVTVSAGSLGQLSTlvNPVGLpAIPENAVYIM 5771
Cdd:PRK12316  3127 ILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ-SHLRLPLAQGVQVLDLDRGDENYAEA--NPAIR-TMPENLAYVI 3202
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5772 FTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCIcVPSDSDRRNDLVKAIS 5851
Cdd:PRK12316  3203 YTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV-VLAGPEDWRDPALLVE 3281
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5852 TMDVSCALLTPSVARLLE-------PSSVPTLQMLVLQGEQVSFADWNRWPASVQTINGYGPTECSICCNTYSGKQGFKS 5924
Cdd:PRK12316  3282 LINSEGVDVLHAYPSMLQafleeedAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKD 3361
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5925 GI-IGTSVASVSWVVDPENHDRlAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypgHPGrqGRLYKTGD 6003
Cdd:PRK12316  3362 AVpIGRPIANRACYILDGSLEP-VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF--------VPG--ERLYRTGD 3430
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6004 LVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQLAVEVIlpsgqkDHAMLAAFVQLEegtqnallDKE 6083
Cdd:PRK12316  3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEH-PWVREAVVLAV------DGRQLVAYVVPE--------DEA 3495
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6084 ASGEDSMAqvvflasveEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQIAnmqtssqdpkrQPST 6163
Cdd:PRK12316  3496 GDLREALK---------AHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVN 3555
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6164 EAEQTMQKLWAQVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRIGLQLSVADIFRYARLVDLAsldtsqcnsaigev 6243
Cdd:PRK12316  3556 ELERRLAAIWADVLKLE--QVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLA-------------- 3619
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6244 PAFSLLGGRAADTAQVSQDAAAMcsvdassvedmypcsPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVV 6323
Cdd:PRK12316  3620 RVARVGGGVAVDQGPVSGETLLL---------------PIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALV 3684
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6324 QLTAALRTRIVQ---HSELGLLQVVVEEKIQW---TESKRLEEYLREDKAVSMGLGD-PLARYAIIKEAWGGKRwFVWTI 6396
Cdd:PRK12316  3685 EHHDALRLRFVEdagGWTAEHLPVELGGALLWraeLDDAEELERLGEEAQRSLDLADgPLLRALLATLADGSQR-LLLVI 3763
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6397 HHALYDGWSLPRVLQAVKQAYnGAVLETQP--------SFNAFIQ----YLSQQDLEATAAYWQTALADCEATLFPPLPS 6464
Cdd:PRK12316  3764 HHLVVDGVSWRILLEDLQQAY-QQLLQGEAprlpaktsSFKAWAErlqeHARGEALKAELAYWQEQLQGVSSELPCDHPQ 3842
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6465 SVKQLVADTTVehQCPLPSRSTSDTTTST----------LIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTSID--AIV 6532
Cdd:PRK12316  3843 GALQNRHAASV--QTRLDRELTRRLLQQApaayrtqvndLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDlsRTV 3920
                         2570
                   ....*....|.
gi 1820002560 6533 GPTIATVPLRV 6543
Cdd:PRK12316  3921 GWFTSLFPVRL 3931
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
7609-8128 0e+00

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


:

Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 749.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7609 VHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 7688
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7689 PDHPASRHEEIFEQTGAQVVVASaqysarwtssschvvtvskalssqlpavvdstntsvRPENAAYIIFTSGSTGVPKGV 7768
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7769 VLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFLTPS 7848
Cdd:cd05918    125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7849 VARLLDPGLIPSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPSTIGTSVASVSWVVDPENH 7928
Cdd:cd05918    205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNH 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7929 NRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAWLLEgypGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQV 8008
Cdd:cd05918    285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQ---EGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8009 KVRGQRVELGEVEHHVRECLPEARQLAVEVILPSGQKNHAMLAVFVQLGKGTHIAHLEEKAGGEDSMAQVVFLTGTEEEL 8088
Cdd:cd05918    362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKL 441
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 8089 AKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGASFT 8128
Cdd:cd05918    442 RQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
PRK12316 super family cl36106
peptide synthase; Provisional
6257-8441 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12316:

Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 734.07  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6257 AQVSQDAAAMCSVDASSVEDMYPCSPLQEGLM--SLTAKRAGDYIMQsvleLRVDV---DEDAFRAAWEHVVQLTAALRT 6331
Cdd:PRK12316  1536 AGLSQAQLDALPLPAGEIADIYPLSPMQQGMLfhSLYEQEAGDYINQ----LRVDVqglDPDRFRAAWQATVDRHEILRS 1611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6332 RIVQHSELGLLQVVVEEKIQ-------WTESKRLEEYLREDKAVSMGLG-----DPLARYAIIKEawGGKRW-FVWTIHH 6398
Cdd:PRK12316  1612 GFLWQDGLEQPLQVIHKQVElpfaeldWRGREDLGQALDALAQAERQKGfdltrAPLLRLVLVRT--GEGRHhLIYTNHH 1689
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6399 ALYDGWSLPRVLQAVKQAYNG-AVLETQPSFNAFIQYLSQQDLEATAAYWQTALADCEAtlfpplPSSVKQLVA-----D 6472
Cdd:PRK12316  1690 ILMDGWSNAQLLGEVLQRYAGqPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEE------PTRLAQAARtedgqV 1763
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6473 TTVEHQCPLPSRSTSDTTT---------STLIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTSIDAIVGPTIATVPLRV 6543
Cdd:PRK12316  1764 GYGDHQQLLDPAQTRALAEfaraqkvtlNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIA 1843
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6544 RLQKDQTVSSFLGYLQQQATEMIAYEQTGLQQIAKMGPDPQHACgFQTLLVVQ--PAGDVLGSDDTLGKWRGYSGLQDFM 6621
Cdd:PRK12316  1844 APRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEAL-FDSLLVFEnyPVAEALKQGAPAGLVFGRVSNHEQT 1922
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6622 TYALGVRCTLsAEGVKITASFDARVIEHWVVEKMLGQFSFAMQQLAEaSADRKVADIDITTTTDRQQLWA-WN-AELPLA 6699
Cdd:PRK12316  1923 NYPLTLAVTL-GETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAE-DAQAALGELALLDAGERQRILAdWDrTPEAYP 2000
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6700 VDRCVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAF 6779
Cdd:PRK12316  2001 RGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY 2080
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6780 VPLDPDHPASRHEDILRQTGAQVIL---------------------------ASAQNTTLFQSSNQTVVTV--------- 6823
Cdd:PRK12316  2081 VPLDPNYPAERLAYMLEDSGAALLLtqrhllerlplpagvarlpldrdaewaDYPDTAPAVQLAGENLAYViytsgstgl 2160
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6824 --------------------------------------------------NRSSYILFPDENREAY-------------- 6839
Cdd:PRK12316  2161 pkgvavshgalvahcqaageryelspadcelqfmsfsfdgaheqwfhpllNGARVLIRDDELWDPEqlydemerhgvtil 2240
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6840 --------------------PFVR------------------------------------------------PSNAALAP 6851
Cdd:PRK12316  2241 dfppvylqqlaehaerdgrpPAVRvycfggeavpaaslrlawealrpvylfngygpteavvtpllwkcrpqdPCGAAYVP 2320
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6852 LGS---------------------IGELLVEGPILARGYLNDADKTAAAFVNDPAwlveghgKHPGrrGRLYKTGDLVYY 6910
Cdd:PRK12316  2321 IGRalgnrrayildadlnllapgmAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG--ERLYRTGDLARY 2391
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6911 NKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAGAaeqakTMVVAFLqlndeardallggnVP 6990
Cdd:PRK12316  2392 RADGVVEYLGRIDHQVKIRGFRIELGEIEARLQA-HPAVREAVVVAQDGASG-----KQLVAYV--------------VP 2451
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6991 NDdnlsAQVVFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREIGASFTAQQLAemrtssqgpkrQPSTE 7070
Cdd:PRK12316  2452 DD----AAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYV-----------APQEG 2516
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7071 AERTMQQLWARMLKVkaDSIGLDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADVFRHPRLVDLAYVQNSQCSSAAeev 7149
Cdd:PRK12316  2517 LEQRLAAIWQAVLKV--EQVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTSRA--- 2591
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7150 pafsllgEDVNPVQLSQDAAAMCSvaasivkdiypcSPLQEGLISLTAKRAGdYIMQSVLELRADVDEDVFCAAWEHVVQ 7229
Cdd:PRK12316  2592 -------PVLQKVTRVQPLPLSHA------------QQRQWFLWQLEPESAA-YHLPSALHLRGVLDQAALEQAFDALVL 2651
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7230 STAALRTRIVQHSE--------LGLLQVVVEEKIQWTESEALEEYLKEDKAVSMGLGDPLAHYALVKEAwGGKRWFVWTI 7301
Cdd:PRK12316  2652 RHETLRTRFVEVGEqtrqvilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALD-GQEHVLVITQ 2730
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7302 HHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAFI-----------QYLGQQDLEATAAYWQTALSDCEAVLFPPL--P 7368
Cdd:PRK12316  2731 HHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLGGEQPVLELPLdrP 2810
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7369 STVTQPVADTTVEYQCP-PLSKATLD------TTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPiaGVEAMVGPTI 7441
Cdd:PRK12316  2811 RPALQSHRGARLDVALDvALSRELLAlarregVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFV 2888
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7442 ATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIAKLGSGPR---HACGFQTLLVVQPVDDVLGSDDMLgEWRS 7518
Cdd:PRK12316  2889 NTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERslsHSPLFQVMYNHQSGERAAAQLPGL-HIES 2967
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7519 YSKMQDFTTYALMVQFTLAAEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLAEASEDSKVADIDTTTPEDRQQLWAWN 7598
Cdd:PRK12316  2968 FAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWN 3047
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7599 A-DVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAV 7677
Cdd:PRK12316  3048 AtAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAI 3127
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7678 LKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARwtssscHVVTVSKALSSQLPAVVDSTNTSVR--PENAAYI 7755
Cdd:PRK12316  3128 LKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLP------LAQGVQVLDLDRGDENYAEANPAIRtmPENLAYV 3201
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7756 IFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICV--PSDSDRRNSLAK 7833
Cdd:PRK12316  3202 IYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLagPEDWRDPALLVE 3281
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7834 AISTMDVNWAFLTPSVARLL----DPGLIPSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEP 7909
Cdd:PRK12316  3282 LINSEGVDVLHAYPSMLQAFleeeDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKD 3361
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7910 ST-IGTSVASVSWVVDPENHNRlAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypgHPGrqGRLYKTGD 7988
Cdd:PRK12316  3362 AVpIGRPIANRACYILDGSLEP-VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF--------VPG--ERLYRTGD 3430
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7989 LVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVevilpsgqknhamLAVFVQLGKGTHIAHLEEK 8068
Cdd:PRK12316  3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEH-PWVREAVV-------------LAVDGRQLVAYVVPEDEAG 3496
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8069 AGGEDSMAQvvfltgteeeLAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGASFTAQQLAetqtssqgpkrQPLT 8148
Cdd:PRK12316  3497 DLREALKAH----------LKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVN 3555
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8149 EAEQTMQQLWARVLGIDAdiIGLDDSFFRLGGDSIAAMKLVGEARRTGLQLSVADIFRHPRLIDLASLKSTFCNSVVEEV 8228
Cdd:PRK12316  3556 ELERRLAAIWADVLKLEQ--VGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQG 3633
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8229 PafsllspvmkdamfsvtepfgpslriddITDVVPASYIQQFYIATGVRAPREAFNYPFIDLSDAVDIQVLQASCSALLE 8308
Cdd:PRK12316  3634 P----------------------------VSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVE 3685
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8309 HFPILRTHFVYFQGkLYQVIPRHQDLPFSIF--------EVNGALAEESQaihiRDLD-QTSPLglpTSFTLVRNASGMN 8379
Cdd:PRK12316  3686 HHDALRLRFVEDAG-GWTAEHLPVELGGALLwraelddaEELERLGEEAQ----RSLDlADGPL---LRALLATLADGSQ 3757
                         2410      2420      2430      2440      2450      2460      2470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 8380 RLIIRLSHAQYDGVCMPVIWASLASIYQQ-----EPLL--STTGFHSYLAYVHNQRS-----ASINYWSRLLKG 8441
Cdd:PRK12316  3758 RLLLVIHHLVVDGVSWRILLEDLQQAYQQllqgeAPRLpaKTSSFKAWAERLQEHARgealkAELAYWQEQLQG 3831
AFD_class_I super family cl17068
Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, ...
1-291 7.41e-127

Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


The actual alignment was detected with superfamily member cd05918:

Pssm-ID: 473059 [Multi-domain]  Cd Length: 481  Bit Score: 410.78  E-value: 7.41e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    1 MRVNWALLTPSVARLLEPSHIPSLRILVMGGEQVNSADWDRWPSSVQTINGYGPTECCIVCTGYTSEQDFTTGTIGTSIA 80
Cdd:cd05918    194 LRVTWAFLTPSVARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLG 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   81 SVSWVVDPKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAWLLEGHGgyaGRQGRLYKTGDLVRYDADGN 160
Cdd:cd05918    274 ATCWVVDPDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQEGS---GRGRRLYRTGDLVRYNPDGS 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  161 LVCLGRKDSQVKLRGQRVELGEVEHHVRECLPEAKQLAVEVVLPLGQKNHATLAAFIQLDKGTHNALLKEKVGGDDSIAR 240
Cdd:cd05918    351 LEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEF 430
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  241 VVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASFT 291
Cdd:cd05918    431 RALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
8261-8636 1.88e-79

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


:

Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 270.72  E-value: 1.88e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8261 VVPASYIQQFYIATGVRAPREAFNYPFIDLSDAVDIQVLQASCSALLEHFPILRTHFV--YFQGKLYQVIPRHQDLPFSI 8338
Cdd:cd19542      1 IYPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVesSAEGTFLQVVLKSLDPPIEE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8339 FEVNgalaEESQAIHIRDLDQ--TSPLGLPTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQEPLLSTTG 8416
Cdd:cd19542     81 VETD----EDSLDALTRDLLDdpTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8417 FHSYLAYVHNQ-RSASINYWSRLLKGSHITNITSkLRPKLGKDTTIRSV-----KVERVIRTPqlptGLTMASLVSSAWA 8490
Cdd:cd19542    157 FSDYISYLQSQsQEESLQYWRKYLQGASPCAFPS-LSPKRPAERSLSSTrrslaKLEAFCASL----GVTLASLFQAAWA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8491 VVLSHISGEEDVVYGLVVAGRNSDLPSITEV-------------------------SVQDQYISLGESDSIGLDDIVQHC 8545
Cdd:cd19542    232 LVLARYTGSRDVVFGYVVSGRDLPVPGIDDIvgpcintlpvrvkldpdwtvldllrQLQQQYLRSLPHQHLSLREIQRAL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8546 TDWPAKSEFDSIIQHQNIEEQPEIQFAGET-TKLQWFKNSFAVSRQLFVFSHprGNSLTITITGNTGILTDQCAEKLLVM 8624
Cdd:cd19542    312 GLWPSGTLFNTLVSYQNFEASPESELSGSSvFELSAAEDPTEYPVAVEVEPS--GDSLKVSLAYSTSVLSEEQAEELLEQ 389
                          410
                   ....*....|..
gi 1820002560 8625 LCDTISQLSDSL 8636
Cdd:cd19542    390 FDDILEALLANP 401
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
315-375 1.48e-14

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


:

Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 71.83  E-value: 1.48e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560  315 RTMQQLWARVLGIEPDSIGLDDSFFRLGGDSIAAIKLVGEARRT-GLQPSVADIFRHPTLAA 375
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
 
Name Accession Description Interval E-value
PRK12316 PRK12316
peptide synthase; Provisional
366-4096 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1459.40  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  366 DIFRHPTLAALASLETNQYNITIE---ETPPLSLLGENADVAQVRDEAAAMCSVDGSAIEDMYLCSPLQEGLM--SLTTK 440
Cdd:PRK12316  1495 EMFAEATVQRLADDYARELQALIEhccDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIADIYPLSPMQQGMLfhSLYEQ 1574
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  441 RAGDYIMQdvleLRADV---DEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQVVVEEKMQ-------WTESESLEEYLN 510
Cdd:PRK12316  1575 EAGDYINQ----LRVDVqglDPDRFRAAWQATVDRHEILRSGFLWQDGLEQPLQVIHKQVElpfaeldWRGREDLGQALD 1650
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  511 EDKAASMGLGDRLARYALIKESC---GGKRW-FVWTIHHALYDGWSLPLVLDAVKQVYSG----AALERqpsFNTFIQYV 582
Cdd:PRK12316  1651 ALAQAERQKGFDLTRAPLLRLVLvrtGEGRHhLIYTNHHILMDGWSNAQLLGEVLQRYAGqpvaAPGGR---YRDYIAWL 1727
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  583 SQQDVKAAAAYWQTALADCEAvlfpplPSTVTQPVA-----DTTVKYQCPPSPEVTSS--------NITTSTLIRAAWAI 649
Cdd:PRK12316  1728 QRQDAAASEAFWKEQLAALEE------PTRLAQAARtedgqVGYGDHQQLLDPAQTRAlaefaraqKVTLNTLVQAAWLL 1801
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  650 IASRYTSSEDIVFGTTVTGRNAPITGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTGLQRIMKMGp 729
Cdd:PRK12316  1802 LLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWA- 1880
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  730 GPQHACGFQTLLVV--HPTDDVLS----SDDTLGEWHSRSDselqyfTTYALTIQCTLAvEGVQITASFDARVVEHWVVE 803
Cdd:PRK12316  1881 GQGGEALFDSLLVFenYPVAEALKqgapAGLVFGRVSNHEQ------TNYPLTLAVTLG-ETLSLQYSYDRGHFDAAAIE 1953
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  804 KMLGQFSFVMQQLAE----AGVEKKVADIEtttlEDRQQLWVWNADMPPA-VDRCIHDLFAEQARARPDASAVCAWDGEL 878
Cdd:PRK12316  1954 RLDRHLLHLLEQMAEdaqaALGELALLDAG----ERQRILADWDRTPEAYpRGPGVHQRIAEQAARAPEAIAVVFGDQHL 2029
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  879 TYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSQ 958
Cdd:PRK12316  2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRH 2109
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  959 hamlfaSSERHQVTVSKVSTSqLPTVVNFAKSP-------VDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAF 1031
Cdd:PRK12316  2110 ------LLERLPLPAGVARLP-LDRDAEWADYPdtapavqLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY 2182
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1032 GYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRR-NNLAKAISTMDVNCALLTPSVARLLEPSA-----VPS 1105
Cdd:PRK12316  2183 ELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDpEQLYDEMERHGVTILDFPPVYLQQLAEHAerdgrPPA 2262
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1106 LKRLVLQGEQVSFADWNRWPGSVQT---INGYGPTECSV------CCNTYSGkqGFKSGIIGTSVASLS-WVVDAGNHnr 1175
Cdd:PRK12316  2263 VRVYCFGGEAVPAASLRLAWEALRPvylFNGYGPTEAVVtpllwkCRPQDPC--GAAYVPIGRALGNRRaYILDADLN-- 2338
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1176 LAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAwllegyeGHAGrrGRLYKTGDLVRCDADGNLVCLGRKDSQVKV 1255
Cdd:PRK12316  2339 LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG--ERLYRTGDLARYRADGVVEYLGRIDHQVKI 2409
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1256 RGQRVELGEIEHHVR--ECLPEARQLAVEVilPSGQKehalLAAFIqldkgnhnalfeekaSGEDsmAQVVFLTGVEEEL 1333
Cdd:PRK12316  2410 RGFRIELGEIEARLQahPAVREAVVVAQDG--ASGKQ----LVAYV---------------VPDD--AAEDLLAELRAWL 2466
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1334 AKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDIGASftvqqlaemrtSSQGPKRQPSTEVEQTMQQLWAQVLSIEpnS 1413
Cdd:PRK12316  2467 AARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVS-----------QLRQAYVAPQEGLEQRLAAIWQAVLKVE--Q 2533
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1414 IGLDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADIFRHPRLVDLARVQNSQFSSAAeevpafsllgedVNAVQLSQDA 1492
Cdd:PRK12316  2534 VGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTSRA------------PVLQKVTRVQ 2601
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1493 AAMCSVAagivediypcSPLQEGLMSLTAKRAGdYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSE----- 1567
Cdd:PRK12316  2602 PLPLSHA----------QQRQWFLWQLEPESAA-YHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEqtrqv 2670
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1568 ---LGLLQVVIEENIQWTEPKSLEEYLSEDKAVSVGLGDPLARyAFVKEACGGKRWFVWTIHHAVYDGWSLPLILHAVKQ 1644
Cdd:PRK12316  2671 ilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLR-VRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQ 2749
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1645 VYSGGVLQWQPSFNAFI-----------QYLGQQDLEATVAYWQTALADCEAVLFPTL--PPTVTQPVADATVEYQCP-P 1710
Cdd:PRK12316  2750 AYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLGGEQPVLELPLdrPRPALQSHRGARLDVALDvA 2829
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1711 LSKA------TSDTTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNTPvtGVEAMVGPTIATVPVRLRVQRDQTVFAFL 1784
Cdd:PRK12316  2830 LSREllalarREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQVLRAQVDAQLAFRDLL 2907
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1785 QGLQQQATDMIAHEQT-------GLQRIAKMGQGP--QHACSFQTLLVVQPVDDVLDNTLGEWRDHSelqefTTYTLMLQ 1855
Cdd:PRK12316  2908 GQVKEQALGAQAHQDLpfeqlveALQPERSLSHSPlfQVMYNHQSGERAAAQLPGLHIESFAWDGAA-----TQFDLALD 2982
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1856 CMLAAEGVQITASFDTRVIEKWVVEKMLRQFSFIMQQLAEaGAEKTVSDIETTTPEDRQQ-LWAWNQ-EVPPAIERCVHD 1933
Cdd:PRK12316  2983 TWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVE-NPQRSVDELAMLDAEERGQlLEAWNAtAAEYPLERGVHR 3061
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1934 LFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 2013
Cdd:PRK12316  3062 LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2014 PASRHEDIFRQTGAQVVVTSaQHSARWIGTNHQVVTVSAGSlEQFSTLVNPVDLpaKPENAAYVMFTSGSTGTPKGVVLE 2093
Cdd:PRK12316  3142 PEERLAYMLEDSGAQLLLSQ-SHLRLPLAQGVQVLDLDRGD-ENYAEANPAIRT--MPENLAYVIYTSGSTGKPKGVGIR 3217
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2094 HRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRDNLA-------KAITDMQVNWGY 2166
Cdd:PRK12316  3218 HSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALlvelinsEGVDVLHAYPSM 3297
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2167 LTSSVARLlDPCLVPSLKVLVLGGEQVNSTDWGKWPSSVQTINGYGPTECCVFCTGYTGIQGFQSG-NIGTSIASVSWVV 2245
Cdd:PRK12316  3298 LQAFLEEE-DAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvPIGRPIANRACYI 3376
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2246 DPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegYPGhegrqGRLYKTGDLVRYSSDGNLVCLGR 2325
Cdd:PRK12316  3377 LDGS-LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF-----VPG-----ERLYRTGDLARYRADGVIEYIGR 3445
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2326 KDSQVKVRGQRVELGEVEhhmrKCLPEANQLAVEVVPPSGERDhamLAAFIRLDDETRNSPLIIKyaednstaqivfltg 2405
Cdd:PRK12316  3446 VDHQVKIRGFRIELGEIE----ARLLEHPWVREAVVLAVDGRQ---LVAYVVPEDEAGDLREALK--------------- 3503
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2406 ieEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssegpkrQPSTEAERTMQQLWAQVLG 2485
Cdd:PRK12316  3504 --AHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVNELERRLAAIWADVLK 3570
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2486 ieLESIGLDDSFFRLGGDSITAMQISSSARALHLSVSTGDILKKKTIALIAREILPSTSTfsrSVWRDPVNNAFDLTPIQ 2565
Cdd:PRK12316  3571 --LEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGV---AVDQGPVSGETLLLPIQ 3645
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2566 HLYLTLDPSGRSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFQRQTGGRWQQYISEHDSSSLIVNHiHTRDTT 2645
Cdd:PRK12316  3646 QQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRA-ELDDAE 3724
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2646 EIVEALRQSRGSLDIERGPVLAAVLCD-AGERQSLFVAIHHLVVDLVSWRIL----LEELEDLLLGQTLP-PALSTPFQA 2719
Cdd:PRK12316  3725 ELERLGEEAQRSLDLADGPLLRALLATlADGSQRLLLVIHHLVVDGVSWRILledlQQAYQQLLQGEAPRlPAKTSSFKA 3804
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2720 WhaaqAKYIEEHVPPSAVAQveldpdQLSYW-----GVSPD--------DVLSSYAISEEFVLDRKTTSTLLGSCNDAFS 2786
Cdd:PRK12316  3805 W----AERLQEHARGEALKA------ELAYWqeqlqGVSSElpcdhpqgALQNRHAASVQTRLDRELTRRLLQQAPAAYR 3874
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2787 TRPLELMVAALSySFATIFSDRKPAAIFNEIHGREAWDSSIDLTRTVGWFTSMCPVQAANGAGLLDAIRETKDCIRSFQD 2866
Cdd:PRK12316  3875 TQVNDLLLTALA-RVVCRWTGEASALVQLEGHGREDLFADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPN 3953
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2867 NGWSYFASQFASASAADAFASLFPM-EVLFNYQGLYQ-QLERKDSLFknLPMPDSCEPALAALCPRFALFDVSFVVEQGC 2944
Cdd:PRK12316  3954 KGIGFGLLRYLGDEESRRTLAGLPVpRITFNYLGQFDgSFDEEMALF--VPAGESAGAEQSPDAPLDNWLSLNGRVYGGE 4031
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2945 AKVSFVSDKRARHQYRIRQWIQKYK---VTLIDMSALLPNRSAewTLSDLPLAfssyiDLDRFRHKTLPgleVPPEDVED 3021
Cdd:PRK12316  4032 LSLDWTFSREMFEEATIQRLADDYAaelTALVEHCCDAERHGV--TPSDFPLA-----GLDQARLDALP---LPLGEIED 4101
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3022 VFPCTPMQEGILTSQGKDPDA--YWVCFIYEVipnqeTSISLARLQQAWKGVVHQHSLLRTLLVDNvpGSTGT-TNVVLK 3098
Cdd:PRK12316  4102 IYPLSPMQQGMLFHSLYEQEAgdYINQMRVDV-----QGLDVERFRAAWQAALDRHDVLRSGFVWQ--GELGRpLQVVHK 4174
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3099 DPQPSISVFSSEGTATIELFRSRYNPAAQRSIGQLQH----HLSICQLNNGKVYLCLDINHAIIDAHSRGILMHDLQEAY 3174
Cdd:PRK12316  4175 QVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRapllRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY 4254
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3175 DANLNPQSTS-FRDFASYIKQQSQEEAGRYWAEYLDGV-EPCFF------PSLGDSGGANTIPRtvEVPSIDSSAVHMFC 3246
Cdd:PRK12316  4255 SGRPPAQPGGrYRDYIAWLQRQDAAASEAFWREQLAALdEPTRLaqaiarADLRSANGYGEHVR--ELDATATARLREFA 4332
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3247 KIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPLISILPCRIHLHKQLTVLEALKTVQENYAS 3326
Cdd:PRK12316  4333 RTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLA 4412
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3327 SLSFQTFPLASMHSFLGLGTSALFNTAL---------SLQRIddigpcSASEITLKMKEGLDPTEYNITLSAGYSkDAID 3397
Cdd:PRK12316  4413 LREHEHTPLYEIQRWAGQGGEALFDSLLvfenypvseALQQG------APGGLRFGEVTNHEQTNYPLTLAVGLG-ETLS 4485
                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3398 ISMTFRAGCMDLVQAKRLASNFSQAIKAVTTEPHSRIYSLDILTYNESKKI---WGWNADVPPAiERCVHDLFTEQAKAR 3474
Cdd:PRK12316  4486 LQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIvalWNRTDAGYPA-TRCVHQLVAERARMT 4564
                         3290      3300      3310      3320      3330      3340      3350      3360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:PRK12316  4565 PDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMM 4644
                         3370      3380      3390      3400      3410      3420      3430      3440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVASAQYSARwtssschvVTVSKALSSqlpAVVD---------STNTSVR--PENAAYIIFTSGSTGVPKGVV 3623
Cdd:PRK12316  4645 EDSGAALLLTQSHLLQR--------LPIPDGLAS---LALDrdedwegfpAHDPAVRlhPDNLAYVIYTSGSTGRPKGVA 4713
                         3450      3460      3470      3480      3490      3500      3510      3520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3624 LEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDS-DRRNSLAKAISTMDVNWAFLTPS 3702
Cdd:PRK12316  4714 VSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSlWDPERLYAEIHEHRVTVLVFPPV 4793
                         3530      3540      3550      3560      3570      3580      3590      3600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3703 VARLL-----DPGLIPSLKILAIGGEQSSSADWNRWPGSVQKI---HVYGPTECCIFCTGYTTKQGFEPST----IGTSV 3770
Cdd:PRK12316  4794 YLQQLaehaeRDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVylfNGYGPTETTVTVLLWKARDGDACGAaympIGTPL 4873
                         3610      3620      3630      3640      3650      3660      3670      3680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3771 ASVS-WVVDpeNHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNAD 3849
Cdd:PRK12316  4874 GNRSgYVLD--GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF-------GAPG--GRLYRTGDLARYRAD 4942
                         3690      3700      3710      3720      3730      3740      3750      3760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3850 GNLVYLGRKDSQVKVRGQRVELGEVEHHVRE--CLPEARQLAVEVilPSGQKdhamLAAFVqleegtqnaLLDKEAGGED 3927
Cdd:PRK12316  4943 GVIDYLGRVDHQVKIRGFRIELGEIEARLREhpAVREAVVIAQEG--AVGKQ----LVGYV---------VPQDPALADA 5007
                         3770      3780      3790      3800      3810      3820      3830      3840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3928 SMAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssqgpkrQPSTEAEQT 4007
Cdd:PRK12316  5008 DEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYV-----------APRSELEQQ 5076
                         3850      3860      3870      3880      3890      3900      3910      3920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4008 MQQLWAQVLSLgaDIIGLDDSFFRLGGDSIAAMKLVGEAR-RMGLHLSVADIFRHPKLADFAGIQITQCSSGTEEvpays 4086
Cdd:PRK12316  5077 VAAIWAEVLQL--ERVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTLAAFVELAAAAGSGDDEK----- 5149
                         3930
                   ....*....|
gi 1820002560 4087 lLGEDEDVMQ 4096
Cdd:PRK12316  5150 -FDDLEELLS 5158
PRK12316 PRK12316
peptide synthase; Provisional
4106-6543 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 892.77  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4106 SVDASAITDVYPCSPLQEGLM--SLTAKRAGDYIMQtvleLRADV---NEDAFRAAWELVVQLTAVLRTRIVQHSELGLL 4180
Cdd:PRK12316  1547 PLPAGEIADIYPLSPMQQGMLfhSLYEQEAGDYINQ----LRVDVqglDPDRFRAAWQATVDRHEILRSGFLWQDGLEQP 1622
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4181 QVVVEERIQ--WTESESLEEYPREDKAVSMGVGDRLARYALIKEPY-------DGGKRW-FVWTMHHALYDGWSLPRILH 4250
Cdd:PRK12316  1623 LQVIHKQVElpFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLlrlvlvrTGEGRHhLIYTNHHILMDGWSNAQLLG 1702
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4251 AVKQAYSG-VVLERQPSFNAFIQYLSQQDPEAAAAYWqtalvdcKAALFPTLPPTVTQPVADTTVE-------YQCPPPS 4322
Cdd:PRK12316  1703 EVLQRYAGqPVAAPGGRYRDYIAWLQRQDAAASEAFW-------KEQLAALEEPTRLAQAARTEDGqvgygdhQQLLDPA 1775
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4323 QSAT--------DITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQTVFAFL 4394
Cdd:PRK12316  1776 QTRAlaefaraqKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWL 1855
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4395 QGVQQQATDMIAHEQTGLQRIAKMSpGARHACGFQTLLVVQ--PTDDVL--GSDDMLGEWRSYSEMQdfTTYALMVqCVL 4470
Cdd:PRK12316  1856 QEVQALNLALREHEHTPLYDIQRWA-GQGGEALFDSLLVFEnyPVAEALkqGAPAGLVFGRVSNHEQ--TNYPLTL-AVT 1931
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4471 VKDRVGVTASFDARVIEQWVVEKMLRQFGFVMQQLADAGEeKKVAGIETTTTGDRQQLWA-WNQDVPPA-IERCVHDQFA 4548
Cdd:PRK12316  1932 LGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQ-AALGELALLDAGERQRILAdWDRTPEAYpRGPGVHQRIA 2010
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4549 EQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 4628
Cdd:PRK12316  2011 EQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE 2090
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4629 RHEHIFRQTGAQVVLA-SAQYATLWTSLG-RSVVIVSEASTSQLPvvTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEH 4706
Cdd:PRK12316  2091 RLAYMLEDSGAALLLTqRHLLERLPLPAGvARLPLDRDAEWADYP--DTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSH 2168
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4707 KAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRR-NNLAKAINAMDVNWALLTPSVAR 4785
Cdd:PRK12316  2169 GALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDpEQLYDEMERHGVTILDFPPVYLQ 2248
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4786 ML------DPCVVqSLKILVLGGEQVNSADWDRWPKSIQT---INAYGPTECSICCTTYSGKQGFKSGT----IGTSIVS 4852
Cdd:PRK12316  2249 QLaehaerDGRPP-AVRVYCFGGEAVPAASLRLAWEALRPvylFNGYGPTEAVVTPLLWKCRPQDPCGAayvpIGRALGN 2327
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4853 VS-WVVDPENHnrLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygGHSGrqGRLYKTGDLVRYDADGN 4931
Cdd:PRK12316  2328 RRaYILDADLN--LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG--ERLYRTGDLARYRADGV 2396
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4932 LVYLGRKDSQVKLRGQRVELGEVEHHVR--ECLTEAKqlaveVIVPEGEGGyAMLAAFVqLGDDtyntlvkekaggdslt 5009
Cdd:PRK12316  2397 VEYLGRIDHQVKIRGFRIELGEIEARLQahPAVREAV-----VVAQDGASG-KQLVAYV-VPDD---------------- 2453
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5010 VQVVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREIGASFTAQQLAEmrtssqgpkrqPSTEAERTMQ 5089
Cdd:PRK12316  2454 AAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVA-----------PQEGLEQRLA 2522
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5090 QLWTRVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRT-GLQLSVADVFRHPRLVDLAYVQNSECSSAAEEVPAFSLL 5168
Cdd:PRK12316  2523 AIWQAVLKVE--QVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRV 2600
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5169 GGRAADTAQVSQdaaamcsvdassvedmypcsplqEGLMSLTAKRAGdYIMQSVLELRVDVDEDAFRAAWEHVVQLTAAL 5248
Cdd:PRK12316  2601 QPLPLSHAQQRQ-----------------------WFLWQLEPESAA-YHLPSALHLRGVLDQAALEQAFDALVLRHETL 2656
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5249 RTRIVQHSE--------LGLLQVVVEEKIQWTESKRLEEYLREDKAVSMGLGDRLARYALIKepYDGGKRWFVWTIHHAL 5320
Cdd:PRK12316  2657 RTRFVEVGEqtrqvilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLA--LDGQEHVLVITQHHIV 2734
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5321 YDGWSLPRILQAVKQIYSGAVPERQPSFNAFI-----------QYLGQQDLEAATLYWQTAL--ADCKAALFPTLPPTVT 5387
Cdd:PRK12316  2735 SDGWSMQVMVDELVQAYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLggEQPVLELPLDRPRPAL 2814
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5388 QPVADTTVEYQCPPP-------SQSATDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGVEAMVGPTIATVP 5460
Cdd:PRK12316  2815 QSHRGARLDVALDVAlsrellaLARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQV 2892
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5461 LRVCLQKDQTVSTLLECLQQQSTDMIAHEQTGL-QRIAKMSP--GARHACGFQTLLVVQPTD----DVLGSDDMLGEWRS 5533
Cdd:PRK12316  2893 LRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFeQLVEALQPerSLSHSPLFQVMYNHQSGEraaaQLPGLHIESFAWDG 2972
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5534 YSEMQDFTTYALMVQCTLAKDRVEVTASFDARVIEQwvvekMLRQFGFVMQQLAEaGAEKTVSDIETTTLEDRQQ-LWAW 5612
Cdd:PRK12316  2973 AATQFDLALDTWESAEGLGASLTYATDLFDARTVER-----LARHWQNLLRGMVE-NPQRSVDELAMLDAEERGQlLEAW 3046
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5613 NQN-VPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLA 5691
Cdd:PRK12316  3047 NATaAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLA 3126
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5692 VLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSaQHSARWIGTNHQVVTVSAGSLGQLSTlvNPVGLpAIPENAVYIM 5771
Cdd:PRK12316  3127 ILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ-SHLRLPLAQGVQVLDLDRGDENYAEA--NPAIR-TMPENLAYVI 3202
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5772 FTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCIcVPSDSDRRNDLVKAIS 5851
Cdd:PRK12316  3203 YTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV-VLAGPEDWRDPALLVE 3281
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5852 TMDVSCALLTPSVARLLE-------PSSVPTLQMLVLQGEQVSFADWNRWPASVQTINGYGPTECSICCNTYSGKQGFKS 5924
Cdd:PRK12316  3282 LINSEGVDVLHAYPSMLQafleeedAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKD 3361
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5925 GI-IGTSVASVSWVVDPENHDRlAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypgHPGrqGRLYKTGD 6003
Cdd:PRK12316  3362 AVpIGRPIANRACYILDGSLEP-VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF--------VPG--ERLYRTGD 3430
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6004 LVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQLAVEVIlpsgqkDHAMLAAFVQLEegtqnallDKE 6083
Cdd:PRK12316  3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEH-PWVREAVVLAV------DGRQLVAYVVPE--------DEA 3495
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6084 ASGEDSMAqvvflasveEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQIAnmqtssqdpkrQPST 6163
Cdd:PRK12316  3496 GDLREALK---------AHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVN 3555
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6164 EAEQTMQKLWAQVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRIGLQLSVADIFRYARLVDLAsldtsqcnsaigev 6243
Cdd:PRK12316  3556 ELERRLAAIWADVLKLE--QVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLA-------------- 3619
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6244 PAFSLLGGRAADTAQVSQDAAAMcsvdassvedmypcsPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVV 6323
Cdd:PRK12316  3620 RVARVGGGVAVDQGPVSGETLLL---------------PIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALV 3684
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6324 QLTAALRTRIVQ---HSELGLLQVVVEEKIQW---TESKRLEEYLREDKAVSMGLGD-PLARYAIIKEAWGGKRwFVWTI 6396
Cdd:PRK12316  3685 EHHDALRLRFVEdagGWTAEHLPVELGGALLWraeLDDAEELERLGEEAQRSLDLADgPLLRALLATLADGSQR-LLLVI 3763
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6397 HHALYDGWSLPRVLQAVKQAYnGAVLETQP--------SFNAFIQ----YLSQQDLEATAAYWQTALADCEATLFPPLPS 6464
Cdd:PRK12316  3764 HHLVVDGVSWRILLEDLQQAY-QQLLQGEAprlpaktsSFKAWAErlqeHARGEALKAELAYWQEQLQGVSSELPCDHPQ 3842
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6465 SVKQLVADTTVehQCPLPSRSTSDTTTST----------LIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTSID--AIV 6532
Cdd:PRK12316  3843 GALQNRHAASV--QTRLDRELTRRLLQQApaayrtqvndLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDlsRTV 3920
                         2570
                   ....*....|.
gi 1820002560 6533 GPTIATVPLRV 6543
Cdd:PRK12316  3921 GWFTSLFPVRL 3931
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
3463-3982 0e+00

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 759.00  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3463 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 3542
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3543 PDHPASRHEEIFEQTGAQVVVASaqysarwtssschvvtvskalssqlpavvdstntsvRPENAAYIIFTSGSTGVPKGV 3622
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3623 VLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFLTPS 3702
Cdd:cd05918    125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3703 VARLLDPGLIPSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPSTIGTSVASVSWVVDPENH 3782
Cdd:cd05918    205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNH 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3783 NRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAWLLEgypGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQV 3862
Cdd:cd05918    285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQ---EGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3863 KVRGQRVELGEVEHHVRECLPEARQLAVEVILPSGQKDHAMLAAFVQLEEGTQNALLDKEAGGEDSMAQVVFLASVEEEL 3942
Cdd:cd05918    362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKL 441
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 3943 AKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFT 3982
Cdd:cd05918    442 RQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
7609-8128 0e+00

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 749.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7609 VHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 7688
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7689 PDHPASRHEEIFEQTGAQVVVASaqysarwtssschvvtvskalssqlpavvdstntsvRPENAAYIIFTSGSTGVPKGV 7768
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7769 VLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFLTPS 7848
Cdd:cd05918    125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7849 VARLLDPGLIPSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPSTIGTSVASVSWVVDPENH 7928
Cdd:cd05918    205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNH 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7929 NRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAWLLEgypGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQV 8008
Cdd:cd05918    285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQ---EGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8009 KVRGQRVELGEVEHHVRECLPEARQLAVEVILPSGQKNHAMLAVFVQLGKGTHIAHLEEKAGGEDSMAQVVFLTGTEEEL 8088
Cdd:cd05918    362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKL 441
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 8089 AKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGASFT 8128
Cdd:cd05918    442 RQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
4543-5062 0e+00

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 739.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4543 VHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 4622
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4623 PDHPASRHEHIFRQTGAQVVLASaqyatlwtslgrsvvivseastsqlpvvtktadpsvNPGNAAYAIFTSGSTGIPKGV 4702
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4703 VLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLAKAINAMDVNWALLTPS 4782
Cdd:cd05918    125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4783 VARMLDPCVVQSLKILVLGGEQVNSADWDRWPKSIQTINAYGPTECSICCTTYSGKQGFKSGTIGTSIVSVSWVVDPENH 4862
Cdd:cd05918    205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNH 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4863 NRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAWLLEgygGHSGRQGRLYKTGDLVRYDADGNLVYLGRKDSQV 4942
Cdd:cd05918    285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQ---EGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4943 KLRGQRVELGEVEHHVRECLTEAKQLAVEVIVPEGEGGYAMLAAFVQLGDDTyntlvKEKAGGDSLTVQV-----VFLDR 5017
Cdd:cd05918    362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSS-----SGSGDGDSLFLEPsdefrALVAE 436
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 5018 VEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREIGASFT 5062
Cdd:cd05918    437 LRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
PRK12316 PRK12316
peptide synthase; Provisional
6257-8441 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 734.07  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6257 AQVSQDAAAMCSVDASSVEDMYPCSPLQEGLM--SLTAKRAGDYIMQsvleLRVDV---DEDAFRAAWEHVVQLTAALRT 6331
Cdd:PRK12316  1536 AGLSQAQLDALPLPAGEIADIYPLSPMQQGMLfhSLYEQEAGDYINQ----LRVDVqglDPDRFRAAWQATVDRHEILRS 1611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6332 RIVQHSELGLLQVVVEEKIQ-------WTESKRLEEYLREDKAVSMGLG-----DPLARYAIIKEawGGKRW-FVWTIHH 6398
Cdd:PRK12316  1612 GFLWQDGLEQPLQVIHKQVElpfaeldWRGREDLGQALDALAQAERQKGfdltrAPLLRLVLVRT--GEGRHhLIYTNHH 1689
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6399 ALYDGWSLPRVLQAVKQAYNG-AVLETQPSFNAFIQYLSQQDLEATAAYWQTALADCEAtlfpplPSSVKQLVA-----D 6472
Cdd:PRK12316  1690 ILMDGWSNAQLLGEVLQRYAGqPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEE------PTRLAQAARtedgqV 1763
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6473 TTVEHQCPLPSRSTSDTTT---------STLIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTSIDAIVGPTIATVPLRV 6543
Cdd:PRK12316  1764 GYGDHQQLLDPAQTRALAEfaraqkvtlNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIA 1843
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6544 RLQKDQTVSSFLGYLQQQATEMIAYEQTGLQQIAKMGPDPQHACgFQTLLVVQ--PAGDVLGSDDTLGKWRGYSGLQDFM 6621
Cdd:PRK12316  1844 APRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEAL-FDSLLVFEnyPVAEALKQGAPAGLVFGRVSNHEQT 1922
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6622 TYALGVRCTLsAEGVKITASFDARVIEHWVVEKMLGQFSFAMQQLAEaSADRKVADIDITTTTDRQQLWA-WN-AELPLA 6699
Cdd:PRK12316  1923 NYPLTLAVTL-GETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAE-DAQAALGELALLDAGERQRILAdWDrTPEAYP 2000
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6700 VDRCVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAF 6779
Cdd:PRK12316  2001 RGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY 2080
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6780 VPLDPDHPASRHEDILRQTGAQVIL---------------------------ASAQNTTLFQSSNQTVVTV--------- 6823
Cdd:PRK12316  2081 VPLDPNYPAERLAYMLEDSGAALLLtqrhllerlplpagvarlpldrdaewaDYPDTAPAVQLAGENLAYViytsgstgl 2160
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6824 --------------------------------------------------NRSSYILFPDENREAY-------------- 6839
Cdd:PRK12316  2161 pkgvavshgalvahcqaageryelspadcelqfmsfsfdgaheqwfhpllNGARVLIRDDELWDPEqlydemerhgvtil 2240
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6840 --------------------PFVR------------------------------------------------PSNAALAP 6851
Cdd:PRK12316  2241 dfppvylqqlaehaerdgrpPAVRvycfggeavpaaslrlawealrpvylfngygpteavvtpllwkcrpqdPCGAAYVP 2320
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6852 LGS---------------------IGELLVEGPILARGYLNDADKTAAAFVNDPAwlveghgKHPGrrGRLYKTGDLVYY 6910
Cdd:PRK12316  2321 IGRalgnrrayildadlnllapgmAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG--ERLYRTGDLARY 2391
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6911 NKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAGAaeqakTMVVAFLqlndeardallggnVP 6990
Cdd:PRK12316  2392 RADGVVEYLGRIDHQVKIRGFRIELGEIEARLQA-HPAVREAVVVAQDGASG-----KQLVAYV--------------VP 2451
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6991 NDdnlsAQVVFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREIGASFTAQQLAemrtssqgpkrQPSTE 7070
Cdd:PRK12316  2452 DD----AAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYV-----------APQEG 2516
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7071 AERTMQQLWARMLKVkaDSIGLDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADVFRHPRLVDLAYVQNSQCSSAAeev 7149
Cdd:PRK12316  2517 LEQRLAAIWQAVLKV--EQVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTSRA--- 2591
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7150 pafsllgEDVNPVQLSQDAAAMCSvaasivkdiypcSPLQEGLISLTAKRAGdYIMQSVLELRADVDEDVFCAAWEHVVQ 7229
Cdd:PRK12316  2592 -------PVLQKVTRVQPLPLSHA------------QQRQWFLWQLEPESAA-YHLPSALHLRGVLDQAALEQAFDALVL 2651
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7230 STAALRTRIVQHSE--------LGLLQVVVEEKIQWTESEALEEYLKEDKAVSMGLGDPLAHYALVKEAwGGKRWFVWTI 7301
Cdd:PRK12316  2652 RHETLRTRFVEVGEqtrqvilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALD-GQEHVLVITQ 2730
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7302 HHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAFI-----------QYLGQQDLEATAAYWQTALSDCEAVLFPPL--P 7368
Cdd:PRK12316  2731 HHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLGGEQPVLELPLdrP 2810
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7369 STVTQPVADTTVEYQCP-PLSKATLD------TTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPiaGVEAMVGPTI 7441
Cdd:PRK12316  2811 RPALQSHRGARLDVALDvALSRELLAlarregVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFV 2888
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7442 ATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIAKLGSGPR---HACGFQTLLVVQPVDDVLGSDDMLgEWRS 7518
Cdd:PRK12316  2889 NTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERslsHSPLFQVMYNHQSGERAAAQLPGL-HIES 2967
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7519 YSKMQDFTTYALMVQFTLAAEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLAEASEDSKVADIDTTTPEDRQQLWAWN 7598
Cdd:PRK12316  2968 FAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWN 3047
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7599 A-DVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAV 7677
Cdd:PRK12316  3048 AtAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAI 3127
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7678 LKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARwtssscHVVTVSKALSSQLPAVVDSTNTSVR--PENAAYI 7755
Cdd:PRK12316  3128 LKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLP------LAQGVQVLDLDRGDENYAEANPAIRtmPENLAYV 3201
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7756 IFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICV--PSDSDRRNSLAK 7833
Cdd:PRK12316  3202 IYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLagPEDWRDPALLVE 3281
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7834 AISTMDVNWAFLTPSVARLL----DPGLIPSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEP 7909
Cdd:PRK12316  3282 LINSEGVDVLHAYPSMLQAFleeeDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKD 3361
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7910 ST-IGTSVASVSWVVDPENHNRlAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypgHPGrqGRLYKTGD 7988
Cdd:PRK12316  3362 AVpIGRPIANRACYILDGSLEP-VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF--------VPG--ERLYRTGD 3430
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7989 LVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVevilpsgqknhamLAVFVQLGKGTHIAHLEEK 8068
Cdd:PRK12316  3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEH-PWVREAVV-------------LAVDGRQLVAYVVPEDEAG 3496
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8069 AGGEDSMAQvvfltgteeeLAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGASFTAQQLAetqtssqgpkrQPLT 8148
Cdd:PRK12316  3497 DLREALKAH----------LKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVN 3555
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8149 EAEQTMQQLWARVLGIDAdiIGLDDSFFRLGGDSIAAMKLVGEARRTGLQLSVADIFRHPRLIDLASLKSTFCNSVVEEV 8228
Cdd:PRK12316  3556 ELERRLAAIWADVLKLEQ--VGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQG 3633
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8229 PafsllspvmkdamfsvtepfgpslriddITDVVPASYIQQFYIATGVRAPREAFNYPFIDLSDAVDIQVLQASCSALLE 8308
Cdd:PRK12316  3634 P----------------------------VSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVE 3685
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8309 HFPILRTHFVYFQGkLYQVIPRHQDLPFSIF--------EVNGALAEESQaihiRDLD-QTSPLglpTSFTLVRNASGMN 8379
Cdd:PRK12316  3686 HHDALRLRFVEDAG-GWTAEHLPVELGGALLwraelddaEELERLGEEAQ----RSLDlADGPL---LRALLATLADGSQ 3757
                         2410      2420      2430      2440      2450      2460      2470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 8380 RLIIRLSHAQYDGVCMPVIWASLASIYQQ-----EPLL--STTGFHSYLAYVHNQRS-----ASINYWSRLLKG 8441
Cdd:PRK12316  3758 RLLLVIHHLVVDGVSWRILLEDLQQAYQQllqgeAPRLpaKTSSFKAWAERLQEHARgealkAELAYWQEQLQG 3831
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1510-2750 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 618.02  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1510 SPLQEGLMSLTAKRAGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQVVIEENIQWTEPKSLEE 1589
Cdd:COG1020     34 LLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEA 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1590 YLSEDKAVSVGLGDPLARYAFVKEACGGKRWFVWTIHHAVYDGWSLPLILHAVKQVY-----------SGGVLQWQPSFN 1658
Cdd:COG1020    114 AAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYlaayagaplplPPLPIQYADYAL 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1659 AFIQYLGQQDLEATVAYWQTALADCEAVL-FPTLPPTVT-QPVADATVEYQCPP-LSKA------TSDTTTSTLIRAAWA 1729
Cdd:COG1020    194 WQREWLQGEELARQLAYWRQQLAGLPPLLeLPTDRPRPAvQSYRGARVSFRLPAeLTAAlralarRHGVTLFMVLLAAFA 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1730 IVTSRYTTSDDVVFGTTVTGRNTPvtGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAHEQTG---LQRIA 1806
Cdd:COG1020    274 LLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPferLVEEL 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1807 KMGQGPQHACSFQTLLVVQPVDDVLDNTLG-EWRDHSELQEFTTYTLMLQCMLAAEGVQITASFDTRVIEKWVVEKMLRQ 1885
Cdd:COG1020    352 QPERDLSRNPLFQVMFVLQNAPADELELPGlTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGH 431
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1886 FSFIMQQLAeAGAEKTVSDIETTTPEDRQQLWA-WNQ-EVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDAL 1963
Cdd:COG1020    432 LVTLLEALA-ADPDQPLGDLPLLTAAERQQLLAeWNAtAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNAR 510
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1964 SSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSAQHSARWIGT 2043
Cdd:COG1020    511 ANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPEL 590
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2044 NHQVVTVSAGSLEQFSTLvNPVdLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLRALQFTAYT 2123
Cdd:COG1020    591 GVPVLALDALALAAEPAT-NPP-VPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLS 668
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2124 FDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSSVARLL---DPCLVPSLKVLVLGGEQVNSTDW 2198
Cdd:COG1020    669 FDASVWEIFGALLSGATLVLAPPEARRDpaALAELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELV 748
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2199 GKW---PSSVQTINGYGPTECCVFCTGYTgIQGFQSGN----IGTSIASVS-WVVDPenHGRLAPLGSIGELLVEGPILA 2270
Cdd:COG1020    749 RRWrarLPGARLVNLYGPTETTVDSTYYE-VTPPDADGgsvpIGRPIANTRvYVLDA--HLQPVPVGVPGELYIGGAGLA 825
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2271 RGYLNDVDKTQAAFIDDPAwlleGYPGhegrqGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKCl 2350
Cdd:COG1020    826 RGYLNRPELTAERFVADPF----GFPG-----ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQH- 895
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2351 PEANQlAVeVVPPSGERDHAMLAAFIRLDDETRNSPLIIKYAednstaqivfltgieeeLSERLPQHMVPTVFFALVHFP 2430
Cdd:COG1020    896 PGVRE-AV-VVAREDAPGDKRLVAYVVPEAGAAAAAALLRLA-----------------LALLLPPYMVPAAVVLLLPLP 956
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2431 TTTSGKTDRKRLREIGASFTAQqlaemrtssegpkRQPSTEAERTMQQLWAQVLGIELESIGLDDSFFRLGGDSITAMQI 2510
Cdd:COG1020    957 LTGNGKLDRLALPAPAAAAAAA-------------AAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLAL 1023
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2511 SSSARALHLSVSTGDILKKKTIALIAREILPSTSTFSRSVWRDPVNNAFDLTPIQHLYLTLDPSGRSSFDQCFF---LEL 2587
Cdd:COG1020   1024 ARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLAlllLLL 1103
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2588 RNRVQPQLLVTALTALVQRHSMLRARFQRQTGGRWQQYISEHDSSSLIVNHIHTRDTTEIVEALRQSRGSLDIERGPVLA 2667
Cdd:COG1020   1104 LLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLA 1183
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2668 AVLCDAGERQSLFVAIHHLVVDLVSWRILLEELEDLLLGQTLPPALSTPFQAWHAAQAKYIEEHVPPSAVAQVELDPDQL 2747
Cdd:COG1020   1184 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALA 1263

                   ...
gi 1820002560 2748 SYW 2750
Cdd:COG1020   1264 LAL 1266
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
7199-8439 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 601.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7199 RAGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVVVEEKIQWTESEALEEYLKEDKA----VS 7274
Cdd:COG1020     47 LLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALapfdLL 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7275 MGLGDPLAHYALVKEAWGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAFIQY-------LGQQDLEA 7347
Cdd:COG1020    127 RGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYalwqrewLQGEELAR 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7348 TAAYWQTALSDCEAVLFPPL--PSTVTQPVADTTVEYQCPP-LSKA------TLDTTTSTLIRAAWAIVTSCYTSSDDVV 7418
Cdd:COG1020    207 QLAYWRQQLAGLPPLLELPTdrPRPAVQSYRGARVSFRLPAeLTAAlralarRHGVTLFMVLLAAFALLLARYSGQDDVV 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7419 YGTTVTGRNAPiaGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTG---LQHIAKLGSGPRHACGFQ 7495
Cdd:COG1020    287 VGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPferLVEELQPERDLSRNPLFQ 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7496 TLLVVQ--PVDDVlgsdDMLG-EWRSYSKMQDFTTYALMVQFTLAAEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLA 7572
Cdd:COG1020    365 VMFVLQnaPADEL----ELPGlTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALA 440
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7573 eASEDSKVADIDTTTPEDRQQLWA-WNA-DVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLV 7650
Cdd:COG1020    441 -ADPDQPLGDLPLLTAAERQQLLAeWNAtAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLR 519
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7651 QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSK 7730
Cdd:COG1020    520 ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDA 599
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7731 ALSSQLPAvvDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEII 7810
Cdd:COG1020    600 LALAAEPA--TNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIF 677
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7811 TTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL---DPGLIPSLKILAIGGEQSSSADWNRW---PGS 7882
Cdd:COG1020    678 GALLSGATLVLAPPEARRDpaALAELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELVRRWrarLPG 757
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7883 VQKIHVYGPTECCIFCTGYTTKQGF---EPSTIGTSVASVS-WVVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKT 7958
Cdd:COG1020    758 ARLVNLYGPTETTVDSTYYEVTPPDadgGSVPIGRPIANTRvYVLDA--HLQPVPVGVPGELYIGGAGLARGYLNRPELT 835
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7959 EAAFIDDPAwlleGYPGhpgrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQlAVeV 8038
Cdd:COG1020    836 AERFVADPF----GFPG-----ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQH-PGVRE-AV-V 903
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8039 ILPSGQKNHAMLAVFVQLGKGTHIAHLEEkaggedsmaqvvfltgtEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRK 8118
Cdd:COG1020    904 VAREDAPGDKRLVAYVVPEAGAAAAAALL-----------------RLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8119 RLREIGAsftaqqlaetqtssQGPKRQPLTEAEQTMQQLWARVLGIDADIIGLDDSFFRLGGDSIAAMKLVGEARRTGLQ 8198
Cdd:COG1020    967 ALPAPAA--------------AAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLL 1032
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8199 LSVADIFRHPRLIDLASLKSTFCNSVVEEVPAfsllspvmkdamfsvtepfgpsLRIDDITDVVPASYIQQFYIATGVRA 8278
Cdd:COG1020   1033 LLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLA----------------------AAAAPLPLPPLLLSLLALLLALLLLL 1090
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8279 PREAFNYPFIDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIPRHQDLPFSIFEVNGAL----AEESQAIHI 8354
Cdd:COG1020   1091 ALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLlaaaAAAAELLAA 1170
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8355 RDLDQTSPLGLPTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQEPLLSTTGFHSYLAYVHNQRSASINY 8434
Cdd:COG1020   1171 AALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALA 1250

                   ....*
gi 1820002560 8435 WSRLL 8439
Cdd:COG1020   1251 ALAAL 1255
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
5201-6503 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 597.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5201 PLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEEKIQWTE------- 5273
Cdd:COG1020     28 WLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLvdleala 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5274 ----SKRLEEYLREDKAVSMGLGDRLARYALIKEPYDGGKRWFVWtIHHALYDGWSLPRILQAVKQIYSGAVPERQPSFN 5349
Cdd:COG1020    108 eaaaEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHI-ISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPI 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5350 AFIQY-------LGQQDLEAATLYWQTALADCKAAL-FPTLPPTVTQPVADTTVEYQCPPPSQSA--------TDITTST 5413
Cdd:COG1020    187 QYADYalwqrewLQGEELARQLAYWRQQLAGLPPLLeLPTDRPRPAVQSYRGARVSFRLPAELTAalralarrHGVTLFM 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5414 LVRAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAHEQTG- 5492
Cdd:COG1020    267 VLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPf 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5493 --LQRIAKMSPGARHACGFQTLLVVQPTDDvlGSDDMLG-EWRSYSEMQDFTTYALMVQCTLAKDRVEVTASFDARVIEQ 5569
Cdd:COG1020    345 erLVEELQPERDLSRNPLFQVMFVLQNAPA--DELELPGlTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDA 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5570 WVVEKMLRQFGFVMQQLAeAGAEKTVSDIETTTLEDRQQLWA-WNQN-VPPAIERCVHDLFTEQAKARPHAPAICAWDGE 5647
Cdd:COG1020    423 ATIERMAGHLVTLLEALA-ADPDQPLGDLPLLTAAERQQLLAeWNATaAPYPADATLHELFEAQAARTPDAVAVVFGDQS 501
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSA 5727
Cdd:COG1020    502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQS 581
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5728 QHSARWIGTNHQVVTVSAGSLGQLSTLvNPVgLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLS 5807
Cdd:COG1020    582 ALAARLPELGVPVLALDALALAAEPAT-NPP-VPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGD 659
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5808 RVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRN--DLVKAISTMDVSCALLTPSVARLL---EPSSVPTLQMLVLQ 5882
Cdd:COG1020    660 RVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDpaALAELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVG 739
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5883 GEQVSFADWNRW---PASVQTINGYGPTECSICCNTY--SGKQGFKSGI-IGTSVASVS-WVVDPenHDRLAPLGSIGEL 5955
Cdd:COG1020    740 GEALPPELVRRWrarLPGARLVNLYGPTETTVDSTYYevTPPDADGGSVpIGRPIANTRvYVLDA--HLQPVPVGVPGEL 817
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5956 LVEGPILARGYLNDIQKTAAVFIDDPAwlleGYPGhpgrqGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEV 6035
Cdd:COG1020    818 YIGGAGLARGYLNRPELTAERFVADPF----GFPG-----ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEI 888
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6036 EHHVREClPEARQlAVeVILPSGQKDHAMLAAFVQLEEGTQNAlldkeasgedsmaqvvfLASVEEELAKRLPEHMVPTV 6115
Cdd:COG1020    889 EAALLQH-PGVRE-AV-VVAREDAPGDKRLVAYVVPEAGAAAA-----------------AALLRLALALLLPPYMVPAA 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6116 FFSLLHFPTTTSGKTDRKRLREIGAsftaqqianmqtssQDPKRQPSTEAEQTMQKLWAQVLGIELNGIGLDDSFFRLGG 6195
Cdd:COG1020    949 VVLLLPLPLTGNGKLDRLALPAPAA--------------AAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGG 1014
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6196 DSIAAMKLVGEARRIGLQLSVADIFRYARLVDLASLDTSQCNSAIGEVPAfslLGGRAADTAQVSQDAAAMCSVDASSVE 6275
Cdd:COG1020   1015 LGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLA---AAAAPLPLPPLLLSLLALLLALLLLLA 1091
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6276 DMYPCSPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEEKIQWTES 6355
Cdd:COG1020   1092 LLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAA 1171
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6356 KRLEEYLREDKAVSMGLGDPLARYAIIKEAWggkRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSFNAFIQYL 6435
Cdd:COG1020   1172 ALLLLLALLLLALLLLLLLLLLLLLLLLLLL---LLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLA 1248
                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 6436 SQQDLEATAAYWQTALADCEATLFPPLPSSVKQLVADTTVEHQCPLPSRSTSDTTTSTLIRAAWAIVA 6503
Cdd:COG1020   1249 LAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLL 1316
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
7182-7574 1.88e-164

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 514.92  E-value: 1.88e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7182 IYPCSPLQEGLISLTAKRAGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVVV-EEKIQWTES 7260
Cdd:cd19545      1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVkESPISWTES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7261 EALEEYLKEDKAVSMGLGDPLAHYALVKEAwGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAFIQYL 7340
Cdd:cd19545     81 TSLDEYLEEDRAAPMGLGGPLVRLALVEDP-DTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRFVKYL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7341 GQQDLEATAAYWQTALSDCEAVLFPPLPSTVTQPVADTTVEYQCPPLSKATLDTTTSTLIRAAWAIVTSCYTSSDDVVYG 7420
Cdd:cd19545    160 RQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSASSGVTLATVLRAAWALVLSRYTGSDDVVFG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7421 TTVTGRNAPIAGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIAKLGSGPRHACGFQTLLVV 7500
Cdd:cd19545    240 VTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDARAACNFQTLLVV 319
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 7501 QPVDDVLGSDDM-LGEWRSYSKMQDFTTYALMVQFTLAAEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLAEA 7574
Cdd:cd19545    320 QPALPSSTSESLeLGIEEESEDLEDFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASA 394
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
4568-4961 4.38e-136

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 434.39  E-value: 4.38e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4568 TYGELDTLSSKLASHLVQL-GVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLASA 4646
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4647 QYATLWTSLGRSVVIVS---EASTSQLPVvTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGIT 4723
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDpleLAALDDAPA-PPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4724 DHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRR---NNLAKAINAMDVNWALLTPSVARMLDPCVVQ---SLKI 4797
Cdd:TIGR01733  160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERddaALLAALIAEHPVTVLNLTPSLLALLAAALPPalaSLRL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4798 LVLGGEQVNSADWDRW---PKSIQTINAYGPTECSICCTTYS----GKQGFKSGTIGTSIVSVS-WVVDPenHNRLAPLG 4869
Cdd:TIGR01733  240 VILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLvdpdDAPRESPVPIGRPLANTRlYVLDD--DLRPVPVG 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4870 SIGELLVEGPILARGYLNDMEKTEAAFIDDPAWllegygghSGRQGRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRV 4949
Cdd:TIGR01733  318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRI 389
                          410
                   ....*....|..
gi 1820002560 4950 ELGEVEHHVREC 4961
Cdd:TIGR01733  390 ELGEIEAALLRH 401
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1956-2349 3.07e-135

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 431.69  E-value: 3.07e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1956 TYGELDALSSKLASHLVQL-GVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSA 2034
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2035 QHSAR--WIGTNHQVVTVSAGSLEQFSTLVNPVDLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTN 2112
Cdd:TIGR01733   81 ALASRlaGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2113 LLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD---NLAKAITDMQVNWGYLTSSVARLLDPCLVP---SLKVL 2186
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDdaaLLAALIAEHPVTVLNLTPSLLALLAAALPPalaSLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2187 VLGGEQVNSTDWGKW---PSSVQTINGYGPTECCVFCTGYT----GIQGFQSGNIGTSIASVS-WVVDPenHGRLAPLGS 2258
Cdd:TIGR01733  241 ILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLvdpdDAPRESPVPIGRPLANTRlYVLDD--DLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2259 IGELLVEGPILARGYLNDVDKTQAAFIDDPAWLlegypgheGRQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVE 2338
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAG--------GDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIE 390
                          410
                   ....*....|.
gi 1820002560 2339 LGEVEHHMRKC 2349
Cdd:TIGR01733  391 LGEIEAALLRH 401
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
7634-8036 3.81e-134

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 428.61  E-value: 3.81e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7634 TYGELDVLSSNLAGHLVQL-GVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASA 7712
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7713 QYSAR--WTSSSCHVVTVSKALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITN 7790
Cdd:TIGR01733   81 ALASRlaGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7791 LSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRR---NSLAKAISTMDVNWAFLTPSVARLLDPGLIP---SLKIL 7864
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERddaALLAALIAEHPVTVLNLTPSLLALLAAALPPalaSLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7865 AIGGEQSSSADWNRW---PGSVQKIHVYGPTECCIFCTGYTT----KQGFEPSTIGTSVASVS-WVVDPenHNRLAPLGS 7936
Cdd:TIGR01733  241 ILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLVdpddAPRESPVPIGRPLANTRlYVLDD--DLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7937 MGELLMEGPILARGYLNDVDKTEAAFIDDPAWllegypghPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVE 8016
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIE 390
                          410       420
                   ....*....|....*....|
gi 1820002560 8017 LGEVEHHVREClPEARQLAV 8036
Cdd:TIGR01733  391 LGEIEAALLRH-PGVREAVV 409
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1-291 7.41e-127

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 410.78  E-value: 7.41e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    1 MRVNWALLTPSVARLLEPSHIPSLRILVMGGEQVNSADWDRWPSSVQTINGYGPTECCIVCTGYTSEQDFTTGTIGTSIA 80
Cdd:cd05918    194 LRVTWAFLTPSVARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLG 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   81 SVSWVVDPKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAWLLEGHGgyaGRQGRLYKTGDLVRYDADGN 160
Cdd:cd05918    274 ATCWVVDPDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQEGS---GRGRRLYRTGDLVRYNPDGS 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  161 LVCLGRKDSQVKLRGQRVELGEVEHHVRECLPEAKQLAVEVVLPLGQKNHATLAAFIQLDKGTHNALLKEKVGGDDSIAR 240
Cdd:cd05918    351 LEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEF 430
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  241 VVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASFT 291
Cdd:cd05918    431 RALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
AMP-binding pfam00501
AMP-binding enzyme;
4547-4945 3.92e-85

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 288.06  E-value: 3.92e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQARARPDTPAICAWDGE-LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 4625
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4626 PASRHEHIFRQTGAQVVLASAQ----------------YATLWTSLGRSVVIVSEASTSQLPVVTKTADPSVNPGNAAYA 4689
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDAlkleellealgklevvKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4690 IFTSGSTGIPKGVVLEHKAVVTSCLGHGQ----AFGITDHTRVLQFASYTFDA-CIAEIITTLLCCGCICVPSDSDRRN- 4763
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDp 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4764 -NLAKAINAMDVNWALLTPSVARML------DPCVVQSLKILVLGGEQVNSADWDRW----PKSIqtINAYGPTECSICC 4832
Cdd:pfam00501  241 aALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFrelfGGAL--VNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4833 TT--YSGKQGFKSGTIGTSIVSVSW-VVDPEnHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpawllegygg 4909
Cdd:pfam00501  319 TTplPLDEDLRSLGSVGRPLPGTEVkIVDDE-TGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED---------- 387
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1820002560 4910 hsgrqgRLYKTGDLVRYDADGNLVYLGRKDSQVKLR 4945
Cdd:pfam00501  388 ------GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
1935-2333 5.35e-84

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 284.59  E-value: 5.35e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1935 FTEQAKARPHAPAICAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 2013
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2014 PASRHEDIFRQTGAQVVVTSAQHSARWIGTNHQ-------VVTVSAGSLEQFSTL---------VNPVDLPAKPENAAYV 2077
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEALGklevvklVLVLDRDPVLKEEPLpeeakpadvPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2078 MFTSGSTGTPKGVVLEHRAVVTSCLGHGQ----AFGVTNLLRALQFTAYTFDV-CIAEIITTLVHGGCICVPSDSERRD- 2151
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDp 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2152 -NLAKAITDMQVNWGYLTSSVARLL------DPCLVPSLKVLVLGGEQVNSTDWGKW----PSSVqtINGYGPTECCVFC 2220
Cdd:pfam00501  241 aALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFrelfGGAL--VNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2221 TGYTGIQGFQS--GNIGTSIASVSW-VVDPEnHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpawllegypg 2297
Cdd:pfam00501  319 TTPLPLDEDLRslGSVGRPLPGTEVkIVDDE-TGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED---------- 387
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1820002560 2298 hegrqgRLYKTGDLVRYSSDGNLVCLGRKDSQVKVR 2333
Cdd:pfam00501  388 ------GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
7613-8011 1.17e-82

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 280.74  E-value: 1.17e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7613 FAEQARARPGAPAICAWDGE-LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 7691
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7692 PASRHEEIFEQTGAQVVVASAQY---------SARWTSSSCHVVTVSKALSSQL-------PAVVDSTNTSVRPENAAYI 7755
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleellealGKLEVVKLVLVLDRDPVLKEEPlpeeakpADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7756 IFTSGSTGVPKGVVLEHRAVATSCLGHG----RAFGITNLSRVLQFASYTFDA-CIAEIITTLLCGGCICVPSDSDRRN- 7829
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDp 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7830 -SLAKAISTMDVNWAFLTPSVARLL------DPGLIPSLKILAIGGEQSSSADWNRW----PGSVqkIHVYGPTECCIFC 7898
Cdd:pfam00501  241 aALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFrelfGGAL--VNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7899 TGYTTKQGFE--PSTIGTSVASVSW-VVDPEnHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllegypg 7975
Cdd:pfam00501  319 TTPLPLDEDLrsLGSVGRPLPGTEVkIVDDE-TGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED---------- 387
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1820002560 7976 hpgrqgRLYKTGDLVQYNADGNLVYLGRKDSQVKVR 8011
Cdd:pfam00501  388 ------GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
8261-8636 1.88e-79

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 270.72  E-value: 1.88e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8261 VVPASYIQQFYIATGVRAPREAFNYPFIDLSDAVDIQVLQASCSALLEHFPILRTHFV--YFQGKLYQVIPRHQDLPFSI 8338
Cdd:cd19542      1 IYPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVesSAEGTFLQVVLKSLDPPIEE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8339 FEVNgalaEESQAIHIRDLDQ--TSPLGLPTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQEPLLSTTG 8416
Cdd:cd19542     81 VETD----EDSLDALTRDLLDdpTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8417 FHSYLAYVHNQ-RSASINYWSRLLKGSHITNITSkLRPKLGKDTTIRSV-----KVERVIRTPqlptGLTMASLVSSAWA 8490
Cdd:cd19542    157 FSDYISYLQSQsQEESLQYWRKYLQGASPCAFPS-LSPKRPAERSLSSTrrslaKLEAFCASL----GVTLASLFQAAWA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8491 VVLSHISGEEDVVYGLVVAGRNSDLPSITEV-------------------------SVQDQYISLGESDSIGLDDIVQHC 8545
Cdd:cd19542    232 LVLARYTGSRDVVFGYVVSGRDLPVPGIDDIvgpcintlpvrvkldpdwtvldllrQLQQQYLRSLPHQHLSLREIQRAL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8546 TDWPAKSEFDSIIQHQNIEEQPEIQFAGET-TKLQWFKNSFAVSRQLFVFSHprGNSLTITITGNTGILTDQCAEKLLVM 8624
Cdd:cd19542    312 GLWPSGTLFNTLVSYQNFEASPESELSGSSvFELSAAEDPTEYPVAVEVEPS--GDSLKVSLAYSTSVLSEEQAEELLEQ 389
                          410
                   ....*....|..
gi 1820002560 8625 LCDTISQLSDSL 8636
Cdd:cd19542    390 FDDILEALLANP 401
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
7609-8122 6.33e-79

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 271.30  E-value: 6.33e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7609 VHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 7688
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7689 PDHPASRHEEIFEQTGAQVVVAsaqysarwtssschvvtvskalssqlpavvdstntsvrpenaAYIIFTSGSTGVPKGV 7768
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7769 VLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFD-ACIAEIITTLLCGGCICVPSDSDRRnSLAKAISTMDVNWAFLTP 7847
Cdd:COG0318    119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPRFDPE-RVLELIERERVTVLFGVP 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7848 SVARLL------DPGLIPSLKILAIGGEQSSSADWNRWpgsVQK-----IHVYGPTECCIFCTGYTTKQGFE-PSTIGTS 7915
Cdd:COG0318    198 TMLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERF---EERfgvriVEGYGLTETSPVVTVNPEDPGERrPGSVGRP 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7916 VASVS-WVVDPEnhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLlegypghpgrqgrlyKTGDLVQYNA 7994
Cdd:COG0318    275 LPGVEvRIVDED--GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG--WL---------------RTGDLGRLDE 335
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7995 DGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKNHAMLAvFVQLgkgthiahleeKAGGEDS 8074
Cdd:COG0318    336 DGYLYIVGRKKDMIISGGENVYPAEVEEVLAAH-PGVAEAAV-VGVPDEKWGERVVA-FVVL-----------RPGAELD 401
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 8075 MAQVVfltgteEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:COG0318    402 AEELR------AFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1-199 1.03e-63

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 225.61  E-value: 1.03e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    1 MRVNWALLTPSVARLLEPSHIP---SLRILVMGGEQVNSADWDRW---PSSVQTINGYGPTECCIVCTGYTSEQDFTTGT 74
Cdd:TIGR01733  211 HPVTVLNLTPSLLALLAAALPPalaSLRLVILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLVDPDDAPRE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   75 ----IGTSIASVS-WVVDPkdHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAWlleghggyAGRQGRLYKT 149
Cdd:TIGR01733  291 spvpIGRPLANTRlYVLDD--DLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRT 360
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560  150 GDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAV 199
Cdd:TIGR01733  361 GDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRH-PGVREAVV 409
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
7617-8120 6.86e-60

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 217.46  E-value: 6.86e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 7696
Cdd:PRK04813    12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7697 EEIFEQTGAQVVVASAQYSArwTSSSCHVVTVSKALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVA 7776
Cdd:PRK04813    92 EMIIEVAKPSLIIATEELPL--EILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7777 TSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGC-ICVPSD-SDRRNSLAKAISTMDVN-WAFlTPSVAR-- 7851
Cdd:PRK04813   170 SFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTlVALPKDmTANFKQLFETLPQLPINvWVS-TPSFADmc 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7852 LLDPGL----IPSLKILAIGGE----QSSSADWNRWPGSVqKIHVYGPTECCIFCTGY-TTKQ---GFEPSTIGTSVASV 7919
Cdd:PRK04813   249 LLDPSFneehLPNLTHFLFCGEelphKTAKKLLERFPSAT-IYNTYGPTEATVAVTSIeITDEmldQYKRLPIGYAKPDS 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7920 SWVVDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllEGYPGhpgrqgrlYKTGDLVqYNADGNLV 7999
Cdd:PRK04813   328 PLLIIDEEGTKL-PDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF-----DGQPA--------YHTGDAG-YLEDGLLF 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8000 YLGRKDSQVKVRGQRVELGEVEHHVREClpeaRQLAVEVILPSgQKNHAMlavfVQLgkgthIAHLEEKAGGEDSMAQvv 8079
Cdd:PRK04813   393 YQGRIDFQIKLNGYRIELEEIEQNLRQS----SYVESAVVVPY-NKDHKV----QYL-----IAYVVPKEEDFEREFE-- 456
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 8080 fLTGT-EEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:PRK04813   457 -LTKAiKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
PRK12316 PRK12316
peptide synthase; Provisional
2-379 9.15e-55

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 215.98  E-value: 9.15e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL-----EPSHIPSLRILVMGGEQVNSADWDRWPSS---VQTINGYGPTECCIVCTGYTSEQDFTTG 73
Cdd:PRK12316  4784 RVTVLVFPPVYLQQLaehaeRDGEPPSLRVYCFGGEAVAQASYDLAWRAlkpVYLFNGYGPTETTVTVLLWKARDGDACG 4863
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   74 T----IGTSIASVS-WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawlLEGHGGyagrqgRLYK 148
Cdd:PRK12316  4864 AaympIGTPLGNRSgYVLD--GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDP---FGAPGG------RLYR 4932
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  149 TGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVRE--CLPEAKQLAVEVvlPLGQKnhatLAAFIQLDKgthNA 226
Cdd:PRK12316  4933 TGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREhpAVREAVVIAQEG--AVGKQ----LVGYVVPQD---PA 5003
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  227 LLkekvggDDSIARVVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssqgpk 306
Cdd:PRK12316  5004 LA------DADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYV---------- 5067
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560  307 rQPSTEAERTMQQLWARVLGIEpdSIGLDDSFFRLGGDSIAAIKLVGEAR-RTGLQPSVADIFRHPTLAALASL 379
Cdd:PRK12316  5068 -APRSELEQQVAAIWAEVLQLE--RVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTLAAFVEL 5138
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
6729-6945 5.55e-54

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 197.49  E-value: 5.55e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6729 TYGELEALSTKLAGHLVQL-GVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDILRQTGAQVILASA 6807
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6808 QNTTLFQSSNQTVVTVNRS-----------------------SYILF--------------------------------- 6831
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLelaalddapappppdapsgpddlAYVIYtsgstgrpkgvvvthrslvnllawlarrygldp 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6832 -------------------------------PDEN--------------------------------------------- 6835
Cdd:TIGR01733  161 ddrvlqfaslsfdasveeifgallagatlvvPPEDeerddaallaaliaehpvtvlnltpsllallaaalppalaslrlv 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6836 ---------------REAYPFVR------PSNAA--------------------------------------LAPLGSIG 6856
Cdd:TIGR01733  241 ilggealtpalvdrwRARGPGARlinlygPTETTvwstatlvdpddaprespvpigrplantrlyvldddlrPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6857 ELLVEGPILARGYLNDADKTAAAFVNDPAWlveghgkhPGRRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELG 6936
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELG 392

                   ....*....
gi 1820002560 6937 EIENRLREC 6945
Cdd:TIGR01733  393 EIEAALLRH 401
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
7179-7594 2.51e-42

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 164.43  E-value: 2.51e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7179 VKDIYPCSPLQEGL----ISLTAKRAgdYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVVVEEK 7254
Cdd:pfam00668    1 VQDEYPLSPAQKRMwfleKLEPHSSA--YNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7255 -IQW-----------TESEALEEYLKEDKAVSMGL-GDPLAHYALVKEAWGGKRWFvWTIHHALYDGGSLPLILHAVKQV 7321
Cdd:pfam00668   79 pFELeiidisdlsesEEEEAIEAFIQRDLQSPFDLeKGPLFRAGLFRIAENRHHLL-LSMHHIIVDGVSLGILLRDLADL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7322 YSGAVLERQ------PSFNAFI----QYLGQQDLEATAAYWQTALSDCEAVLfpPLPSTVTQPVADTTVEYQ----CPPL 7387
Cdd:pfam00668  158 YQQLLKGEPlplppkTPYKDYAewlqQYLQSEDYQKDAAYWLEQLEGELPVL--QLPKDYARPADRSFKGDRlsftLDED 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7388 SKATL-------DTTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPiaGVEAMVGPTIATVPVRLRVQRDQTVFAFL 7460
Cdd:pfam00668  236 TEELLrklakahGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTFSELI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7461 QGLQQQSTDMIAHEQTGLQHIAKLGSGPR---HACGFQTLLVVQPvddVLGSDDMLGEW-RSYSKM------QDFTTYAL 7530
Cdd:pfam00668  314 KRVQEDLLSAEPHQGYPFGDLVNDLRLPRdlsRHPLFDPMFSFQN---YLGQDSQEEEFqLSELDLsvssviEEEAKYDL 390
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 7531 MVQFTLAAEGVQITASFDARVIEhwvLEKMLRQFSFIMQQLAEASED--SKVADIDTTTPEDRQQL 7594
Cdd:pfam00668  391 SLTASERGGGLTIKIDYNTSLFD---EETIERFAEHFKELLEQAIAHpsQPLSELDLLSDAEKQKL 453
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
2-285 3.27e-41

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 161.13  E-value: 3.27e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL------EPSHIPSLRILVMGGEQVNSADWDRWPS--SVQTINGYGPTECCIVCTGYTSEQDFT-T 72
Cdd:COG0318    189 RVTVLFGVPTMLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFEErfGVRIVEGYGLTETSPVVTVNPEDPGERrP 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   73 GTIGTSIASVS-WVVDPkdHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinnpawllegHGGYagrqgrlYKTGD 151
Cdd:COG0318    269 GSVGRPLPGVEvRIVDE--DGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF----------RDGW-------LRTGD 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  152 LVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAVeVVLP---LGQknhaTLAAFIQLDKGTHnall 228
Cdd:COG0318    330 LGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAH-PGVAEAAV-VGVPdekWGE----RVVAFVVLRPGAE---- 399
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  229 kekvggddsiarvVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:COG0318    400 -------------LDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
AMP-binding pfam00501
AMP-binding enzyme;
2-174 1.24e-34

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 140.91  E-value: 1.24e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL------EPSHIPSLRILVMGGEQVNSADWDRW----PSSVqtINGYGPTECCIVCT--GYTSEQD 69
Cdd:pfam00501  251 KVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFrelfGGAL--VNGYGLTETTGVVTtpLPLDEDL 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   70 FTTGTIGTSIASVSW-VVDPkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINnpawlleghggyagrqGRLYK 148
Cdd:pfam00501  329 RSLGSVGRPLPGTEVkIVDD-ETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE----------------DGWYR 391
                          170       180
                   ....*....|....*....|....*.
gi 1820002560  149 TGDLVRYDADGNLVCLGRKDSQVKLR 174
Cdd:pfam00501  392 TGDLGRRDEDGYLEIVGRKKDQIKLG 417
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
8260-8649 1.39e-20

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 99.33  E-value: 1.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8260 DVVPASYIQQFYIATGVRAPR-EAFNYPF-IDLSDAVDIQVLQASCSALLEHFPILRTHFVY-FQGKLYQVIprHQDLPF 8336
Cdd:pfam00668    3 DEYPLSPAQKRMWFLEKLEPHsSAYNMPAvLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVI--LEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8337 SIFEVNGALAEESQAIHIRDL----DQTSPLGLPTS----FTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQ 8408
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAfiqrDLQSPFDLEKGplfrAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8409 E------PLLSTTGFHSY-------LAYVHNQRSASinYWSRLLKGSHITNITSKLRPKLGKDT--------TIRSVKVE 8467
Cdd:pfam00668  161 LlkgeplPLPPKTPYKDYaewlqqyLQSEDYQKDAA--YWLEQLEGELPVLQLPKDYARPADRSfkgdrlsfTLDEDTEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8468 RVIRTPQLpTGLTMASLVSSAWAVVLSHISGEEDVVYGLVVAGRNSD------------LPSITEVS-----------VQ 8524
Cdd:pfam00668  239 LLRKLAKA-HGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPdiermvgmfvntLPLRIDPKggktfselikrVQ 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8525 DQYISLGESDSIGLDDIVQHCTDWPAKSE---FDSIIQHQNIEEQPEI----QFAGETTKLQWFKN---SFAVSRQLFvf 8594
Cdd:pfam00668  318 EDLLSAEPHQGYPFGDLVNDLRLPRDLSRhplFDPMFSFQNYLGQDSQeeefQLSELDLSVSSVIEeeaKYDLSLTAS-- 395
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 8595 shPRGNSLTITITGNTGILTDQCAEKLLVMLCDTISQLSDSLDTPLAACKLLLPT 8649
Cdd:pfam00668  396 --ERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDA 448
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
315-375 1.48e-14

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 71.83  E-value: 1.48e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560  315 RTMQQLWARVLGIEPDSIGLDDSFFRLGGDSIAAIKLVGEARRT-GLQPSVADIFRHPTLAA 375
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
309-377 1.62e-13

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 69.50  E-value: 1.62e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  309 PSTEAERTMQQLWARVLGIEPDSIGLDDSFFR-LGGDSIAAIKLVGEAR-RTGLQPSVADIFRHPTLAALA 377
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEeEFGIELPDTELFEYPTVADLA 72
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
309-377 9.03e-11

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 61.88  E-value: 9.03e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560   309 PSTEAERTMQQL----WARVLGIE-PDSIGLDDSFFRLGGDSIAAIKLVGE-ARRTGLQPSVADIFRHPTLAALA 377
Cdd:smart00823    5 PPAERRRLLLDLvreqVAAVLGHAaAEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALA 79
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
8142-8214 7.35e-10

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 59.19  E-value: 7.35e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  8142 PKRQPLTEAEQTMQQLWARVLGI-DADIIGLDDSFFRLGGDSIAAMKLVGE-ARRTGLQLSVADIFRHPRLIDLA 8214
Cdd:smart00823    5 PPAERRRLLLDLVREQVAAVLGHaAAEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALA 79
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
8251-8648 1.50e-09

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 65.65  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8251 PSLRIDDITDVVPASYIQQFYIATGVRAPREAFNYPFIDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIPR 8330
Cdd:COG1020      9 LPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8331 HQDLPFSI------FEVNGALAEESQAIHIRDLDQTSPLGLPTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLAS 8404
Cdd:COG1020     89 VVAAPLPVvvllvdLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLR 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8405 IYQQEPLLSTTG----FHSYLAYVHNQR--------SASINYWSRLLKGSHitniTSKLRPKLGKDTTIRSVKVERVIRT 8472
Cdd:COG1020    169 LYLAAYAGAPLPlpplPIQYADYALWQRewlqgeelARQLAYWRQQLAGLP----PLLELPTDRPRPAVQSYRGARVSFR 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8473 pqLP-------------TGLTMASLVSSAWAVVLSHISGEEDVVYGLVVAGRN---------------------SDLPSI 8518
Cdd:COG1020    245 --LPaeltaalralarrHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPrpeleglvgffvntlplrvdlSGDPSF 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8519 TEV--SVQDQYISLGESDSIGLDDIVQHCTdwPAKSE-----FDSIIQHQNiEEQPEIQFAGETTKLQWFKNSFAVSrQL 8591
Cdd:COG1020    323 AELlaRVRETLLAAYAHQDLPFERLVEELQ--PERDLsrnplFQVMFVLQN-APADELELPGLTLEPLELDSGTAKF-DL 398
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 8592 FVFSHPRGNSLTITITGNTGILTDQCAEKLLVMLCDTISQLSDSLDTPLAACKLLLP 8648
Cdd:COG1020    399 TLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTA 455
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1387-1460 1.84e-08

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 55.33  E-value: 1.84e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560  1387 PKRQPSTEVEQTMQQLWAQVLSIEPNS-IGLDDSFFRLGGDSIVAMKLVGE-ARRTGLQLSVADIFRHPRLVDLAR 1460
Cdd:smart00823    5 PPAERRRLLLDLVREQVAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALAE 80
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
5080-5148 3.95e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 51.48  E-value: 3.95e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  5080 PSTEAERTMQQL----WTRVLGIE-LNGIGLDDSFFRLGGDSIAAMKLVGE-ARRTGLQLSVADVFRHPRLVDLA 5148
Cdd:smart00823    5 PPAERRRLLLDLvreqVAAVLGHAaAEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALA 79
PRK05691 PRK05691
peptide synthase; Validated
8293-8594 5.95e-04

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 47.47  E-value: 5.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8293 AVDIQVLQASCSALLEHFPILRTHFVYFQGK-LYQVIPRHQDLPFSIFEVNGaLAEESQAIHIRDLDQTSPlglPTSFTL 8371
Cdd:PRK05691  3291 ALDPERFAQAWQAVVARHEALRASFSWNAGEtMLQVIHKPGRTPIDYLDWRG-LPEDGQEQRLQALHKQER---EAGFDL 3366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8372 VRNASGMNRLIiRLSHAQY-----------DGVCMPVIWASLASIYQ------QEPLLSTTGFHSYLAYVHNQR-SASIN 8433
Cdd:PRK05691  3367 LNQPPFHLRLI-RVDEARYwfmmsnhhiliDAWCRSLLMNDFFEIYTalgegrEAQLPVPPRYRDYIGWLQRQDlAQARQ 3445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8434 YWSRLLKGSHITNITSKLRPKL------------GKDTTIRSVKVERVIRTPQLPTGLTMASLVSSAWAVVLSHISGEED 8501
Cdd:PRK05691  3446 WWQDNLRGFERPTPIPSDRPFLrehagdsggmvvGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRD 3525
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8502 VVYGLVVAGRNSDLPSITE-VSVQDQYISLgesdSIGLDDIVQHCT--DWpAKSEFDSIIQHQNIEEQP--EIQFAGETT 8576
Cdd:PRK05691  3526 VLFGVTVAGRPVSMPQMQRtVGLFINSIAL----RVQLPAAGQRCSvrQW-LQGLLDSNMELREYEYLPlvAIQECSELP 3600
                          330
                   ....*....|....*...
gi 1820002560 8577 KLQWFKNSfavsrqLFVF 8594
Cdd:PRK05691  3601 KGQPLFDS------LFVF 3612
 
Name Accession Description Interval E-value
PRK12316 PRK12316
peptide synthase; Provisional
366-4096 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1459.40  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  366 DIFRHPTLAALASLETNQYNITIE---ETPPLSLLGENADVAQVRDEAAAMCSVDGSAIEDMYLCSPLQEGLM--SLTTK 440
Cdd:PRK12316  1495 EMFAEATVQRLADDYARELQALIEhccDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIADIYPLSPMQQGMLfhSLYEQ 1574
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  441 RAGDYIMQdvleLRADV---DEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQVVVEEKMQ-------WTESESLEEYLN 510
Cdd:PRK12316  1575 EAGDYINQ----LRVDVqglDPDRFRAAWQATVDRHEILRSGFLWQDGLEQPLQVIHKQVElpfaeldWRGREDLGQALD 1650
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  511 EDKAASMGLGDRLARYALIKESC---GGKRW-FVWTIHHALYDGWSLPLVLDAVKQVYSG----AALERqpsFNTFIQYV 582
Cdd:PRK12316  1651 ALAQAERQKGFDLTRAPLLRLVLvrtGEGRHhLIYTNHHILMDGWSNAQLLGEVLQRYAGqpvaAPGGR---YRDYIAWL 1727
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  583 SQQDVKAAAAYWQTALADCEAvlfpplPSTVTQPVA-----DTTVKYQCPPSPEVTSS--------NITTSTLIRAAWAI 649
Cdd:PRK12316  1728 QRQDAAASEAFWKEQLAALEE------PTRLAQAARtedgqVGYGDHQQLLDPAQTRAlaefaraqKVTLNTLVQAAWLL 1801
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  650 IASRYTSSEDIVFGTTVTGRNAPITGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTGLQRIMKMGp 729
Cdd:PRK12316  1802 LLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWA- 1880
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  730 GPQHACGFQTLLVV--HPTDDVLS----SDDTLGEWHSRSDselqyfTTYALTIQCTLAvEGVQITASFDARVVEHWVVE 803
Cdd:PRK12316  1881 GQGGEALFDSLLVFenYPVAEALKqgapAGLVFGRVSNHEQ------TNYPLTLAVTLG-ETLSLQYSYDRGHFDAAAIE 1953
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  804 KMLGQFSFVMQQLAE----AGVEKKVADIEtttlEDRQQLWVWNADMPPA-VDRCIHDLFAEQARARPDASAVCAWDGEL 878
Cdd:PRK12316  1954 RLDRHLLHLLEQMAEdaqaALGELALLDAG----ERQRILADWDRTPEAYpRGPGVHQRIAEQAARAPEAIAVVFGDQHL 2029
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  879 TYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSQ 958
Cdd:PRK12316  2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRH 2109
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  959 hamlfaSSERHQVTVSKVSTSqLPTVVNFAKSP-------VDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAF 1031
Cdd:PRK12316  2110 ------LLERLPLPAGVARLP-LDRDAEWADYPdtapavqLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY 2182
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1032 GYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRR-NNLAKAISTMDVNCALLTPSVARLLEPSA-----VPS 1105
Cdd:PRK12316  2183 ELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDpEQLYDEMERHGVTILDFPPVYLQQLAEHAerdgrPPA 2262
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1106 LKRLVLQGEQVSFADWNRWPGSVQT---INGYGPTECSV------CCNTYSGkqGFKSGIIGTSVASLS-WVVDAGNHnr 1175
Cdd:PRK12316  2263 VRVYCFGGEAVPAASLRLAWEALRPvylFNGYGPTEAVVtpllwkCRPQDPC--GAAYVPIGRALGNRRaYILDADLN-- 2338
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1176 LAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAwllegyeGHAGrrGRLYKTGDLVRCDADGNLVCLGRKDSQVKV 1255
Cdd:PRK12316  2339 LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG--ERLYRTGDLARYRADGVVEYLGRIDHQVKI 2409
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1256 RGQRVELGEIEHHVR--ECLPEARQLAVEVilPSGQKehalLAAFIqldkgnhnalfeekaSGEDsmAQVVFLTGVEEEL 1333
Cdd:PRK12316  2410 RGFRIELGEIEARLQahPAVREAVVVAQDG--ASGKQ----LVAYV---------------VPDD--AAEDLLAELRAWL 2466
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1334 AKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDIGASftvqqlaemrtSSQGPKRQPSTEVEQTMQQLWAQVLSIEpnS 1413
Cdd:PRK12316  2467 AARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVS-----------QLRQAYVAPQEGLEQRLAAIWQAVLKVE--Q 2533
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1414 IGLDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADIFRHPRLVDLARVQNSQFSSAAeevpafsllgedVNAVQLSQDA 1492
Cdd:PRK12316  2534 VGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTSRA------------PVLQKVTRVQ 2601
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1493 AAMCSVAagivediypcSPLQEGLMSLTAKRAGdYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSE----- 1567
Cdd:PRK12316  2602 PLPLSHA----------QQRQWFLWQLEPESAA-YHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEqtrqv 2670
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1568 ---LGLLQVVIEENIQWTEPKSLEEYLSEDKAVSVGLGDPLARyAFVKEACGGKRWFVWTIHHAVYDGWSLPLILHAVKQ 1644
Cdd:PRK12316  2671 ilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLR-VRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQ 2749
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1645 VYSGGVLQWQPSFNAFI-----------QYLGQQDLEATVAYWQTALADCEAVLFPTL--PPTVTQPVADATVEYQCP-P 1710
Cdd:PRK12316  2750 AYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLGGEQPVLELPLdrPRPALQSHRGARLDVALDvA 2829
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1711 LSKA------TSDTTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNTPvtGVEAMVGPTIATVPVRLRVQRDQTVFAFL 1784
Cdd:PRK12316  2830 LSREllalarREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQVLRAQVDAQLAFRDLL 2907
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1785 QGLQQQATDMIAHEQT-------GLQRIAKMGQGP--QHACSFQTLLVVQPVDDVLDNTLGEWRDHSelqefTTYTLMLQ 1855
Cdd:PRK12316  2908 GQVKEQALGAQAHQDLpfeqlveALQPERSLSHSPlfQVMYNHQSGERAAAQLPGLHIESFAWDGAA-----TQFDLALD 2982
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1856 CMLAAEGVQITASFDTRVIEKWVVEKMLRQFSFIMQQLAEaGAEKTVSDIETTTPEDRQQ-LWAWNQ-EVPPAIERCVHD 1933
Cdd:PRK12316  2983 TWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVE-NPQRSVDELAMLDAEERGQlLEAWNAtAAEYPLERGVHR 3061
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1934 LFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 2013
Cdd:PRK12316  3062 LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2014 PASRHEDIFRQTGAQVVVTSaQHSARWIGTNHQVVTVSAGSlEQFSTLVNPVDLpaKPENAAYVMFTSGSTGTPKGVVLE 2093
Cdd:PRK12316  3142 PEERLAYMLEDSGAQLLLSQ-SHLRLPLAQGVQVLDLDRGD-ENYAEANPAIRT--MPENLAYVIYTSGSTGKPKGVGIR 3217
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2094 HRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRDNLA-------KAITDMQVNWGY 2166
Cdd:PRK12316  3218 HSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALlvelinsEGVDVLHAYPSM 3297
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2167 LTSSVARLlDPCLVPSLKVLVLGGEQVNSTDWGKWPSSVQTINGYGPTECCVFCTGYTGIQGFQSG-NIGTSIASVSWVV 2245
Cdd:PRK12316  3298 LQAFLEEE-DAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvPIGRPIANRACYI 3376
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2246 DPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegYPGhegrqGRLYKTGDLVRYSSDGNLVCLGR 2325
Cdd:PRK12316  3377 LDGS-LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF-----VPG-----ERLYRTGDLARYRADGVIEYIGR 3445
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2326 KDSQVKVRGQRVELGEVEhhmrKCLPEANQLAVEVVPPSGERDhamLAAFIRLDDETRNSPLIIKyaednstaqivfltg 2405
Cdd:PRK12316  3446 VDHQVKIRGFRIELGEIE----ARLLEHPWVREAVVLAVDGRQ---LVAYVVPEDEAGDLREALK--------------- 3503
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2406 ieEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssegpkrQPSTEAERTMQQLWAQVLG 2485
Cdd:PRK12316  3504 --AHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVNELERRLAAIWADVLK 3570
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2486 ieLESIGLDDSFFRLGGDSITAMQISSSARALHLSVSTGDILKKKTIALIAREILPSTSTfsrSVWRDPVNNAFDLTPIQ 2565
Cdd:PRK12316  3571 --LEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGV---AVDQGPVSGETLLLPIQ 3645
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2566 HLYLTLDPSGRSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFQRQTGGRWQQYISEHDSSSLIVNHiHTRDTT 2645
Cdd:PRK12316  3646 QQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRA-ELDDAE 3724
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2646 EIVEALRQSRGSLDIERGPVLAAVLCD-AGERQSLFVAIHHLVVDLVSWRIL----LEELEDLLLGQTLP-PALSTPFQA 2719
Cdd:PRK12316  3725 ELERLGEEAQRSLDLADGPLLRALLATlADGSQRLLLVIHHLVVDGVSWRILledlQQAYQQLLQGEAPRlPAKTSSFKA 3804
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2720 WhaaqAKYIEEHVPPSAVAQveldpdQLSYW-----GVSPD--------DVLSSYAISEEFVLDRKTTSTLLGSCNDAFS 2786
Cdd:PRK12316  3805 W----AERLQEHARGEALKA------ELAYWqeqlqGVSSElpcdhpqgALQNRHAASVQTRLDRELTRRLLQQAPAAYR 3874
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2787 TRPLELMVAALSySFATIFSDRKPAAIFNEIHGREAWDSSIDLTRTVGWFTSMCPVQAANGAGLLDAIRETKDCIRSFQD 2866
Cdd:PRK12316  3875 TQVNDLLLTALA-RVVCRWTGEASALVQLEGHGREDLFADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPN 3953
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2867 NGWSYFASQFASASAADAFASLFPM-EVLFNYQGLYQ-QLERKDSLFknLPMPDSCEPALAALCPRFALFDVSFVVEQGC 2944
Cdd:PRK12316  3954 KGIGFGLLRYLGDEESRRTLAGLPVpRITFNYLGQFDgSFDEEMALF--VPAGESAGAEQSPDAPLDNWLSLNGRVYGGE 4031
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2945 AKVSFVSDKRARHQYRIRQWIQKYK---VTLIDMSALLPNRSAewTLSDLPLAfssyiDLDRFRHKTLPgleVPPEDVED 3021
Cdd:PRK12316  4032 LSLDWTFSREMFEEATIQRLADDYAaelTALVEHCCDAERHGV--TPSDFPLA-----GLDQARLDALP---LPLGEIED 4101
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3022 VFPCTPMQEGILTSQGKDPDA--YWVCFIYEVipnqeTSISLARLQQAWKGVVHQHSLLRTLLVDNvpGSTGT-TNVVLK 3098
Cdd:PRK12316  4102 IYPLSPMQQGMLFHSLYEQEAgdYINQMRVDV-----QGLDVERFRAAWQAALDRHDVLRSGFVWQ--GELGRpLQVVHK 4174
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3099 DPQPSISVFSSEGTATIELFRSRYNPAAQRSIGQLQH----HLSICQLNNGKVYLCLDINHAIIDAHSRGILMHDLQEAY 3174
Cdd:PRK12316  4175 QVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRapllRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY 4254
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3175 DANLNPQSTS-FRDFASYIKQQSQEEAGRYWAEYLDGV-EPCFF------PSLGDSGGANTIPRtvEVPSIDSSAVHMFC 3246
Cdd:PRK12316  4255 SGRPPAQPGGrYRDYIAWLQRQDAAASEAFWREQLAALdEPTRLaqaiarADLRSANGYGEHVR--ELDATATARLREFA 4332
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3247 KIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPLISILPCRIHLHKQLTVLEALKTVQENYAS 3326
Cdd:PRK12316  4333 RTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLA 4412
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3327 SLSFQTFPLASMHSFLGLGTSALFNTAL---------SLQRIddigpcSASEITLKMKEGLDPTEYNITLSAGYSkDAID 3397
Cdd:PRK12316  4413 LREHEHTPLYEIQRWAGQGGEALFDSLLvfenypvseALQQG------APGGLRFGEVTNHEQTNYPLTLAVGLG-ETLS 4485
                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3398 ISMTFRAGCMDLVQAKRLASNFSQAIKAVTTEPHSRIYSLDILTYNESKKI---WGWNADVPPAiERCVHDLFTEQAKAR 3474
Cdd:PRK12316  4486 LQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIvalWNRTDAGYPA-TRCVHQLVAERARMT 4564
                         3290      3300      3310      3320      3330      3340      3350      3360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:PRK12316  4565 PDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMM 4644
                         3370      3380      3390      3400      3410      3420      3430      3440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVASAQYSARwtssschvVTVSKALSSqlpAVVD---------STNTSVR--PENAAYIIFTSGSTGVPKGVV 3623
Cdd:PRK12316  4645 EDSGAALLLTQSHLLQR--------LPIPDGLAS---LALDrdedwegfpAHDPAVRlhPDNLAYVIYTSGSTGRPKGVA 4713
                         3450      3460      3470      3480      3490      3500      3510      3520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3624 LEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDS-DRRNSLAKAISTMDVNWAFLTPS 3702
Cdd:PRK12316  4714 VSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSlWDPERLYAEIHEHRVTVLVFPPV 4793
                         3530      3540      3550      3560      3570      3580      3590      3600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3703 VARLL-----DPGLIPSLKILAIGGEQSSSADWNRWPGSVQKI---HVYGPTECCIFCTGYTTKQGFEPST----IGTSV 3770
Cdd:PRK12316  4794 YLQQLaehaeRDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVylfNGYGPTETTVTVLLWKARDGDACGAaympIGTPL 4873
                         3610      3620      3630      3640      3650      3660      3670      3680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3771 ASVS-WVVDpeNHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNAD 3849
Cdd:PRK12316  4874 GNRSgYVLD--GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF-------GAPG--GRLYRTGDLARYRAD 4942
                         3690      3700      3710      3720      3730      3740      3750      3760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3850 GNLVYLGRKDSQVKVRGQRVELGEVEHHVRE--CLPEARQLAVEVilPSGQKdhamLAAFVqleegtqnaLLDKEAGGED 3927
Cdd:PRK12316  4943 GVIDYLGRVDHQVKIRGFRIELGEIEARLREhpAVREAVVIAQEG--AVGKQ----LVGYV---------VPQDPALADA 5007
                         3770      3780      3790      3800      3810      3820      3830      3840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3928 SMAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssqgpkrQPSTEAEQT 4007
Cdd:PRK12316  5008 DEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYV-----------APRSELEQQ 5076
                         3850      3860      3870      3880      3890      3900      3910      3920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4008 MQQLWAQVLSLgaDIIGLDDSFFRLGGDSIAAMKLVGEAR-RMGLHLSVADIFRHPKLADFAGIQITQCSSGTEEvpays 4086
Cdd:PRK12316  5077 VAAIWAEVLQL--ERVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTLAAFVELAAAAGSGDDEK----- 5149
                         3930
                   ....*....|
gi 1820002560 4087 lLGEDEDVMQ 4096
Cdd:PRK12316  5150 -FDDLEELLS 5158
PRK12467 PRK12467
peptide synthase; Provisional
451-4069 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1407.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  451 LELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSElGLLQVVVEE-----------KMQWTESES-LEEYLNEDKAASMG 518
Cdd:PRK12467    78 LRLRGELDVSALRRAFDALVARHESLRTRFVQDEE-GFRQVIDASlsltiplddlaNEQGRARESqIEAYINEEVARPFD 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  519 LGD-RLARYALIKEScGGKRWFVWTIHHALYDGWSLPLVLDAVKQVYSGAALERQPSF-NTFIQY----VSQQDVKAAA- 591
Cdd:PRK12467   157 LANgPLLRVRLLRLA-DDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLpALPIQYadyaIWQRSWLEAGe 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  592 -----AYWQTALADCEAVLFPPL--PSTVTQPVADTTVKYQCPPS------PEVTSSNITTSTLIRAAWAIIASRYTSSE 658
Cdd:PRK12467   236 rerqlAYWQEQLGGEHTVLELPTdrPRPAVPSYRGARLRVDLPQAlsaglkALAQREGVTLFMVLLASFQTLLHRYSGQS 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  659 DIVFGTTVTGRNAPITgvEAMVGPTIATVPLRVRPrkgQTVSAFLENLQQ--------QATEMIAYEQ--TGLQrimkmg 728
Cdd:PRK12467   316 DIRIGVPNANRNRVET--ERLIGFFVNTQVLKAEV---DPQASFLELLQQvkrtalgaQAHQDLPFEQlvEALQ------ 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  729 pgPQHACGFQTLLVVHPTDDVLSSDDTLGEWHSRSDSELQYFTTYALTIQCTLAV------EGVQITASFDARVVEHWVV 802
Cdd:PRK12467   385 --PERSLSHSPLFQVMFNHQNTATGGRDREGAQLPGLTVEELSWARHTAQFDLALdtyesaQGLWAAFTYATDLFEATTI 462
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  803 EKMLGQFSFVMQQLAEAgVEKKVADIETTTLEDRQQLWV-WNADMPPAVDRCIHDLFAEQARARPDASAVCAWDGELTYG 881
Cdd:PRK12467   463 ERLATHWRNLLEAIVAE-PRRRLGELPLLDAEERARELVrWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYA 541
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  882 ELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSQHAM 961
Cdd:PRK12467   542 ELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLA 621
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  962 LFASSerhqVTVSKVSTSQLPTVVN-----FAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDH 1036
Cdd:PRK12467   622 QLPVP----AGLRSLCLDEPADLLCgysghNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAAD 697
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1037 ARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRN--NLAKAISTMDVNCALLTPSVARLL----EPSAVPSLKRLV 1110
Cdd:PRK12467   698 DSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDaeAFAALMADQGVTVLKIVPSHLQALlqasRVALPRPQRALV 777
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1111 LQGEQVSFADWNRW----PGsVQTINGYGPTECSVCCNTYS-GKQGFKSGI--IGTSVASLSWVVDAGNHNrLAPLGSIG 1183
Cdd:PRK12467   778 CGGEALQVDLLARVralgPG-ARLINHYGPTETTVGVSTYElSDEERDFGNvpIGQPLANLGLYILDHYLN-PVPVGVVG 855
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1184 ELLVEGPILARGYLNDIDKTEAAFIDDPAwllegyeGHAGrrGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELG 1263
Cdd:PRK12467   856 ELYIGGAGLARGYHRRPALTAERFVPDPF-------GADG--GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELG 926
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1264 EIEHHVREcLPEARQLAVEVILPSGqkeHALLAAFIQldkgnhnalfeeKASGEDSMAQVVFLTGVEEELAKRLPEHMVP 1343
Cdd:PRK12467   927 EIEARLLA-QPGVREAVVLAQPGDA---GLQLVAYLV------------PAAVADGAEHQATRDELKAQLRQVLPDYMVP 990
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1344 TILFTVKAMPITTSGKIDRKRLQDIGASftvqqlaemrtSSQGPKRQPSTEVEQTMQQLWAQVLSIEPnsIGLDDSFFRL 1423
Cdd:PRK12467   991 AHLLLLDSLPLTPNGKLDRKALPKPDAS-----------AVQATFVAPQTELEKRLAAIWADVLKVER--VGLTDNFFEL 1057
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1424 GGDSIVAMKLVGEARRT-GLQLSVADIFRHPRLVDLARVQNSQFSSAAEEVPafsllgedvnavQLSQDAAAMCSVAagi 1502
Cdd:PRK12467  1058 GGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALP------------DVDRDQPLPLSYA--- 1122
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1503 vediypcSPLQEGLMSLTAKRAGdYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGL------LQVVIE 1576
Cdd:PRK12467  1123 -------QERQWFLWQLEPGSAA-YHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRqvihpvGSLTLE 1194
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1577 ENIQWTEPKSLEEYLSEDKAVSVGLGD----PLARYAFVKEAcGGKRWFVWTIHHAVYDGWSLPLILHAVKQVYS----G 1648
Cdd:PRK12467  1195 EPLLLAADKDEAQLKVYVEAEARQPFDleqgPLLRVGLLRLA-ADEHVLVLTLHHIVSDGWSMQVLVDELVALYAaysqG 1273
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1649 GVLQWqPSFNafIQYL------------GQQDLEatVAYWQTALADCEAVL-FPT-LPPTVTQPVADATVEYQCPP-LSK 1713
Cdd:PRK12467  1274 QSLQL-PALP--IQYAdyavwqrqwmdaGERARQ--LAYWKAQLGGEQPVLeLPTdRPRPAVQSHRGARLAFELPPaLAE 1348
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1714 A------TSDTTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNTPVTgvEAMVGPTIATVPVRLRVQRDQTVFAFLQGL 1787
Cdd:PRK12467  1349 GlralarREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAET--EGLIGFFVNTQVLRAEVDGQASFQQLLQQV 1426
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1788 QQQATDMIAH-----EQ--TGLQRIAKMGQGPQhacsFQTLLVVQPVDDVLDNTLGEWRDHS-ELQEFTT-YTLMLQCML 1858
Cdd:PRK12467  1427 KQAALEAQAHqdlpfEQlvEALQPERSLSHSPL----FQVMFNHQRDDHQAQAQLPGLSVESlSWESQTAqFDLTLDTYE 1502
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1859 AAEGVQITASFDTRVIEKWVVEKMLRQFSFIMQQLAeAGAEKTVSDIETTTPEDRQQ-LWAWNQ---EVPPAieRCVHDL 1934
Cdd:PRK12467  1503 SSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLV-ADPERRLGELDLLDEAERRQiLEGWNAthtGYPLA--RLVHQL 1579
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1935 FTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHP 2014
Cdd:PRK12467  1580 IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYP 1659
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2015 ASRHEDIFRQTGAQVVVTSAQHSARW-IGTNHQVVTVSAGS--LEQFSTlVNPVDLPAkPENAAYVMFTSGSTGTPKGVV 2091
Cdd:PRK12467  1660 RERLAYMIEDSGIELLLTQSHLQARLpLPDGLRSLVLDQEDdwLEGYSD-SNPAVNLA-PQNLAYVIYTSGSTGRPKGAG 1737
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2092 LEHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTS 2169
Cdd:PRK12467  1738 NRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDpeQLIQLIERQQVTTLHFVP 1817
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2170 SVARLL---DPCLV--PSLKVLVLGGE--QVNSTD--WGKWPsSVQTINGYGPTECCVFCTGYT----GIQGFQSGNIGT 2236
Cdd:PRK12467  1818 SMLQQLlqmDEQVEhpLSLRRVVCGGEalEVEALRpwLERLP-DTGLFNLYGPTETAVDVTHWTcrrkDLEGRDSVPIGQ 1896
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2237 SIASVSW-VVDPENHgrLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPawllEGYPGhegrqGRLYKTGDLVRYS 2315
Cdd:PRK12467  1897 PIANLSTyILDASLN--PVPIGVAGELYLGGVGLARGYLNRPALTAERFVADP----FGTVG-----SRLYRTGDLARYR 1965
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2316 SDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRkclpEANQLAVEVVPPSGERDHAMLAAFIRLDDEtrnsPLIikyaeDN 2395
Cdd:PRK12467  1966 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLR----EQGGVREAVVIAQDGANGKQLVAYVVPTDP----GLV-----DD 2032
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2396 STAQIVFLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREIGASftaqqlaEMRTSSEGPKrqpsTEAERT 2475
Cdd:PRK12467  2033 DEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS-------ELQQAYVAPQ----SELEQR 2101
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2476 MQQLWAQVLGieLESIGLDDSFFRLGGDSITAMQISSSARALHLSVSTGDILKKKTIALIAreILPSTSTFSRSVWRDPV 2555
Cdd:PRK12467  2102 LAAIWQDVLG--LEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLA--AVAQEGDGTVSIDQGPV 2177
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2556 NNAFDLTPIQHLYLTLDPSGRSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFqRQTGGRWQQYISEHDSSSLI 2635
Cdd:PRK12467  2178 TGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGF-VQEDGGWSAMHRAPEQERRP 2256
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2636 VNHIHTRDTTEIVEAL-RQSRGSLDIERGPVLAAVLCDAGE-RQSLFVAIHHLVVDLVSWRI----LLEELEDLLLGQTL 2709
Cdd:PRK12467  2257 LLWQVVVADKEELEALcEQAQRSLDLEEGPLLRAVLATLPDgSQRLLLVIHHLVVDGVSWRIlledLQTAYRQLQGGQPV 2336
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2710 P-PALSTPFQAWhaaqAKYIEEHVPPSAVAqveldpDQLSYW-----GVS---PDDVLSS-----YAISEEFVLDRKTTS 2775
Cdd:PRK12467  2337 KlPAKTSAFKAW----AERLQTYAASAALA------DELGYWqaqlqGAStelPCDHPQGglqrrHAASVTTHLDSEWTR 2406
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2776 TLLGSCNDAFSTRPLELMVAALSYSFATiFSDRKPAAIFNEIHGREAWDSSIDLTRTVGWFTSMCPVQAANGAGLLDAIR 2855
Cdd:PRK12467  2407 RLLQEAPAAYRTQVNDLLLTALARVIAR-WTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLATSIK 2485
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2856 ETKDCIRSFQDNGWSYFASQFASASAADAFASLFPM-EVLFNYQGLYQQ--LERKDSLFKnlPMPDSCEPALAALCPRFA 2932
Cdd:PRK12467  2486 TIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPVpRITFNYLGQFDGsfDAEKQALFV--PSGEFSGAEQSEEAPLGN 2563
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2933 LFDVSFVVEQGCAKVSFVSDKRARHQYRIRQWIQKYKV---TLIDMSALLPNRSAewTLSDLPLAFSSYIDLDRfrhktl 3009
Cdd:PRK12467  2564 WLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEelrALIEHCCSNDQRGV--TPSDFPLAGLSQEQLDR------ 2635
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3010 pgLEVPPEDVEDVFPCTPMQEGIL--TSQGKDPDAYWVCFIYEVipnqeTSISLARLQQAWKGVVHQHSLLRTLLVDnVP 3087
Cdd:PRK12467  2636 --LPVAVGDIEDIYPLSPMQQGMLfhTLYEGGAGDYINQMRVDV-----EGLDVERFRTAWQAVIDRHEILRSGFLW-DG 2707
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3088 GSTGTTNVVLKDPQPSISV--FSSEGTATIELfRSRYNPAAQRSIGQLQH---HLSICQLNNGKVYLCLDINHAIIDAHS 3162
Cdd:PRK12467  2708 ELEEPLQVVYKQARLPFSRldWRDRADLEQAL-DALAAADRQQGFDLLSApllRLTLVRTGEDRHHLIYTNHHILMDGWS 2786
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3163 RGILMHDLQEAYDANLNPQSTS-FRDFASYIKQQSQEEAGRYWAEyldgvepcffpSLGDSGGANTIPRTVEVPSIDSSA 3241
Cdd:PRK12467  2787 GSQLLGEVLQRYFGQPPPAREGrYRDYIAWLQAQDAEASEAFWKE-----------QLAALEEPTRLARALYPAPAEAVA 2855
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3242 VH----------------MFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPLISILPCRI 3305
Cdd:PRK12467  2856 GHgahylhldatqtrqliEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIA 2935
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3306 HLHKQLTVLEALKTVQENYASSLSFQTFPLASMHSFLGLGTSALFNTALSLQ------RIDDIGPcsaSEITLKMKEGLD 3379
Cdd:PRK12467  2936 SPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEALFDSILVFEnypiseALKQGAP---SGLRFGAVSSRE 3012
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3380 PTEYNITLSAGYSkDAIDISMTFRAGCMDLVQAKRLASNFSQAIKAVTTEPHSRIYSLDILTYNESKKIW-GWNAD-VPP 3457
Cdd:PRK12467  3013 QTNYPLTLAVGLG-DTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLhAWNATaAAY 3091
                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3458 AIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGA 3537
Cdd:PRK12467  3092 PSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGA 3171
                         3290      3300      3310      3320      3330      3340      3350      3360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3538 FVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARW-TSSSCHVVTVSK-ALSSQLPAVVDstnTSVRPENAAYIIFTSGS 3615
Cdd:PRK12467  3172 YVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLpAPAGDTALTLDRlDLNGYSENNPS---TRVMGENLAYVIYTSGS 3248
                         3370      3380      3390      3400      3410      3420      3430      3440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3616 TGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVpSDSDRRN--SLAKAISTMD 3693
Cdd:PRK12467  3249 TGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV-RDNDLWDpeELWQAIHAHR 3327
                         3450      3460      3470      3480      3490      3500      3510      3520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3694 VNWAFLTPSVARLL----DPGLIPSLKILAIGGE---QSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPST- 3765
Cdd:PRK12467  3328 ISIACFPPAYLQQFaedaGGADCASLDIYVFGGEavpPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAp 3407
                         3530      3540      3550      3560      3570      3580      3590      3600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3766 ---IGTSVASVSWVVDPENHNRlAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPawllegypgHPGRQGRLYKTGD 3842
Cdd:PRK12467  3408 yapIGRPVAGRSIYVLDGQLNP-VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP---------FSGSGGRLYRTGD 3477
                         3610      3620      3630      3640      3650      3660      3670      3680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3843 LVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVEVILPSGQKDhamLAAFVQLEEgTQNALLDKE 3922
Cdd:PRK12467  3478 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQ-HPSVREAVVLARDGAGGKQ---LVAYVVPAD-PQGDWRETL 3552
                         3690      3700      3710      3720      3730      3740      3750      3760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3923 AGGedsmaqvvflasveeeLAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssqgpkrqPST 4002
Cdd:PRK12467  3553 RDH----------------LAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA------------PRS 3604
                         3770      3780      3790      3800      3810      3820
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 4003 EAEQTMQQLWAQVlsLGADIIGLDDSFFRLGGDSIAAMKLVGEARR-MGLHLSVADIFRHPKLADFAG 4069
Cdd:PRK12467  3605 EVEQQLAAIWADV--LGVEQVGVTDNFFELGGDSLLALQVLSRIRQsLGLKLSLRDLMSAPTIAELAG 3670
PRK12316 PRK12316
peptide synthase; Provisional
1524-5464 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1350.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1524 AGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQV-------VIEENIQWTEPKSLEEYLsEDKA 1596
Cdd:PRK12316    69 SGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVpldrpleVEFEDCSGLPEAEQEARL-RDEA 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1597 VSVGL------GDPLARYAFVKEAcGGKRWFVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQWQPSFNAF-IQY----LG 1665
Cdd:PRK12316   148 QRESLqpfdlcEGPLLRVRLLRLG-EEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALpIQYadyaLW 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1666 QQD-LEA-----TVAYWQTALADCEAVL-FPT-LPPTVTQPVADATVEYQCPP-LSKATSDT------TTSTLIRAAWAI 1730
Cdd:PRK12316   227 QRSwLEAgeqerQLEYWRAQLGEEHPVLeLPTdHPRPAVPSYRGSRYEFSIDPaLAEALRGTarrqglTLFMLLLGAFNV 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1731 VTSRYTTSDDVVFGTTVTGRNTpvTGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAHEQTGLQRIA---K 1807
Cdd:PRK12316   307 LLHRYSGQTDIRVGVPIANRNR--AEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVealK 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1808 MGQGPQHACSFQTLLVVQP-VDDV--LDNTLG------EWRDHSelqefTTYTLMLQCMLAAEGVQITASFDTRVIEKWV 1878
Cdd:PRK12316   385 VERSLSHSPLFQVMYNHQPlVADIeaLDTVAGlefgqlEWKSRT-----TQFDLTLDTYEKGGRLHAALTYATDLFEART 459
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1879 VEKMLRQFSFIMQQLAEAGaEKTVSDIETTTPEDRQQL-WAWNQ--EVPPaIERCVHDLFTEQAKARPHAPAICAWDGEL 1955
Cdd:PRK12316   460 VERMARHWQNLLRGMVENP-QARVDELPMLDAEERGQLvEGWNAtaAEYP-LQRGVHRLFEEQVERTPEAPALAFGEETL 537
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1956 TYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSaQ 2035
Cdd:PRK12316   538 DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ-S 616
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2036 HSARWIGTNH--QVVTVSAGSLEQFSTLVNPVDLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNL 2113
Cdd:PRK12316   617 HLGRKLPLAAgvQVLDLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVG 696
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2114 LRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSSVARLL----DPCLVPSLKVLV 2187
Cdd:PRK12316   697 DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDpaKLVELINREGVDTLHFVPSMLQAFlqdeDVASCTSLRRIV 776
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2188 LGGE--------QVnstdWGKWPSSvQTINGYGPTECCVFCTGYTGI-QGFQSGNIGTSIASV-SWVVDPEnhGRLAPLG 2257
Cdd:PRK12316   777 CSGEalpadaqeQV----FAKLPQA-GLYNLYGPTEAAIDVTHWTCVeEGGDSVPIGRPIANLaCYILDAN--LEPVPVG 849
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2258 SIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegypgheGRQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRV 2337
Cdd:PRK12316   850 VLGELYLAGRGLARGYHGRPGLTAERFVPSPF----------VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 919
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2338 ELGEVEHHMRKcLPEANQLAVEVVppsgerDHAMLAAFIRLDDETRNSPLIIKYAednstaqivfltgieeeLSERLPQH 2417
Cdd:PRK12316   920 ELGEIEARLLE-HPWVREAAVLAV------DGKQLVGYVVLESEGGDWREALKAH-----------------LAASLPEY 975
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2418 MVPTVFFALVHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssegpkrQPSTEAERTMQQLWAQVLGIelESIGLDDSF 2497
Cdd:PRK12316   976 MVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYV-----------APRNALERTLAAIWQDVLGV--ERVGLDDNF 1042
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2498 FRLGGDSITAMQISSSARALHLSVSTGDILKKKTIALIAReilpsTSTFSRSVWRD--PVNNAFDLTPIQHLYLTLDPSG 2575
Cdd:PRK12316  1043 FELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLAL-----VAKAGQATAADqgPASGEVALAPVQRWFFEQAIPQ 1117
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2576 RSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFqRQTGGRWQQ-YISEHDSSSLIVNHIhtRDTTEIVEALRQS 2654
Cdd:PRK12316  1118 RQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRF-REEDGGWQQaYAAPQAGEVLWQRQA--ASEEELLALCEEA 1194
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2655 RGSLDIERGPVLAAVLCD-AGERQSLFVAIHHLVVDLVSWRILLEELEDLLLgQTLP--PALSTPFQAWhaaqAKYIEEH 2731
Cdd:PRK12316  1195 QRSLDLEQGPLLRALLVDmADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYA-DLDAdlPARTSSYQAW----ARRLHEH 1269
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2732 VPPSAvaqveldpDQLSYWGVS------------PDDVLSS-YAISEEFVLDRKTTSTLLGSCNDAFSTRPLELMVAALS 2798
Cdd:PRK12316  1270 AGARA--------EELDYWQAQledaphelpcenPDGALENrHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALA 1341
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2799 YSFATiFSDRKPAAIFNEIHGREAWDSSIDLTRTVGWFTSMCPVQAANGAGLLDAIRETKDCIRSFQDNGWSYFASQFAS 2878
Cdd:PRK12316  1342 RVTCR-WSGQASVLVQLEGHGREDLFEDIDLSRTVGWFTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLA 1420
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2879 ASAADAFASLFPM-EVLFNYQGLYQQLERKDSLFknLPMPDSCEPALAALCPRFALFDVSFVVEQGCAKVSFVSDKRARH 2957
Cdd:PRK12316  1421 GEEAAARLAALPQpRITFNYLGQFDRQFDEAALF--VPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFA 1498
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2958 QYRIRQWIQKYKV---TLIDMSALLPNRSAewTLSDLPLAfssyidldRFRHKTLPGLEVPPEDVEDVFPCTPMQEGIL- 3033
Cdd:PRK12316  1499 EATVQRLADDYARelqALIEHCCDERNRGV--TPSDFPLA--------GLSQAQLDALPLPAGEIADIYPLSPMQQGMLf 1568
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3034 -TSQGKDPDAYWVCFIYEVipnqeTSISLARLQQAWKGVVHQHSLLRTLLVDnVPGSTGTTNVVLKDPQPSISVFSSEGT 3112
Cdd:PRK12316  1569 hSLYEQEAGDYINQLRVDV-----QGLDPDRFRAAWQATVDRHEILRSGFLW-QDGLEQPLQVIHKQVELPFAELDWRGR 1642
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3113 ATIELFRSRYNPAAQRSIGQLQH----HLSICQLNNGKVYLCLDINHAIIDAHSRGILMHDLQEAYDANLnPQSTS--FR 3186
Cdd:PRK12316  1643 EDLGQALDALAQAERQKGFDLTRapllRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQP-VAAPGgrYR 1721
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3187 DFASYIKQQSQEEAGRYWAEYLDGVEPcffPSL---------GDSGGANtipRTVEVPSIDSSAVHMFCKIWEVTPATII 3257
Cdd:PRK12316  1722 DYIAWLQRQDAAASEAFWKEQLAALEE---PTRlaqaartedGQVGYGD---HQQLLDPAQTRALAEFARAQKVTLNTLV 1795
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3258 QTAWALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPLISILPCRIHLHKQLTVLEALKTVQENYASSLSFQTFPLAS 3337
Cdd:PRK12316  1796 QAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYD 1875
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3338 MHSFLGLGTSALFNTAL---------SLQRIDDIGpcsaseITLKMKEGLDPTEYNITLSAGYSkDAIDISMTFRAGCMD 3408
Cdd:PRK12316  1876 IQRWAGQGGEALFDSLLvfenypvaeALKQGAPAG------LVFGRVSNHEQTNYPLTLAVTLG-ETLSLQYSYDRGHFD 1948
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3409 LVQAKRLASNFSQAIKAVTTEPHSRIYSLDILTYNESKKIWG-WNADVPPA-IERCVHDLFTEQAKARPHAPAICAWDGE 3486
Cdd:PRK12316  1949 AAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILAdWDRTPEAYpRGPGVHQRIAEQAARAPEAIAVVFGDQH 2028
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASA 3566
Cdd:PRK12316  2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3567 QYSARW---TSSSCHVVTVSKALS---SQLPAVvdstntSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAF 3640
Cdd:PRK12316  2109 HLLERLplpAGVARLPLDRDAEWAdypDTAPAV------QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY 2182
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3641 GITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRR-NSLAKAISTMDVNWAFLTPSVARLLDP-----GLIPS 3714
Cdd:PRK12316  2183 ELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDpEQLYDEMERHGVTILDFPPVYLQQLAEhaerdGRPPA 2262
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3715 LKILAIGGEQSSSADWNRWPGSVQK---IHVYGPTECCIFCTGYTTKQ----GFEPSTIGTSVASVS-WVVDPENHnrLA 3786
Cdd:PRK12316  2263 VRVYCFGGEAVPAASLRLAWEALRPvylFNGYGPTEAVVTPLLWKCRPqdpcGAAYVPIGRALGNRRaYILDADLN--LL 2340
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3787 PLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRG 3866
Cdd:PRK12316  2341 APGMAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG--ERLYRTGDLARYRADGVVEYLGRIDHQVKIRG 2411
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3867 QRVELGEVEHHVR--ECLPEARQLAVEVilPSGQKdhamLAAFVQleegtqnalldkeagGEDsmAQVVFLASVEEELAK 3944
Cdd:PRK12316  2412 FRIELGEIEARLQahPAVREAVVVAQDG--ASGKQ----LVAYVV---------------PDD--AAEDLLAELRAWLAA 2468
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3945 RLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssqgpkrQPSTEAEQTMQQLWAQVLSLgaDIIG 4024
Cdd:PRK12316  2469 RLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYV-----------APQEGLEQRLAAIWQAVLKV--EQVG 2535
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4025 LDDSFFRLGGDSIAAMKLVGEARR-MGLHLSVADIFRHPKLADFAGiqitqcssgteevpaysllgededvmqVCKDVAA 4103
Cdd:PRK12316  2536 LDDHFFELGGHSLLATQVVSRVRQdLGLEVPLRILFERPTLAAFAA---------------------------SLESGQT 2588
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4104 MCSVDASAITDVYP-----CSPLQEGLMSLTAKRAGdYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSE-- 4176
Cdd:PRK12316  2589 SRAPVLQKVTRVQPlplshAQQRQWFLWQLEPESAA-YHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEqt 2667
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4177 ------LGLLQVVVEERIQWTESESLEEYPREDKAVSMGVGDRLARYALIKepYDGGKRWFVWTMHHALYDGWSLPRILH 4250
Cdd:PRK12316  2668 rqvilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLA--LDGQEHVLVITQHHIVSDGWSMQVMVD 2745
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4251 AVKQAYSGVVLERQPSFNAFI-----------QYLSQQDPEAAAAYWQTAL--VDCKAALFPTLPPTVTQPVADTTVEYQ 4317
Cdd:PRK12316  2746 ELVQAYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLggEQPVLELPLDRPRPALQSHRGARLDVA 2825
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4318 CPPP-------SQSATDITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGGEAIVGPTIATVPVRLRVQRDQTV 4390
Cdd:PRK12316  2826 LDVAlsrellaLARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQVLRAQVDAQLAF 2903
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4391 FAFLQGVQQQATDMIAHEQTGL-QRIAKMSP--GARHACGFQTLLVVQPTD----DVLGSDDMLGEWRSYSEMQDFTtya 4463
Cdd:PRK12316  2904 RDLLGQVKEQALGAQAHQDLPFeQLVEALQPerSLSHSPLFQVMYNHQSGEraaaQLPGLHIESFAWDGAATQFDLA--- 2980
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4464 lmVQCVLVKDRVGVTASFDARVIEQWVVEKMLRQFGFVMQQLAdAGEEKKVAGIETTTTGDRQQ-LWAWNQ-DVPPAIER 4541
Cdd:PRK12316  2981 --LDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMV-ENPQRSVDELAMLDAEERGQlLEAWNAtAAEYPLER 3057
                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4542 CVHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL 4621
Cdd:PRK12316  3058 GVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL 3137
                         3290      3300      3310      3320      3330      3340      3350      3360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4622 DPDHPASRHEHIFRQTGAQVVLaSAQYATLWTSLGRSVVIVsEASTSQLpvvtKTADPSVN--PGNAAYAIFTSGSTGIP 4699
Cdd:PRK12316  3138 DPEYPEERLAYMLEDSGAQLLL-SQSHLRLPLAQGVQVLDL-DRGDENY----AEANPAIRtmPENLAYVIYTSGSTGKP 3211
                         3370      3380      3390      3400      3410      3420      3430      3440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4700 KGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLcCGCICVPSDSDRRNNLAKAINAMDVNWALL 4779
Cdd:PRK12316  3212 KGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLM-SGARVVLAGPEDWRDPALLVELINSEGVDV 3290
                         3450      3460      3470      3480      3490      3500      3510      3520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4780 TPSVARML-------DPCVVQSLKILVLGGEQVNSADWDRWPKSIQTINAYGPTECSICCTTYSGKQGFKSGT-IGTSIV 4851
Cdd:PRK12316  3291 LHAYPSMLqafleeeDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAVpIGRPIA 3370
                         3530      3540      3550      3560      3570      3580      3590      3600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4852 SVSWVVDPENHNRlAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawLLEGygghsgrqGRLYKTGDLVRYDADGN 4931
Cdd:PRK12316  3371 NRACYILDGSLEP-VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDP--FVPG--------ERLYRTGDLARYRADGV 3439
                         3610      3620      3630      3640      3650      3660      3670      3680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4932 LVYLGRKDSQVKLRGQRVELGEVEHHVRECLT--EAKQLAVEvivpegeggyamlaafvqlGDDTYNTLVKEKAGGDslt 5009
Cdd:PRK12316  3440 IEYIGRVDHQVKIRGFRIELGEIEARLLEHPWvrEAVVLAVD-------------------GRQLVAYVVPEDEAGD--- 3497
                         3690      3700      3710      3720      3730      3740      3750      3760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5010 vqvvFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREIGASFTAQQLAemrtssqgpkrQPSTEAERTMQ 5089
Cdd:PRK12316  3498 ----LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVNELERRLA 3562
                         3770      3780      3790      3800      3810      3820      3830      3840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5090 QLWTRVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRTGLQLSVADVFRHPRLVDLAyvqnsecssaaeevPAFSLLG 5169
Cdd:PRK12316  3563 AIWADVLKLE--QVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLA--------------RVARVGG 3626
                         3850      3860      3870      3880      3890      3900      3910      3920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5170 GRAADTAQVSQDAAAMcsvdassvedmypcsPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALR 5249
Cdd:PRK12316  3627 GVAVDQGPVSGETLLL---------------PIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALR 3691
                         3930      3940      3950      3960      3970      3980      3990      4000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5250 TRIVQ---HSELGLLQVVVEEKIQW---TESKRLEEYLREDKAVSMGLGDRLARYALIKEPYDGGKRwFVWTIHHALYDG 5323
Cdd:PRK12316  3692 LRFVEdagGWTAEHLPVELGGALLWraeLDDAEELERLGEEAQRSLDLADGPLLRALLATLADGSQR-LLLVIHHLVVDG 3770
                         4010      4020      4030      4040      4050      4060      4070      4080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5324 WSLpRIL-----QAVKQIYSGAVPE---RQPSFNAFIQ----YLGQQDLEAATLYWQTALADCKAALfPTLPP------- 5384
Cdd:PRK12316  3771 VSW-RILledlqQAYQQLLQGEAPRlpaKTSSFKAWAErlqeHARGEALKAELAYWQEQLQGVSSEL-PCDHPqgalqnr 3848
                         4090      4100      4110      4120      4130      4140      4150      4160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5385 ----TVTQPVADTTVEYQCPPPSQSATDIttSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGVE--AMVGPTIAT 5458
Cdd:PRK12316  3849 haasVQTRLDRELTRRLLQQAPAAYRTQV--NDLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDlsRTVGWFTSL 3926

                   ....*.
gi 1820002560 5459 VPLRVC 5464
Cdd:PRK12316  3927 FPVRLS 3932
PRK05691 PRK05691
peptide synthase; Validated
85-4055 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1103.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   85 VVDPKdHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPA--WLLEGHGGYAgRQGRLYKTGDLvrydadgnlv 162
Cdd:PRK05691   383 IVDPQ-SLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHDGrtWLRTGDLGFL-RDGELFVTGRL---------- 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  163 clgrKDSQVkLRGQRVELGEVEHHVREClpeakqlaVEVVlplgqkNHATLAAFIQLDKGthnallKEKVGGDDSIARVV 242
Cdd:PRK05691   451 ----KDMLI-VRGHNLYPQDIEKTVERE--------VEVV------RKGRVAAFAVNHQG------EEGIGIAAEISRSV 505
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  243 FLAGVEEELAKRLPK------HMVPTVFfALLH---FPTTTSGKTDRK--RLR-EIG-----ASFTAQQLAEMRTSSQGP 305
Cdd:PRK05691   506 QKILPPQALIKSIRQavaeacQEAPSVV-LLLNpgaLPKTSSGKLQRSacRLRlADGsldsyALFPALQAVEAAQTAASG 584
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  306 krqpsTEAERTMQQLWARVLGIEpdSIGLDDSFFRLGGDSIAAIKLVGEARRT-GLQPSVADIFRHPTLAAlasletnqY 384
Cdd:PRK05691   585 -----DELQARIAAIWCEQLKVE--QVAADDHFFLLGGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAA--------F 649
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  385 NITIEETPPLSLLGENADVAQVRDEAAAmcsvdgsaiedmylCSPLQEGLMSL--TTKRAGDYIMQDVLELRADVDEHAF 462
Cdd:PRK05691   650 SAAVARQLAGGGAAQAAIARLPRGQALP--------------QSLAQNRLWLLwqLDPQSAAYNIPGGLHLRGELDEAAL 715
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  463 RAAWEYVVQSIAVLRTRIVQHSELGLLQVVVEEKMQW----------TESESLEEYLNEDKAAS---MGLGDrLARYALI 529
Cdd:PRK05691   716 RASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALqridlsdlpeAEREARAAQIREEEARQpfdLEKGP-LLRVTLV 794
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  530 KESCGGKRWFVwTIHHALYDGWSLPLVLDAVKQVYS----GAALERQPSFNTFIQYVSQQ-------DVKAAAAYWQTAL 598
Cdd:PRK05691   795 RLDDEEHQLLV-TLHHIVADGWSLNILLDEFSRLYAaacqGQTAELAPLPLGYADYGAWQrqwlaqgEAARQLAYWKAQL 873
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  599 ADCEAVLFPPLPSTVTQPVADTTVKYQCPPSPEVTSS--------NITTSTLIRAAWAIIASRYTSSEDIVFGttVTGRN 670
Cdd:PRK05691   874 GDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEAlrglaqahQATLFMVLLAAFQALLHRYSGQGDIRIG--VPNAN 951
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  671 APITGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTGLQRIMKMGPGPQHACGFQTLLVvHPTDDvL 750
Cdd:PRK05691   952 RPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQGLFQVMFN-HQQRD-L 1029
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  751 SS----DDTLGE---WHSRSdselqyfTTYALTIQCTLAVEGvQITASFD--ARVVEHWVVEKMLGQFSFVMQQLAEAGv 821
Cdd:PRK05691  1030 SAlrrlPGLLAEelpWHSRE-------AKFDLQLHSEEDRNG-RLTLSFDyaAELFDAATIERLAEHFLALLEQVCEDP- 1100
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  822 EKKVADIETTTLEDRQQLWVWNADMPPAVDRCIHDLFAEQARARPDASAVcAWDGE-LTYGELDELSSKLAAHLVQLGVK 900
Cdd:PRK05691  1101 QRALGDVQLLDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIAL-VWDGGsLDYAELHAQANRLAHYLRDKGVG 1179
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  901 REDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSqhAMLFASSERHQVTVSKVSTSQ 980
Cdd:PRK05691  1180 PDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS--HLLERLPQAEGVSAIALDSLH 1257
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  981 LPtvvNFAKSP----VDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIIT 1056
Cdd:PRK05691  1258 LD---SWPSQApglhLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFW 1334
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1057 TLLYGGCICVPSESDRRN--NLAKAISTMDVNCALLTPSVARLL--EPSAVP--SLKRLVLQGEQVSFADWNR----WPG 1126
Cdd:PRK05691  1335 PLITGCRLVLAGPGEHRDpqRIAELVQQYGVTTLHFVPPLLQLFidEPLAAActSLRRLFSGGEALPAELRNRvlqrLPQ 1414
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1127 sVQTINGYGPTECSVCCNTY--SGKQGFKSGIiGTSVASLSWVVDAGNHNrLAPLGSIGELLVEGPILARGYLNDIDKTE 1204
Cdd:PRK05691  1415 -VQLHNRYGPTETAINVTHWqcQAEDGERSPI-GRPLGNVLCRVLDAELN-LLPPGVAGELCIGGAGLARGYLGRPALTA 1491
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1205 AAFIDDPawllegyEGHAGrrGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQLAVEVi 1284
Cdd:PRK05691  1492 ERFVPDP-------LGEDG--ARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA-QPGVAQAAVLV- 1560
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1285 lpsgqKEHALLAAFIqldkgnhnALFEEKASGEDSMAQVvfltgvEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKR 1364
Cdd:PRK05691  1561 -----REGAAGAQLV--------GYYTGEAGQEAEAERL------KAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRA 1621
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1365 LQDigasfTVQQlaemrtssQGPKRQPSTEVEQTMQQLWAQVLSIEpnSIGLDDSFFRLGGDSIVAMKLVGEAR-RTGLQ 1443
Cdd:PRK05691  1622 LPE-----PVWQ--------QREHVEPRTELQQQIAAIWREVLGLP--RVGLRDDFFALGGHSLLATQIVSRTRqACDVE 1686
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1444 LSVADIFRHPRLVDLA-RVQNSQFSSAAEEVPAFSLLGEDvNAVQLSQDAAAMCsvaagIVEDIYPCSPLqeglmsltak 1522
Cdd:PRK05691  1687 LPLRALFEASELGAFAeQVARIQAAGERNSQGAIARVDRS-QPVPLSYSQQRMW-----FLWQMEPDSPA---------- 1750
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1523 ragdYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQVVIEENI--QWTEPKSLEEYLSEDKAVSvg 1600
Cdd:PRK05691  1751 ----YNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLrmDWQDFSALPADARQQRLQQ-- 1824
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1601 LGD------------PLARYAFVKeACGGKRWFVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQWQPSFNAF-IQYLG-- 1665
Cdd:PRK05691  1825 LADseahqpfdlergPLLRACLVK-AAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLpVQYLDys 1903
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1666 ---QQDLEA-----TVAYWQTALADCEAVLfpTLPPTVTQPVADA----TVEYQCPP-------LSKATSDTTTSTLIRA 1726
Cdd:PRK05691  1904 vwqRQWLESgerqrQLDYWKAQLGNEHPLL--ELPADRPRPPVQShrgeLYRFDLSPelaarvrAFNAQRGLTLFMTMTA 1981
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1727 AWAIVTSRYTTSDDVVFGTTVTGRNTPVTgvEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAHEQTGLQRIA 1806
Cdd:PRK05691  1982 TLAALLYRYSGQRDLRIGAPVANRIRPES--EGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLV 2059
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1807 KMGQGPQHACS---FQTLLVVQ-------------PVDDVLDNTLGEWRDHSelQEFTTYTLMLQCMLAAEgvqiTASFD 1870
Cdd:PRK05691  2060 EALQPPRSAAYnplFQVMCNVQrwefqqsrqlagmTVEYLVNDARATKFDLN--LEVTDLDGRLGCCLTYS----RDLFD 2133
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1871 ----TRVIEKWvvekmlrqfsfimQQLAEA---GAEKTVSDIETTTPEDRQQLWAWNQEVP--PAIERCVHDLFTEQAKA 1941
Cdd:PRK05691  2134 epriARMAEHW-------------QNLLEAllgDPQQRLAELPLLAAAEQQQLLDSLAGEAgeARLDQTLHGLFAAQAAR 2200
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1942 RPHAPAIcAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHED 2020
Cdd:PRK05691  2201 TPQAPAL-TFAGQtLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHY 2279
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2021 IFRQTGAQVVVTSA----------QHSARWIGTNHQVvtvsagSLEQFSTlvNPVDLPAKPENAAYVMFTSGSTGTPKGV 2090
Cdd:PRK05691  2280 MIEDSGIGLLLSDRalfealgelpAGVARWCLEDDAA------ALAAYSD--APLPFLSLPQHQAYLIYTSGSTGKPKGV 2351
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2091 VLEHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSE-RRDNLAKAITDMQVNWGYLTS 2169
Cdd:PRK05691  2352 VVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQwGAEEICQLIREQQVSILGFTP 2431
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2170 SVARLLDPCLVP-----SLKVLVLGGEQVNSTDWGKWPSSVQT---INGYGPTECCVF----CTGYTGIQGFQSGNIGTS 2237
Cdd:PRK05691  2432 SYGSQLAQWLAGqgeqlPVRMCITGGEALTGEHLQRIRQAFAPqlfFNAYGPTETVVMplacLAPEQLEEGAASVPIGRV 2511
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2238 I-ASVSWVVDPEnhgrLAPL--GSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegypGHEGrqGRLYKTGDLVRY 2314
Cdd:PRK05691  2512 VgARVAYILDAD----LALVpqGATGELYVGGAGLAQGYHDRPGLTAERFVADPF-------AADG--GRLYRTGDLVRL 2578
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2315 SSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRK--CLPEANQLAVEVvpPSGERdhamLAAFirlddetrnspLIIKYA 2392
Cdd:PRK05691  2579 RADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEhpAVREAVVLALDT--PSGKQ----LAGY-----------LVSAVA 2641
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2393 EDNSTAQIVFLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLreigasfTAQQLAEMRTSSEgpkrQPSTEA 2472
Cdd:PRK05691  2642 GQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL-------PAPDPELNRQAYQ----APRSEL 2710
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2473 ERTMQQLWAQVLGIelESIGLDDSFFRLGGDSITAMQISSSARALHLSVSTGDILKKKTIALIAReilPSTSTFSRSVWR 2552
Cdd:PRK05691  2711 EQQLAQIWREVLNV--ERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAA---VATHSEAAQAEQ 2785
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2553 DPVNNAFDLTPIQHLYLTLDPSGRSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFqRQTGGRWQ-QYISEHDS 2631
Cdd:PRK05691  2786 GPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRF-SQADGRWQaEYRAVTAQ 2864
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2632 SSLIvnHIHTRDTTEIVEALRQSRGSLDIERGPVLAAVLCDAGE-RQSLFVAIHHLVVDLVSWRI----LLEELEDLLLG 2706
Cdd:PRK05691  2865 ELLW--QVTVADFAECAALFADAQRSLDLQQGPLLRALLVDGPQgQQRLLLAIHHLVVDGVSWRVlledLQALYRQLSAG 2942
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2707 QTLP-PALSTPFQAWHAAQAKYieehvppsavAQVELDPDQLSYWGVSPDDV-------------LSSYAISEEFVLDRK 2772
Cdd:PRK05691  2943 AEPAlPAKTSAFRDWAARLQAY----------AGSESLREELGWWQAQLGGPraelpcdrpqggnLNRHAQTVSVRLDAE 3012
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2773 TTSTLLGSCNDAFSTRPLELMVAALSYSFATiFSDRKPAAIFNEIHGREAWDSSIDLTRTVGWFTSMCPV----QAANGA 2848
Cdd:PRK05691  3013 RTRQLLQQAPAAYRTQVNDLLLTALARVLCR-WSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLrltpAPGDDA 3091
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2849 GLLDAIRETKDCIRSFQDNGWSYFASQFASASAADAFASLFPM-EVLFNYQGLYQQLERKDSLFKnlPMPDSCEPALAAL 2927
Cdd:PRK05691  3092 ARGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAALPQaPITFNYLGQFDQSFASDALFR--PLDEPAGPAHDPD 3169
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2928 CPRFALFDVSFVVEQGCAKVSFV-SDKRARHQyRIRQWIQKYKVTLIDMSA-LLPNRSAEWTLSDLPLAFSSYIDLDrfr 3005
Cdd:PRK05691  3170 APLPNELSVDGQVYGGELVLRWTySAERYDEQ-TIAELAEAYLAELQALIAhCLADGAGGLTPSDFPLAQLTQAQLD--- 3245
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3006 hktlpGLEVPPEDVEDVFPCTPMQEGILTSQGKDPDA--YWVCFIYEVipnqETSISLARLQQAWKGVVHQHSLLRTLLV 3083
Cdd:PRK05691  3246 -----ALPVPAAEIEDVYPLTPMQEGLLLHTLLEPGTglYYMQDRYRI----NSALDPERFAQAWQAVVARHEALRASFS 3316
                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3084 DNV----------PGSTGTtnvvlkDPQPSISVFSSEGTATIELFRSRYNPAAQRSIGQLQHHLSICQLNNGKVYLCLDI 3153
Cdd:PRK05691  3317 WNAgetmlqvihkPGRTPI------DYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSN 3390
                         3290      3300      3310      3320      3330      3340      3350      3360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3154 NHAIIDAHSRGILMHDLQEAY-------DANLnPQSTSFRDFASYIKQQSQEEAGRYWAEYLDGVE-PCFFPS------- 3218
Cdd:PRK05691  3391 HHILIDAWCRSLLMNDFFEIYtalgegrEAQL-PVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFErPTPIPSdrpflre 3469
                         3370      3380      3390      3400      3410      3420      3430      3440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3219 -LGDSGGANTIPRTVEVPSIDSSAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPL 3297
Cdd:PRK05691  3470 hAGDSGGMVVGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLF 3549
                         3450      3460      3470      3480      3490      3500      3510      3520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3298 ISILPCRIHL---HKQLTVLEALKTVQENYASSLSFQTFPLASM--HSFLGLGtSALFNTALSLQRiddiGPCSASeiTL 3372
Cdd:PRK05691  3550 INSIALRVQLpaaGQRCSVRQWLQGLLDSNMELREYEYLPLVAIqeCSELPKG-QPLFDSLFVFEN----APVEVS--VL 3622
                         3530      3540      3550      3560      3570      3580      3590      3600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3373 KMKEGLDP------TEYNITLSA-GYSKDAIDISMTFRAGCMDLVQAKRLASNFSQAIKAVTTEPHSRIYSLDILTYNES 3445
Cdd:PRK05691  3623 DRAQSLNAssdsgrTHTNFPLTAvCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQER 3702
                         3610      3620      3630      3640      3650      3660      3670      3680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3446 K-KIWGWNA---DVPpaIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKS 3521
Cdd:PRK05691  3703 DfLLDGCNRserDYP--LEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERG 3780
                         3690      3700      3710      3720      3730      3740      3750      3760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3522 MWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASA----QYSARWTSSSCHVV--------TVSKALSSQ 3589
Cdd:PRK05691  3781 LDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAacreQARALLDELGCANRprllvweeVQAGEVASH 3860
                         3770      3780      3790      3800      3810      3820      3830      3840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3590 LPAVVDStntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLC 3669
Cdd:PRK05691  3861 NPGIYSG------PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLF 3934
                         3850      3860      3870      3880      3890      3900      3910      3920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3670 GGCI-CVPSD--SDRRNSLAKA----ISTMDVnwaflTPS-VARLL--DPGLIPSLKILAIGGEQSS---SADW-NRWPG 3735
Cdd:PRK05691  3935 GARVeIVPNAiaHDPQGLLAHVqaqgITVLES-----VPSlIQGMLaeDRQALDGLRWMLPTGEAMPpelARQWlQRYPQ 4009
                         3930      3940      3950      3960      3970      3980      3990      4000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3736 sVQKIHVYGPTEC----CIFCTGYTTKQG-FEPstIGTsvasvswvvdPENHNR---------LAPLGSMGELLMEGPIL 3801
Cdd:PRK05691  4010 -IGLVNAYGPAECsddvAFFRVDLASTRGsYLP--IGS----------PTDNNRlylldealeLVPLGAVGELCVAGTGV 4076
                         4010      4020      4030      4040      4050      4060      4070      4080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3802 ARGYLNDVDKTEAAFIDDPAwllegypGHPGRqgRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREc 3881
Cdd:PRK05691  4077 GRGYVGDPLRTALAFVPHPF-------GAPGE--RLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE- 4146
                         4090      4100      4110      4120      4130      4140      4150      4160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3882 LPEARQLAVEVIL-PSGQkdhaMLAAFVQLEEGTQN--ALLDKeaggedsmaqvvflasVEEELAKRLPEHMVPTVFFSL 3958
Cdd:PRK05691  4147 QAEVREAAVAVQEgVNGK----HLVGYLVPHQTVLAqgALLER----------------IKQRLRAELPDYMVPLHWLWL 4206
                         4170      4180      4190      4200      4210      4220      4230      4240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3959 LHFPTTTSGKTDRKRLR--EIGASFTAQQLAemrtssqgpkrqPSTEAEQTMQQLWAQVLSlgADIIGLDDSFFRLGGDS 4036
Cdd:PRK05691  4207 DRLPLNANGKLDRKALPalDIGQLQSQAYLA------------PRNELEQTLATIWADVLK--VERVGVHDNFFELGGHS 4272
                         4250
                   ....*....|....*....
gi 1820002560 4037 IAAMKLVGEARRMgLHLSV 4055
Cdd:PRK05691  4273 LLATQIASRVQKA-LQRNV 4290
PRK12316 PRK12316
peptide synthase; Provisional
4106-6543 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 892.77  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4106 SVDASAITDVYPCSPLQEGLM--SLTAKRAGDYIMQtvleLRADV---NEDAFRAAWELVVQLTAVLRTRIVQHSELGLL 4180
Cdd:PRK12316  1547 PLPAGEIADIYPLSPMQQGMLfhSLYEQEAGDYINQ----LRVDVqglDPDRFRAAWQATVDRHEILRSGFLWQDGLEQP 1622
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4181 QVVVEERIQ--WTESESLEEYPREDKAVSMGVGDRLARYALIKEPY-------DGGKRW-FVWTMHHALYDGWSLPRILH 4250
Cdd:PRK12316  1623 LQVIHKQVElpFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLlrlvlvrTGEGRHhLIYTNHHILMDGWSNAQLLG 1702
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4251 AVKQAYSG-VVLERQPSFNAFIQYLSQQDPEAAAAYWqtalvdcKAALFPTLPPTVTQPVADTTVE-------YQCPPPS 4322
Cdd:PRK12316  1703 EVLQRYAGqPVAAPGGRYRDYIAWLQRQDAAASEAFW-------KEQLAALEEPTRLAQAARTEDGqvgygdhQQLLDPA 1775
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4323 QSAT--------DITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQTVFAFL 4394
Cdd:PRK12316  1776 QTRAlaefaraqKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWL 1855
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4395 QGVQQQATDMIAHEQTGLQRIAKMSpGARHACGFQTLLVVQ--PTDDVL--GSDDMLGEWRSYSEMQdfTTYALMVqCVL 4470
Cdd:PRK12316  1856 QEVQALNLALREHEHTPLYDIQRWA-GQGGEALFDSLLVFEnyPVAEALkqGAPAGLVFGRVSNHEQ--TNYPLTL-AVT 1931
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4471 VKDRVGVTASFDARVIEQWVVEKMLRQFGFVMQQLADAGEeKKVAGIETTTTGDRQQLWA-WNQDVPPA-IERCVHDQFA 4548
Cdd:PRK12316  1932 LGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQ-AALGELALLDAGERQRILAdWDRTPEAYpRGPGVHQRIA 2010
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4549 EQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 4628
Cdd:PRK12316  2011 EQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE 2090
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4629 RHEHIFRQTGAQVVLA-SAQYATLWTSLG-RSVVIVSEASTSQLPvvTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEH 4706
Cdd:PRK12316  2091 RLAYMLEDSGAALLLTqRHLLERLPLPAGvARLPLDRDAEWADYP--DTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSH 2168
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4707 KAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRR-NNLAKAINAMDVNWALLTPSVAR 4785
Cdd:PRK12316  2169 GALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDpEQLYDEMERHGVTILDFPPVYLQ 2248
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4786 ML------DPCVVqSLKILVLGGEQVNSADWDRWPKSIQT---INAYGPTECSICCTTYSGKQGFKSGT----IGTSIVS 4852
Cdd:PRK12316  2249 QLaehaerDGRPP-AVRVYCFGGEAVPAASLRLAWEALRPvylFNGYGPTEAVVTPLLWKCRPQDPCGAayvpIGRALGN 2327
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4853 VS-WVVDPENHnrLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygGHSGrqGRLYKTGDLVRYDADGN 4931
Cdd:PRK12316  2328 RRaYILDADLN--LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG--ERLYRTGDLARYRADGV 2396
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4932 LVYLGRKDSQVKLRGQRVELGEVEHHVR--ECLTEAKqlaveVIVPEGEGGyAMLAAFVqLGDDtyntlvkekaggdslt 5009
Cdd:PRK12316  2397 VEYLGRIDHQVKIRGFRIELGEIEARLQahPAVREAV-----VVAQDGASG-KQLVAYV-VPDD---------------- 2453
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5010 VQVVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREIGASFTAQQLAEmrtssqgpkrqPSTEAERTMQ 5089
Cdd:PRK12316  2454 AAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVA-----------PQEGLEQRLA 2522
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5090 QLWTRVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRT-GLQLSVADVFRHPRLVDLAYVQNSECSSAAEEVPAFSLL 5168
Cdd:PRK12316  2523 AIWQAVLKVE--QVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRV 2600
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5169 GGRAADTAQVSQdaaamcsvdassvedmypcsplqEGLMSLTAKRAGdYIMQSVLELRVDVDEDAFRAAWEHVVQLTAAL 5248
Cdd:PRK12316  2601 QPLPLSHAQQRQ-----------------------WFLWQLEPESAA-YHLPSALHLRGVLDQAALEQAFDALVLRHETL 2656
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5249 RTRIVQHSE--------LGLLQVVVEEKIQWTESKRLEEYLREDKAVSMGLGDRLARYALIKepYDGGKRWFVWTIHHAL 5320
Cdd:PRK12316  2657 RTRFVEVGEqtrqvilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLA--LDGQEHVLVITQHHIV 2734
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5321 YDGWSLPRILQAVKQIYSGAVPERQPSFNAFI-----------QYLGQQDLEAATLYWQTAL--ADCKAALFPTLPPTVT 5387
Cdd:PRK12316  2735 SDGWSMQVMVDELVQAYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLggEQPVLELPLDRPRPAL 2814
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5388 QPVADTTVEYQCPPP-------SQSATDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGVEAMVGPTIATVP 5460
Cdd:PRK12316  2815 QSHRGARLDVALDVAlsrellaLARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQV 2892
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5461 LRVCLQKDQTVSTLLECLQQQSTDMIAHEQTGL-QRIAKMSP--GARHACGFQTLLVVQPTD----DVLGSDDMLGEWRS 5533
Cdd:PRK12316  2893 LRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFeQLVEALQPerSLSHSPLFQVMYNHQSGEraaaQLPGLHIESFAWDG 2972
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5534 YSEMQDFTTYALMVQCTLAKDRVEVTASFDARVIEQwvvekMLRQFGFVMQQLAEaGAEKTVSDIETTTLEDRQQ-LWAW 5612
Cdd:PRK12316  2973 AATQFDLALDTWESAEGLGASLTYATDLFDARTVER-----LARHWQNLLRGMVE-NPQRSVDELAMLDAEERGQlLEAW 3046
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5613 NQN-VPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLA 5691
Cdd:PRK12316  3047 NATaAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLA 3126
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5692 VLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSaQHSARWIGTNHQVVTVSAGSLGQLSTlvNPVGLpAIPENAVYIM 5771
Cdd:PRK12316  3127 ILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ-SHLRLPLAQGVQVLDLDRGDENYAEA--NPAIR-TMPENLAYVI 3202
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5772 FTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCIcVPSDSDRRNDLVKAIS 5851
Cdd:PRK12316  3203 YTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV-VLAGPEDWRDPALLVE 3281
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5852 TMDVSCALLTPSVARLLE-------PSSVPTLQMLVLQGEQVSFADWNRWPASVQTINGYGPTECSICCNTYSGKQGFKS 5924
Cdd:PRK12316  3282 LINSEGVDVLHAYPSMLQafleeedAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKD 3361
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5925 GI-IGTSVASVSWVVDPENHDRlAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypgHPGrqGRLYKTGD 6003
Cdd:PRK12316  3362 AVpIGRPIANRACYILDGSLEP-VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF--------VPG--ERLYRTGD 3430
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6004 LVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQLAVEVIlpsgqkDHAMLAAFVQLEegtqnallDKE 6083
Cdd:PRK12316  3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEH-PWVREAVVLAV------DGRQLVAYVVPE--------DEA 3495
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6084 ASGEDSMAqvvflasveEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQIAnmqtssqdpkrQPST 6163
Cdd:PRK12316  3496 GDLREALK---------AHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVN 3555
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6164 EAEQTMQKLWAQVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRIGLQLSVADIFRYARLVDLAsldtsqcnsaigev 6243
Cdd:PRK12316  3556 ELERRLAAIWADVLKLE--QVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLA-------------- 3619
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6244 PAFSLLGGRAADTAQVSQDAAAMcsvdassvedmypcsPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVV 6323
Cdd:PRK12316  3620 RVARVGGGVAVDQGPVSGETLLL---------------PIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALV 3684
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6324 QLTAALRTRIVQ---HSELGLLQVVVEEKIQW---TESKRLEEYLREDKAVSMGLGD-PLARYAIIKEAWGGKRwFVWTI 6396
Cdd:PRK12316  3685 EHHDALRLRFVEdagGWTAEHLPVELGGALLWraeLDDAEELERLGEEAQRSLDLADgPLLRALLATLADGSQR-LLLVI 3763
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6397 HHALYDGWSLPRVLQAVKQAYnGAVLETQP--------SFNAFIQ----YLSQQDLEATAAYWQTALADCEATLFPPLPS 6464
Cdd:PRK12316  3764 HHLVVDGVSWRILLEDLQQAY-QQLLQGEAprlpaktsSFKAWAErlqeHARGEALKAELAYWQEQLQGVSSELPCDHPQ 3842
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6465 SVKQLVADTTVehQCPLPSRSTSDTTTST----------LIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTSID--AIV 6532
Cdd:PRK12316  3843 GALQNRHAASV--QTRLDRELTRRLLQQApaayrtqvndLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDlsRTV 3920
                         2570
                   ....*....|.
gi 1820002560 6533 GPTIATVPLRV 6543
Cdd:PRK12316  3921 GWFTSLFPVRL 3931
PRK12467 PRK12467
peptide synthase; Provisional
3061-5378 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 793.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3061 LARLQQAWKGVVHQHSLLRTLLVDNvpgSTGTTNVVLKD---PQPSISVFSSEGTATIELFRSRYNPAAQRSIgQLQH-- 3135
Cdd:PRK12467    86 VSALRRAFDALVARHESLRTRFVQD---EEGFRQVIDASlslTIPLDDLANEQGRARESQIEAYINEEVARPF-DLANgp 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3136 --HLSICQLNNGKVYLCLDINHAIIDAHSRGILMHDLQEAYDANLNPQSTS-------FRDFAsyIKQQSQEEAG----- 3201
Cdd:PRK12467   162 llRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSlpalpiqYADYA--IWQRSWLEAGererq 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3202 -RYWAEYLDGVEPCF-------FPSLGDSGGANTiprTVEVPSIDSSAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTN 3273
Cdd:PRK12467   240 lAYWQEQLGGEHTVLelptdrpRPAVPSYRGARL---RVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSD 316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3274 PCFGnlssgrdLPIHNVN-----SIFGPLISILPCRIHLHKQLTVLEALKTVQENYASSLSFQTFPLASMHSFL----GL 3344
Cdd:PRK12467   317 IRIG-------VPNANRNrveteRLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALqperSL 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3345 GTSALFNTALSLQRIDDIGPCS-ASEITLKMKEGLDP----TEYNITLSAGYSKDAIDISMTFRAGCMDLVQAKRLASNF 3419
Cdd:PRK12467   390 SHSPLFQVMFNHQNTATGGRDReGAQLPGLTVEELSWarhtAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHW 469
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3420 SQAIKAVTTEPHSRIYSLDILTYNESKK-IWGWNADVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSK 3498
Cdd:PRK12467   470 RNLLEAIVAEPRRRLGELPLLDAEERAReLVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANR 549
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3499 LASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARW---TSS 3575
Cdd:PRK12467   550 LAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLpvpAGL 629
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3576 SCHVVTVSKALSSQLPAVvdSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYT 3655
Cdd:PRK12467   630 RSLCLDEPADLLCGYSGH--NPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFA 707
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3656 FDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL----DPGLIPSLKILAIGGEQSSSAD 3729
Cdd:PRK12467   708 FDLGVTELFGALASGATLHLLPPDCARDaeAFAALMADQGVTVLKIVPSHLQALlqasRVALPRPQRALVCGGEALQVDL 787
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3730 WNRW----PGsVQKIHVYGPTECCIFCTGYTTK---QGFEPSTIGTSVASVSWVVdPENHNRLAPLGSMGELLMEGPILA 3802
Cdd:PRK12467   788 LARVralgPG-ARLINHYGPTETTVGVSTYELSdeeRDFGNVPIGQPLANLGLYI-LDHYLNPVPVGVVGELYIGGAGLA 865
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3803 RGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcL 3882
Cdd:PRK12467   866 RGYHRRPALTAERFVPDPF-------GADG--GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLA-Q 935
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3883 PEARQLAVEVILPSGqkdHAMLAAFVQleegtqnalldkEAGGEDSMAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFP 3962
Cdd:PRK12467   936 PGVREAVVLAQPGDA---GLQLVAYLV------------PAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLP 1000
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3963 TTTSGKTDRKRLREIGASftaqqlaemrtSSQGPKRQPSTEAEQTMQQLWAQVlsLGADIIGLDDSFFRLGGDSIAAMKL 4042
Cdd:PRK12467  1001 LTPNGKLDRKALPKPDAS-----------AVQATFVAPQTELEKRLAAIWADV--LKVERVGLTDNFFELGGHSLLATQV 1067
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4043 VGEARR-MGLHLSVADIFRHPKLADFAGIQITQCSSgteEVPAYSLLGEDEDVmqvckdvaamcsvdasaitdvyPCSPL 4121
Cdd:PRK12467  1068 ISRVRQrLGIQVPLRTLFEHQTLAGFAQAVAAQQQG---AQPALPDVDRDQPL----------------------PLSYA 1122
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4122 QEG---LMSLTAKRAGdYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSElGLLQVVVEERIQWTESESLEE 4198
Cdd:PRK12467  1123 QERqwfLWQLEPGSAA-YHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDG-RTRQVIHPVGSLTLEEPLLLA 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4199 YPREDKAVSMGVGDR-----------LARYALIkePYDGGKRWFVWTMHHALYDGWSLPRILHAVKQAYSGVVLERQPSF 4267
Cdd:PRK12467  1201 ADKDEAQLKVYVEAEarqpfdleqgpLLRVGLL--RLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQL 1278
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4268 NAF-IQY----------LSQQDPEAAAAYWQTALVDCKAAL-FPT-LPPTVTQPVADTTVEYQCPPPSQSA-------TD 4327
Cdd:PRK12467  1279 PALpIQYadyavwqrqwMDAGERARQLAYWKAQLGGEQPVLeLPTdRPRPAVQSHRGARLAFELPPALAEGlralarrEG 1358
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4328 ITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNApiAGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQATDMIAH 4407
Cdd:PRK12467  1359 VTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNR--AETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAH 1436
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4408 -----EQ--TGLQRIAKMSpgarHACGFQTLLVVQpTDDVLGSDDMLG------EWRSYSEMQDFT--TYalmvqcvlvK 4472
Cdd:PRK12467  1437 qdlpfEQlvEALQPERSLS----HSPLFQVMFNHQ-RDDHQAQAQLPGlsveslSWESQTAQFDLTldTY---------E 1502
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4473 DRVGVTAS-------FDARVIeqwvvEKMLRQFGFVMQQLAdAGEEKKVAGIETTTTGDRQQ-LWAWNQ---DVPPAieR 4541
Cdd:PRK12467  1503 SSEGLQASltyatdlFEASTI-----ERLAGHWLNLLQGLV-ADPERRLGELDLLDEAERRQiLEGWNAthtGYPLA--R 1574
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4542 CVHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL 4621
Cdd:PRK12467  1575 LVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPL 1654
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4622 DPDHPASRHEHIFRQTGAQVVLA-SAQYATLWTSLG-RSVVIVSEASTSQlpvvtktADPSVNPGNA------AYAIFTS 4693
Cdd:PRK12467  1655 DPEYPRERLAYMIEDSGIELLLTqSHLQARLPLPDGlRSLVLDQEDDWLE-------GYSDSNPAVNlapqnlAYVIYTS 1727
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4694 GSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRN--NLAKAINA 4771
Cdd:PRK12467  1728 GSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDpeQLIQLIER 1807
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4772 MDVNWALLTPSVARML---DPCVVQ--SLKILVLGGE--QVNSAD--WDRWPKSiQTINAYGPTECSICCT----TYSGK 4838
Cdd:PRK12467  1808 QQVTTLHFVPSMLQQLlqmDEQVEHplSLRRVVCGGEalEVEALRpwLERLPDT-GLFNLYGPTETAVDVThwtcRRKDL 1886
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4839 QGFKSGTIGTSIVSVSW-VVDPENHnrLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawllEGYGGhsgrqGRL 4917
Cdd:PRK12467  1887 EGRDSVPIGQPIANLSTyILDASLN--PVPIGVAGELYLGGVGLARGYLNRPALTAERFVADP----FGTVG-----SRL 1955
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4918 YKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREcltEAKQLAVEVIVPEGEGGyAMLAAFVqlgddtynt 4997
Cdd:PRK12467  1956 YRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLRE---QGGVREAVVIAQDGANG-KQLVAYV--------- 2022
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4998 LVKEKAGGDSLTVQVVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREIGASftaqqlaEMRTSSQGPK 5077
Cdd:PRK12467  2023 VPTDPGLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS-------ELQQAYVAPQ 2095
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5078 rqpsTEAERTMQQLWTRVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRTGLQLSVADVFRHPRLVDLAYVqnsecss 5157
Cdd:PRK12467  2096 ----SELEQRLAAIWQDVLGLE--QVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAV------- 2162
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5158 aaeevpafsllggraadtAQVSQDAAamcSVDASSVEDMYPCSPLQEGLMSLTAKRAGDYIMQSVLELRvdvdeDAFRAA 5237
Cdd:PRK12467  2163 ------------------AQEGDGTV---SIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPR-----EALDAE 2216
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5238 WehvvqLTAALRTRIVQHSELGLlqVVVEEKIQWTESKRLEEYLRE---------DKAVSMGLGDRLAR----------Y 5298
Cdd:PRK12467  2217 L-----LEAALQALLVHHDALRL--GFVQEDGGWSAMHRAPEQERRpllwqvvvaDKEELEALCEQAQRsldleegpllR 2289
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5299 ALIKEPYDGGKRwFVWTIHHALYDGWSLpRIL-----QAVKQIYSGA---VPERQPSFNAFIQ----YLGQQDLEAATLY 5366
Cdd:PRK12467  2290 AVLATLPDGSQR-LLLVIHHLVVDGVSW-RILledlqTAYRQLQGGQpvkLPAKTSAFKAWAErlqtYAASAALADELGY 2367
                         2490
                   ....*....|..
gi 1820002560 5367 WQTALADCKAAL 5378
Cdd:PRK12467  2368 WQAQLQGASTEL 2379
PRK12467 PRK12467
peptide synthase; Provisional
4136-6453 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 790.13  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4136 YIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSElGLLQVVVEE-RIQWTESESLEEYPREDKA-VSMGVGDR 4213
Cdd:PRK12467    72 YNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEE-GFRQVIDASlSLTIPLDDLANEQGRARESqIEAYINEE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4214 LAR-YALIKEPY--------DGGKRWFVWTMHHALYDGWSLPRILHAVKQAYSGVVLERQPSFNAF-IQY---------- 4273
Cdd:PRK12467   151 VARpFDLANGPLlrvrllrlADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALpIQYadyaiwqrsw 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4274 LSQQDPEAAAAYWQTALVDCKAAL-FPTLPPTVTQP-VADTTVEYQCPPPSQSA-------TDITTSTLARAAWAIVTSR 4344
Cdd:PRK12467   231 LEAGERERQLAYWQEQLGGEHTVLeLPTDRPRPAVPsYRGARLRVDLPQALSAGlkalaqrEGVTLFMVLLASFQTLLHR 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4345 YTSSDDVVFGATVTGRNApiAGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQATDMIAHEQTGL-QRIAKMSP--G 4421
Cdd:PRK12467   311 YSGQSDIRIGVPNANRNR--VETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFeQLVEALQPerS 388
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4422 ARHACGFQTLLVVQPTddVLGSDDMLGEWRSYSEMQDFTTYALMVQCVLVKDR------VGVTASFDARVIEQWVVEKML 4495
Cdd:PRK12467   389 LSHSPLFQVMFNHQNT--ATGGRDREGAQLPGLTVEELSWARHTAQFDLALDTyesaqgLWAAFTYATDLFEATTIERLA 466
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4496 RQFGFVMQQLAdAGEEKKVAGIETTTTGDRQ-QLWAWNQDVPPAIERCVHDQFAEQARARPDTPAICAWDGELTYGELDT 4574
Cdd:PRK12467   467 THWRNLLEAIV-AEPRRRLGELPLLDAEERArELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNR 545
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4575 LSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLA-SAQYATLWT 4653
Cdd:PRK12467   546 QANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTqSHLLAQLPV 625
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4654 SLGRSVVIVSEASTSQLPVVTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFAS 4733
Cdd:PRK12467   626 PAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVST 705
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4734 YTFDACIAEIITTLLCCGCICVPSDSDRRN--NLAKAINAMDVNWALLTPSVARML--DPCVVQ--SLKILVLGGE--QV 4805
Cdd:PRK12467   706 FAFDLGVTELFGALASGATLHLLPPDCARDaeAFAALMADQGVTVLKIVPSHLQALlqASRVALprPQRALVCGGEalQV 785
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4806 N-SADWDRWPKSIQTINAYGPTECSICCTTYS-GKQGFKSGT--IGTSIVSVSWVVdPENHNRLAPLGSIGELLVEGPIL 4881
Cdd:PRK12467   786 DlLARVRALGPGARLINHYGPTETTVGVSTYElSDEERDFGNvpIGQPLANLGLYI-LDHYLNPVPVGVVGELYIGGAGL 864
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4882 ARGYLNDMEKTEAAFIDDPawllegygghSGRQG-RLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVRE 4960
Cdd:PRK12467   865 ARGYHRRPALTAERFVPDP----------FGADGgRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLA 934
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4961 clTEAKQLAVeVIVPEGEGGYAMLAAFVqlgddtyntlvkeKAGGDSLTVQVVFLDRVEEELAKRVPEHMMLTTFFTLEA 5040
Cdd:PRK12467   935 --QPGVREAV-VLAQPGDAGLQLVAYLV-------------PAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDS 998
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5041 MPTTTSGKIDRKRLREIGASftaqqlaemrtSSQGPKRQPSTEAERTMQQLWTRVLGIElnGIGLDDSFFRLGGDSIAAM 5120
Cdd:PRK12467   999 LPLTPNGKLDRKALPKPDAS-----------AVQATFVAPQTELEKRLAAIWADVLKVE--RVGLTDNFFELGGHSLLAT 1065
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5121 KLVGEARRT-GLQLSVADVFRHPRLVDLAYVQNSECSSAAEEVPafsllggraadtaQVSQDAAAmcsvdassvedmyPC 5199
Cdd:PRK12467  1066 QVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALP-------------DVDRDQPL-------------PL 1119
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5200 SPLQEG---LMSLTAKRAGdYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGL------LQVVVEEK-- 5268
Cdd:PRK12467  1120 SYAQERqwfLWQLEPGSAA-YHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRqvihpvGSLTLEEPll 1198
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5269 -IQWTESKRLEEYLREDKAVSMGL-GDRLARYALIkePYDGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGAVPERQP 5346
Cdd:PRK12467  1199 lAADKDEAQLKVYVEAEARQPFDLeQGPLLRVGLL--RLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSL 1276
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5347 SFNAF-IQYL------------GQQDLEAAtlYWQTALADCKAAL-FPT-LPPTVTQPVADTTVEYQCPPPSQSA----- 5406
Cdd:PRK12467  1277 QLPALpIQYAdyavwqrqwmdaGERARQLA--YWKAQLGGEQPVLeLPTdRPRPAVQSHRGARLAFELPPALAEGlrala 1354
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5407 --TDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNApiAGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTD 5484
Cdd:PRK12467  1355 rrEGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNR--AETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALE 1432
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5485 MIAH-----EQ--TGLQRIAKMSpgarHACGFQTLLVVQpTDDVLGSDDMLG------EWRSYSEMQDFT------TYAL 5545
Cdd:PRK12467  1433 AQAHqdlpfEQlvEALQPERSLS----HSPLFQVMFNHQ-RDDHQAQAQLPGlsveslSWESQTAQFDLTldtyesSEGL 1507
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5546 MVQCTLAKDRVEVTAsfdarvieqwvVEKMLRQFGFVMQQLAeAGAEKTVSDIETTTLEDRQQ-LWAWNQnvPPA---IE 5621
Cdd:PRK12467  1508 QASLTYATDLFEAST-----------IERLAGHWLNLLQGLV-ADPERRLGELDLLDEAERRQiLEGWNA--THTgypLA 1573
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5622 RCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVP 5701
Cdd:PRK12467  1574 RLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5702 LDPDHPASRHEDTFRHTGAQVVVTSAQHSARW-IGTNHQVVTVSAGSlGQLST--LVNPVGLPAiPENAVYIMFTSGSTG 5778
Cdd:PRK12467  1654 LDPEYPRERLAYMIEDSGIELLLTQSHLQARLpLPDGLRSLVLDQED-DWLEGysDSNPAVNLA-PQNLAYVIYTSGSTG 1731
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5779 IPKGVVLEHRAVVTS-CWGRgRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRN--DLVKAISTMDV 5855
Cdd:PRK12467  1732 RPKGAGNRHGALVNRlCATQ-EAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDpeQLIQLIERQQV 1810
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5856 SCALLTPS--------VARLLEPSSvptLQMLVLQGEQVSFADWNRWPAS---VQTINGYGPTECSI------CcnTYSG 5918
Cdd:PRK12467  1811 TTLHFVPSmlqqllqmDEQVEHPLS---LRRVVCGGEALEVEALRPWLERlpdTGLFNLYGPTETAVdvthwtC--RRKD 1885
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5919 KQGFKSGIIGTSVASVSW-VVDPENHdrLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypGHPGrqGR 5997
Cdd:PRK12467  1886 LEGRDSVPIGQPIANLSTyILDASLN--PVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPF-------GTVG--SR 1954
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5998 LYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVRE--CLPEARQLAVEVilPSGQKdhamLAAFVqleegt 6075
Cdd:PRK12467  1955 LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREqgGVREAVVIAQDG--ANGKQ----LVAYV------ 2022
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6076 qnaLLDKEASGEDSMAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASftaqqianmqtSSQ 6155
Cdd:PRK12467  2023 ---VPTDPGLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS-----------ELQ 2088
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6156 DPKRQPSTEAEQTMQKLWAQVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRIGLQLSVADIFRYARLVDLASldtsq 6235
Cdd:PRK12467  2089 QAYVAPQSELEQRLAAIWQDVLGLE--QVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAA----- 2161
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6236 cnsaigevpafsllggraadtaqVSQDAAAMCSVDASSVEDMYPCSPLQEGLMSLTAKRAGDYIMQSVLELRvdvdeDAF 6315
Cdd:PRK12467  2162 -----------------------VAQEGDGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPR-----EAL 2213
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6316 RAAWehvvqLTAALRTRIVQHSELGLlqVVVEEKIQWTESKRLEEYLRED-------------KAV------SMGLGD-P 6375
Cdd:PRK12467  2214 DAEL-----LEAALQALLVHHDALRL--GFVQEDGGWSAMHRAPEQERRPllwqvvvadkeelEALceqaqrSLDLEEgP 2286
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6376 LARYAIIKEAWGGKRwFVWTIHHALYDGWSLpRVL-----QAVKQAYNGAVLE---TQPSFNAFIQYLSQQ----DLEAT 6443
Cdd:PRK12467  2287 LLRAVLATLPDGSQR-LLLVIHHLVVDGVSW-RILledlqTAYRQLQGGQPVKlpaKTSAFKAWAERLQTYaasaALADE 2364
                         2490
                   ....*....|
gi 1820002560 6444 AAYWQTALAD 6453
Cdd:PRK12467  2365 LGYWQAQLQG 2374
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
3463-3982 0e+00

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 759.00  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3463 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 3542
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3543 PDHPASRHEEIFEQTGAQVVVASaqysarwtssschvvtvskalssqlpavvdstntsvRPENAAYIIFTSGSTGVPKGV 3622
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3623 VLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFLTPS 3702
Cdd:cd05918    125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3703 VARLLDPGLIPSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPSTIGTSVASVSWVVDPENH 3782
Cdd:cd05918    205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNH 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3783 NRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAWLLEgypGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQV 3862
Cdd:cd05918    285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQ---EGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3863 KVRGQRVELGEVEHHVRECLPEARQLAVEVILPSGQKDHAMLAAFVQLEEGTQNALLDKEAGGEDSMAQVVFLASVEEEL 3942
Cdd:cd05918    362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKL 441
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 3943 AKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFT 3982
Cdd:cd05918    442 RQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
PRK12316 PRK12316
peptide synthase; Provisional
5176-7448 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 756.41  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5176 AQVSQDAAAMCSVDASSVEDMYPCSPLQEGLM--SLTAKRAGDYIMQsvleLRVDV---DEDAFRAAWEHVVQLTAALRT 5250
Cdd:PRK12316  1536 AGLSQAQLDALPLPAGEIADIYPLSPMQQGMLfhSLYEQEAGDYINQ----LRVDVqglDPDRFRAAWQATVDRHEILRS 1611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5251 RIVQHSELGLLQVVVEEKIQ-------WTESKRLEEYLRedkavSMGLGDRLARYALIKEPY-------DGGKRW-FVWT 5315
Cdd:PRK12316  1612 GFLWQDGLEQPLQVIHKQVElpfaeldWRGREDLGQALD-----ALAQAERQKGFDLTRAPLlrlvlvrTGEGRHhLIYT 1686
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5316 IHHALYDGWSLPRILQAVKQIYSG-AVPERQPSFNAFIQYLGQQDLEAATLYWQTALAdckaalfPTLPPTVTQPVADTT 5394
Cdd:PRK12316  1687 NHHILMDGWSNAQLLGEVLQRYAGqPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLA-------ALEEPTRLAQAARTE 1759
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5395 VE-------YQCPPPSQSAT--------DITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGVEAMVGPTIATV 5459
Cdd:PRK12316  1760 DGqvgygdhQQLLDPAQTRAlaefaraqKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTL 1839
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5460 PLRVCLQKDQTVSTLLECLQQQSTDMIAHEQTGLQRIAKMSpGARHACGFQTLLVVQ--PTDDVL--GSDDMLGEWRSYS 5535
Cdd:PRK12316  1840 PVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWA-GQGGEALFDSLLVFEnyPVAEALkqGAPAGLVFGRVSN 1918
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5536 EMQdfTTYALMVQCTLAkDRVEVTASFDARVIEQWVVEKMLRQFGFVMQQLAEAgAEKTVSDIETTTLEDRQQLWAWNQN 5615
Cdd:PRK12316  1919 HEQ--TNYPLTLAVTLG-ETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAED-AQAALGELALLDAGERQRILADWDR 1994
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5616 VPPAIER--CVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVL 5693
Cdd:PRK12316  1995 TPEAYPRgpGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVL 2074
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5694 KAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSAQHSARwIGTNHQVVTVSAGSLGQLSTLvnPVGLPAI---PENAVYI 5770
Cdd:PRK12316  2075 KAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLER-LPLPAGVARLPLDRDAEWADY--PDTAPAVqlaGENLAYV 2151
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5771 MFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRR-NDLVKA 5849
Cdd:PRK12316  2152 IYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDpEQLYDE 2231
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5850 ISTMDVSCALLTPSVARLL-EPSSV----PTLQMLVLQGEQVSFADWNRWPASVQT---INGYGPTECSI------CCNT 5915
Cdd:PRK12316  2232 MERHGVTILDFPPVYLQQLaEHAERdgrpPAVRVYCFGGEAVPAASLRLAWEALRPvylFNGYGPTEAVVtpllwkCRPQ 2311
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5916 YSGkqGFKSGIIGTSVASVS-WVVDPENHdrLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypGHPGr 5994
Cdd:PRK12316  2312 DPC--GAAYVPIGRALGNRRaYILDADLN--LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG- 2379
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5995 qGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVR--ECLPEARQLAVEVilPSGQKdhamLAAFVqle 6072
Cdd:PRK12316  2380 -ERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQahPAVREAVVVAQDG--ASGKQ----LVAYV--- 2449
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6073 egtqnalldkeaSGEDsmAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASftaqqianmqt 6152
Cdd:PRK12316  2450 ------------VPDD--AAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVS----------- 2504
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6153 SSQDPKRQPSTEAEQTMQKLWAQVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARR-IGLQLSVADIFRYARLVDLASL 6231
Cdd:PRK12316  2505 QLRQAYVAPQEGLEQRLAAIWQAVLKVE--QVGLDDHFFELGGHSLLATQVVSRVRQdLGLEVPLRILFERPTLAAFAAS 2582
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6232 DTSQCNSaigevpafsllggRAADTAQVSQDAAAMCSVDASSvedmypcsplQEGLMSLTAKRAGdYIMQSVLELRVDVD 6311
Cdd:PRK12316  2583 LESGQTS-------------RAPVLQKVTRVQPLPLSHAQQR----------QWFLWQLEPESAA-YHLPSALHLRGVLD 2638
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6312 EDAFRAAWEHVVQLTAALRTRIVQHSE--------LGLLQVVVEEKIQWTESKRLEEYLREDKAVSMGLGDPLARyAIIK 6383
Cdd:PRK12316  2639 QAALEQAFDALVLRHETLRTRFVEVGEqtrqvilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLR-VRLL 2717
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6384 EAWGGKRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSFNAFI-----------QYLSQQDLEATAAYWQTALA 6452
Cdd:PRK12316  2718 ALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLG 2797
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6453 DCEATLFPPL--PSSVKQLVADTTVEHQCPLP-------SRSTSDTTTSTLIRAAWAIVASRYTSSDDVVFGTTITGRNA 6523
Cdd:PRK12316  2798 GEQPVLELPLdrPRPALQSHRGARLDVALDVAlsrellaLARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNR 2877
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6524 PVTsiDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEMIAYEQTGLQQIAKM---GPDPQHACGFQTLLVVQ---- 6596
Cdd:PRK12316  2878 AET--ERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEAlqpERSLSHSPLFQVMYNHQsger 2955
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6597 PAGDVLGSDDTLGKWRGYSGLQDfmtyaLGVRCTLSAEGVKITASFDARVIEHWVVEKMLGQFSFAMQQLAEaSADRKVA 6676
Cdd:PRK12316  2956 AAAQLPGLHIESFAWDGAATQFD-----LALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVE-NPQRSVD 3029
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6677 DIDITTTTDRQQ-LWAWN---AELPLAvdRCVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPE 6752
Cdd:PRK12316  3030 ELAMLDAEERGQlLEAWNataAEYPLE--RGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPD 3107
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6753 DVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR-----------------HEDILRQTGAQVILASAQNTTLFQS 6815
Cdd:PRK12316  3108 VLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERlaymledsgaqlllsqsHLRLPLAQGVQVLDLDRGDENYAEA 3187
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6816 SNQTVVTVNRSSYILFPD-------------------------------------------------------------- 6833
Cdd:PRK12316  3188 NPAIRTMPENLAYVIYTSgstgkpkgvgirhsalsnhlcwmqqayglgvgdrvlqfttfsfdvfveelfwplmsgarvvl 3267
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560      --------------------------------------------------------------------------------
Cdd:PRK12316  3268 agpedwrdpallvelinsegvdvlhaypsmlqafleeedahrctslkrivcggealpadlqqqvfaglplynlygpteat 3347
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6834 ---------ENREAYPFVRPSNAALA-----------PLGSIGELLVEGPILARGYLNDADKTAAAFVNDPawLVEGhgk 6893
Cdd:PRK12316  3348 itvthwqcvEEGKDAVPIGRPIANRAcyildgslepvPVGALGELYLGGEGLARGYHNRPGLTAERFVPDP--FVPG--- 3422
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6894 hpgrrGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcmpratqmaVEVISPAGAAEQAKTMVVAF 6973
Cdd:PRK12316  3423 -----ERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLE---------HPWVREAVVLAVDGRQLVAY 3488
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6974 LQLNDEARDAllggnvpnddnlsaqvvfPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREIGASFTAQQL 7053
Cdd:PRK12316  3489 VVPEDEAGDL------------------REALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDY 3550
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7054 AemrtssqgpkrQPSTEAERTMQQLWARMLKVkaDSIGLDDSFFRLGGDSIVAMKLVGEARRTGLQLSVADVFRHPRLVD 7133
Cdd:PRK12316  3551 V-----------APVNELERRLAAIWADVLKL--EQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQG 3617
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7134 LAYVQNSQCSSAAEEVPafsLLGEDvnpvqlsqdaaamcsvaasivkdiyPCSPLQEGLISLTAKRAGDYIMQSVLELRA 7213
Cdd:PRK12316  3618 LARVARVGGGVAVDQGP---VSGET-------------------------LLLPIQQQFFEEPVPERHHWNQSLLLKPRE 3669
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7214 DVDEDVFCAAWEHVVQSTAALRTRIVQ---HSELGLLQVVVEEKIQW----TESEALEEyLKEDKAVSMGLGD-PLAHYA 7285
Cdd:PRK12316  3670 ALDAAALEAALQALVEHHDALRLRFVEdagGWTAEHLPVELGGALLWraelDDAEELER-LGEEAQRSLDLADgPLLRAL 3748
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7286 LVKEAWGGKRwFVWTIHHALYDGGSLPLILHAVKQVYsGAVLERQP--------SFNAFIQ----YLGQQDLEATAAYWQ 7353
Cdd:PRK12316  3749 LATLADGSQR-LLLVIHHLVVDGVSWRILLEDLQQAY-QQLLQGEAprlpaktsSFKAWAErlqeHARGEALKAELAYWQ 3826
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7354 TALSDCEAVLFPPLPSTVTQPVADTTVE--------YQCPPLSKATLDTTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTG 7425
Cdd:PRK12316  3827 EQLQGVSSELPCDHPQGALQNRHAASVQtrldreltRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHG 3906
                         2570      2580
                   ....*....|....*....|....*
gi 1820002560 7426 RNAPIAGVE--AMVGPTIATVPVRL 7448
Cdd:PRK12316  3907 REDLFADIDlsRTVGWFTSLFPVRL 3931
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1931-2450 0e+00

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 752.07  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1931 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 2010
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2011 PDHPASRHEDIFRQTGAQVVVTSaqhsarwigtnhqvvtvsagsleqfstlvnpvdlpaKPENAAYVMFTSGSTGTPKGV 2090
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2091 VLEHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRDNLAKAITDMQVNWGYLTSS 2170
Cdd:cd05918    125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2171 VARLLDPCLVPSLKVLVLGGEQVNSTDWGKWPSSVQTINGYGPTECCVFCTGYTGIQGFQSGNIGTSIASVSWVVDPENH 2250
Cdd:cd05918    205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNH 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2251 GRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAWLLEGYPgheGRQGRLYKTGDLVRYSSDGNLVCLGRKDSQV 2330
Cdd:cd05918    285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQEGS---GRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2331 KVRGQRVELGEVEHHMRKCLPEANQLAVEVVPPSGERDHAMLAAFIRLDDETRNSPLIIKYAEDNSTAQIVFLTGIEEEL 2410
Cdd:cd05918    362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKL 441
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 2411 SERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREIGASFT 2450
Cdd:cd05918    442 RQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
7609-8128 0e+00

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 749.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7609 VHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 7688
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7689 PDHPASRHEEIFEQTGAQVVVASaqysarwtssschvvtvskalssqlpavvdstntsvRPENAAYIIFTSGSTGVPKGV 7768
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7769 VLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFLTPS 7848
Cdd:cd05918    125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7849 VARLLDPGLIPSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPSTIGTSVASVSWVVDPENH 7928
Cdd:cd05918    205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNH 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7929 NRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAWLLEgypGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQV 8008
Cdd:cd05918    285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQ---EGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8009 KVRGQRVELGEVEHHVRECLPEARQLAVEVILPSGQKNHAMLAVFVQLGKGTHIAHLEEKAGGEDSMAQVVFLTGTEEEL 8088
Cdd:cd05918    362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKL 441
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 8089 AKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGASFT 8128
Cdd:cd05918    442 RQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
4543-5062 0e+00

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 739.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4543 VHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 4622
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4623 PDHPASRHEHIFRQTGAQVVLASaqyatlwtslgrsvvivseastsqlpvvtktadpsvNPGNAAYAIFTSGSTGIPKGV 4702
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4703 VLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLAKAINAMDVNWALLTPS 4782
Cdd:cd05918    125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4783 VARMLDPCVVQSLKILVLGGEQVNSADWDRWPKSIQTINAYGPTECSICCTTYSGKQGFKSGTIGTSIVSVSWVVDPENH 4862
Cdd:cd05918    205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNH 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4863 NRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAWLLEgygGHSGRQGRLYKTGDLVRYDADGNLVYLGRKDSQV 4942
Cdd:cd05918    285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQ---EGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4943 KLRGQRVELGEVEHHVRECLTEAKQLAVEVIVPEGEGGYAMLAAFVQLGDDTyntlvKEKAGGDSLTVQV-----VFLDR 5017
Cdd:cd05918    362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSS-----SGSGDGDSLFLEPsdefrALVAE 436
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 5018 VEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREIGASFT 5062
Cdd:cd05918    437 LRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
854-1373 0e+00

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 737.04  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 933
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 PGHPASRHEEIFKQIGAQVVLTSsqhamlfasserhqvtvskvstsqlptvvnfakspvDPGNTAYIIFTSGTTGIPKGV 1013
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1014 VLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNNLAKAISTMDVNCALLTPS 1093
Cdd:cd05918    125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1094 VARLLEPSAVPSLKRLVLQGEQVSFADWNRWPGSVQTINGYGPTECSVCCNTYSGKQGFKSGIIGTSVASLSWVVDAGNH 1173
Cdd:cd05918    205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNH 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1174 NRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAWLLegyEGHAGRRGRLYKTGDLVRCDADGNLVCLGRKDSQV 1253
Cdd:cd05918    285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLK---QEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1254 KVRGQRVELGEIEHHVRECLPEARQLAVEVILPSGQKEHALLAAFIQLDKGNHNALFEEKASGEDSMAQVVFLTGVEEEL 1333
Cdd:cd05918    362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKL 441
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 1334 AKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDIGASFT 1373
Cdd:cd05918    442 RQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
5624-6143 0e+00

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 734.73  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5624 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 5703
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5704 PDHPASRHEDTFRHTGAQVVVTSAqhsarwigtnhqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKGV 5783
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTSS------------------------------------PSDAAYVIFTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5784 VLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRNDLVKAISTMDVSCALLTPS 5863
Cdd:cd05918    125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5864 VARLLEPSSVPTLQMLVLQGEQVSFADWNRWPASVQTINGYGPTECSICCNTYSGKQGFKSGIIGTSVASVSWVVDPENH 5943
Cdd:cd05918    205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNH 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5944 DRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAWLLEgypGHPGRQGRLYKTGDLVRYDANGNLVCLGRKDSQV 6023
Cdd:cd05918    285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQ---EGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6024 KLRGQRVELGEVEHHVRECLPEARQLAVEVILPSGQKDHAMLAAFVQLEEGTQNALLDKEASGEDSMAQVVFLASVEEEL 6103
Cdd:cd05918    362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKL 441
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 6104 AKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFT 6143
Cdd:cd05918    442 RQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
PRK12316 PRK12316
peptide synthase; Provisional
6257-8441 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 734.07  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6257 AQVSQDAAAMCSVDASSVEDMYPCSPLQEGLM--SLTAKRAGDYIMQsvleLRVDV---DEDAFRAAWEHVVQLTAALRT 6331
Cdd:PRK12316  1536 AGLSQAQLDALPLPAGEIADIYPLSPMQQGMLfhSLYEQEAGDYINQ----LRVDVqglDPDRFRAAWQATVDRHEILRS 1611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6332 RIVQHSELGLLQVVVEEKIQ-------WTESKRLEEYLREDKAVSMGLG-----DPLARYAIIKEawGGKRW-FVWTIHH 6398
Cdd:PRK12316  1612 GFLWQDGLEQPLQVIHKQVElpfaeldWRGREDLGQALDALAQAERQKGfdltrAPLLRLVLVRT--GEGRHhLIYTNHH 1689
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6399 ALYDGWSLPRVLQAVKQAYNG-AVLETQPSFNAFIQYLSQQDLEATAAYWQTALADCEAtlfpplPSSVKQLVA-----D 6472
Cdd:PRK12316  1690 ILMDGWSNAQLLGEVLQRYAGqPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEE------PTRLAQAARtedgqV 1763
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6473 TTVEHQCPLPSRSTSDTTT---------STLIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTSIDAIVGPTIATVPLRV 6543
Cdd:PRK12316  1764 GYGDHQQLLDPAQTRALAEfaraqkvtlNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIA 1843
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6544 RLQKDQTVSSFLGYLQQQATEMIAYEQTGLQQIAKMGPDPQHACgFQTLLVVQ--PAGDVLGSDDTLGKWRGYSGLQDFM 6621
Cdd:PRK12316  1844 APRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEAL-FDSLLVFEnyPVAEALKQGAPAGLVFGRVSNHEQT 1922
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6622 TYALGVRCTLsAEGVKITASFDARVIEHWVVEKMLGQFSFAMQQLAEaSADRKVADIDITTTTDRQQLWA-WN-AELPLA 6699
Cdd:PRK12316  1923 NYPLTLAVTL-GETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAE-DAQAALGELALLDAGERQRILAdWDrTPEAYP 2000
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6700 VDRCVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAF 6779
Cdd:PRK12316  2001 RGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY 2080
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6780 VPLDPDHPASRHEDILRQTGAQVIL---------------------------ASAQNTTLFQSSNQTVVTV--------- 6823
Cdd:PRK12316  2081 VPLDPNYPAERLAYMLEDSGAALLLtqrhllerlplpagvarlpldrdaewaDYPDTAPAVQLAGENLAYViytsgstgl 2160
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6824 --------------------------------------------------NRSSYILFPDENREAY-------------- 6839
Cdd:PRK12316  2161 pkgvavshgalvahcqaageryelspadcelqfmsfsfdgaheqwfhpllNGARVLIRDDELWDPEqlydemerhgvtil 2240
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6840 --------------------PFVR------------------------------------------------PSNAALAP 6851
Cdd:PRK12316  2241 dfppvylqqlaehaerdgrpPAVRvycfggeavpaaslrlawealrpvylfngygpteavvtpllwkcrpqdPCGAAYVP 2320
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6852 LGS---------------------IGELLVEGPILARGYLNDADKTAAAFVNDPAwlveghgKHPGrrGRLYKTGDLVYY 6910
Cdd:PRK12316  2321 IGRalgnrrayildadlnllapgmAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG--ERLYRTGDLARY 2391
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6911 NKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAGAaeqakTMVVAFLqlndeardallggnVP 6990
Cdd:PRK12316  2392 RADGVVEYLGRIDHQVKIRGFRIELGEIEARLQA-HPAVREAVVVAQDGASG-----KQLVAYV--------------VP 2451
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6991 NDdnlsAQVVFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREIGASFTAQQLAemrtssqgpkrQPSTE 7070
Cdd:PRK12316  2452 DD----AAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYV-----------APQEG 2516
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7071 AERTMQQLWARMLKVkaDSIGLDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADVFRHPRLVDLAYVQNSQCSSAAeev 7149
Cdd:PRK12316  2517 LEQRLAAIWQAVLKV--EQVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTSRA--- 2591
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7150 pafsllgEDVNPVQLSQDAAAMCSvaasivkdiypcSPLQEGLISLTAKRAGdYIMQSVLELRADVDEDVFCAAWEHVVQ 7229
Cdd:PRK12316  2592 -------PVLQKVTRVQPLPLSHA------------QQRQWFLWQLEPESAA-YHLPSALHLRGVLDQAALEQAFDALVL 2651
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7230 STAALRTRIVQHSE--------LGLLQVVVEEKIQWTESEALEEYLKEDKAVSMGLGDPLAHYALVKEAwGGKRWFVWTI 7301
Cdd:PRK12316  2652 RHETLRTRFVEVGEqtrqvilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALD-GQEHVLVITQ 2730
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7302 HHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAFI-----------QYLGQQDLEATAAYWQTALSDCEAVLFPPL--P 7368
Cdd:PRK12316  2731 HHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLGGEQPVLELPLdrP 2810
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7369 STVTQPVADTTVEYQCP-PLSKATLD------TTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPiaGVEAMVGPTI 7441
Cdd:PRK12316  2811 RPALQSHRGARLDVALDvALSRELLAlarregVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFV 2888
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7442 ATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIAKLGSGPR---HACGFQTLLVVQPVDDVLGSDDMLgEWRS 7518
Cdd:PRK12316  2889 NTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERslsHSPLFQVMYNHQSGERAAAQLPGL-HIES 2967
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7519 YSKMQDFTTYALMVQFTLAAEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLAEASEDSKVADIDTTTPEDRQQLWAWN 7598
Cdd:PRK12316  2968 FAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWN 3047
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7599 A-DVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAV 7677
Cdd:PRK12316  3048 AtAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAI 3127
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7678 LKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARwtssscHVVTVSKALSSQLPAVVDSTNTSVR--PENAAYI 7755
Cdd:PRK12316  3128 LKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLP------LAQGVQVLDLDRGDENYAEANPAIRtmPENLAYV 3201
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7756 IFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICV--PSDSDRRNSLAK 7833
Cdd:PRK12316  3202 IYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLagPEDWRDPALLVE 3281
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7834 AISTMDVNWAFLTPSVARLL----DPGLIPSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEP 7909
Cdd:PRK12316  3282 LINSEGVDVLHAYPSMLQAFleeeDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKD 3361
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7910 ST-IGTSVASVSWVVDPENHNRlAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypgHPGrqGRLYKTGD 7988
Cdd:PRK12316  3362 AVpIGRPIANRACYILDGSLEP-VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF--------VPG--ERLYRTGD 3430
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7989 LVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVevilpsgqknhamLAVFVQLGKGTHIAHLEEK 8068
Cdd:PRK12316  3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEH-PWVREAVV-------------LAVDGRQLVAYVVPEDEAG 3496
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8069 AGGEDSMAQvvfltgteeeLAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGASFTAQQLAetqtssqgpkrQPLT 8148
Cdd:PRK12316  3497 DLREALKAH----------LKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVN 3555
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8149 EAEQTMQQLWARVLGIDAdiIGLDDSFFRLGGDSIAAMKLVGEARRTGLQLSVADIFRHPRLIDLASLKSTFCNSVVEEV 8228
Cdd:PRK12316  3556 ELERRLAAIWADVLKLEQ--VGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQG 3633
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8229 PafsllspvmkdamfsvtepfgpslriddITDVVPASYIQQFYIATGVRAPREAFNYPFIDLSDAVDIQVLQASCSALLE 8308
Cdd:PRK12316  3634 P----------------------------VSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVE 3685
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8309 HFPILRTHFVYFQGkLYQVIPRHQDLPFSIF--------EVNGALAEESQaihiRDLD-QTSPLglpTSFTLVRNASGMN 8379
Cdd:PRK12316  3686 HHDALRLRFVEDAG-GWTAEHLPVELGGALLwraelddaEELERLGEEAQ----RSLDlADGPL---LRALLATLADGSQ 3757
                         2410      2420      2430      2440      2450      2460      2470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 8380 RLIIRLSHAQYDGVCMPVIWASLASIYQQ-----EPLL--STTGFHSYLAYVHNQRS-----ASINYWSRLLKG 8441
Cdd:PRK12316  3758 RLLLVIHHLVVDGVSWRILLEDLQQAYQQllqgeAPRLpaKTSSFKAWAERLQEHARgealkAELAYWQEQLQG 3831
PRK05691 PRK05691
peptide synthase; Validated
3743-6458 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 693.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3743 YGPTECCIFCTGYTTKQGF---------------EPSTiGTSVASVSW--------VVDPENHNRLAPlGSMGELLMEGP 3799
Cdd:PRK05691   328 YGLAEATLFVSGGRRGQGIpaleldaealarnraEPGT-GSVLMSCGRsqpghavlIVDPQSLEVLGD-NRVGEIWASGP 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3800 ILARGYLNDVDKTEAAFI--DDPAWLlegypghpgrqgrlyKTGDLvQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHH 3877
Cdd:PRK05691   406 SIAHGYWRNPEASAKTFVehDGRTWL---------------RTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKT 469
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3878 VRECLPEARQLAVEVILPSGQKDHAMLAAfVQLEEGTQNALLDKEAggEDSMAQVVFLASVEeelakrlpehmVPTVFFs 3957
Cdd:PRK05691   470 VEREVEVVRKGRVAAFAVNHQGEEGIGIA-AEISRSVQKILPPQAL--IKSIRQAVAEACQE-----------APSVVL- 534
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3958 LLH---FPTTTSGKTDRK--RLR-EIG-----ASFTAQQLAEMRTSSQGPkrqpsTEAEQTMQQLWAQVLSLGAdiIGLD 4026
Cdd:PRK05691   535 LLNpgaLPKTSSGKLQRSacRLRlADGsldsyALFPALQAVEAAQTAASG-----DELQARIAAIWCEQLKVEQ--VAAD 607
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4027 DSFFRLGGDSIAAMKLVGEAR-RMGLHLSVADIFRHPKLADFAGIQITQCSSGTEEVPAYSLLGEDEDVmqvckdvaamc 4105
Cdd:PRK05691   608 DHFFLLGGNSIAATQVVARLRdELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAQAAIARLPRGQAL----------- 676
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4106 svdasaitdvyPCSPLQEGLMSL--TAKRAGDYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELGL---- 4179
Cdd:PRK05691   677 -----------PQSLAQNRLWLLwqLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALqrid 745
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4180 ------LQVVVEERIQWTESESLEEYPREDKA---VSMGVGDrLARYALIKEPYDGGKRWFvwTMHHALYDGWSLPRILH 4250
Cdd:PRK05691   746 aqgefaLQRIDLSDLPEAEREARAAQIREEEArqpFDLEKGP-LLRVTLVRLDDEEHQLLV--TLHHIVADGWSLNILLD 822
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4251 AVKQAYS----GVVLERQP---SFNAFI----QYLSQQDPEAAAAYWQTALVDCKaalfPTLPPTVTQP----VADTTVE 4315
Cdd:PRK05691   823 EFSRLYAaacqGQTAELAPlplGYADYGawqrQWLAQGEAARQLAYWKAQLGDEQ----PVLELATDHPrsarQAHSAAR 898
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4316 YQCPPPSQSATDITTSTLAR---------AAWAIVTSRYTSSDDVVFGatVTGRNAPIAGGEAIVGPTIATVPVRLRVQR 4386
Cdd:PRK05691   899 YSLRVDASLSEALRGLAQAHqatlfmvllAAFQALLHRYSGQGDIRIG--VPNANRPRLETQGLVGFFINTQVLRAQLDG 976
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4387 DQTVFAFLQGVQQQATDMIAHEQTGLQRIAKMSPGARHACGFQTLLVVQPTDdvLGS----DDMLGE---WRSYSEMQDf 4459
Cdd:PRK05691   977 RLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQGLFQVMFNHQQRD--LSAlrrlPGLLAEelpWHSREAKFD- 1053
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4460 ttyalmVQCVLVKDRVG-VTASFD--ARVIEQWVVEKMLRQFGFVMQQLADAgEEKKVAGIETTTTGDRQQLWAWNQDVP 4536
Cdd:PRK05691  1054 ------LQLHSEEDRNGrLTLSFDyaAELFDAATIERLAEHFLALLEQVCED-PQRALGDVQLLDAAERAQLAQWGQAPC 1126
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4537 PAIERCVHDQFAEQARARPDTPAIcAWDGE-LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAG 4615
Cdd:PRK05691  1127 APAQAWLPELLNEQARQTPERIAL-VWDGGsLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAG 1205
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4616 GAFVPLDPDHPASRHEHIFRQTGAQVVLA-SAQYATLWTSLGRSVVIVSEASTSQLPVVTKTADpsVNPGNAAYAIFTSG 4694
Cdd:PRK05691  1206 GAYVPLDPDYPAERLAYMLADSGVELLLTqSHLLERLPQAEGVSAIALDSLHLDSWPSQAPGLH--LHGDNLAYVIYTSG 1283
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4695 STGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLcCGC-ICVPSDSDRRN--NLAKAINA 4771
Cdd:PRK05691  1284 STGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLI-TGCrLVLAGPGEHRDpqRIAELVQQ 1362
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4772 MDVNWALLTPSVARML--DPCVVQ--SLKILVLGGEQVNSADWDR----WPKsIQTINAYGPTECSICCTTY--SGKQGF 4841
Cdd:PRK05691  1363 YGVTTLHFVPPLLQLFidEPLAAActSLRRLFSGGEALPAELRNRvlqrLPQ-VQLHNRYGPTETAINVTHWqcQAEDGE 1441
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4842 KSgTIGTSIVSV-SWVVDPENHnrLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawllegygghSGRQG-RLYK 4919
Cdd:PRK05691  1442 RS-PIGRPLGNVlCRVLDAELN--LLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDP----------LGEDGaRLYR 1508
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4920 TGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVrecLTEAKQLAVEVIVPEGEGGYAMLAafvqlgddtYNTLv 4999
Cdd:PRK05691  1509 TGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARL---LAQPGVAQAAVLVREGAAGAQLVG---------YYTG- 1575
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5000 keKAGGDSLTvqvvflDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREIGAsftaqqlaemrtsSQGPKRQ 5079
Cdd:PRK05691  1576 --EAGQEAEA------ERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVW-------------QQREHVE 1634
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5080 PSTEAERTMQQLWTRVLGieLNGIGLDDSFFRLGGDSIAAMKLVGEAR-RTGLQLSVADVFRHprlvdlayvqnSECSSA 5158
Cdd:PRK05691  1635 PRTELQQQIAAIWREVLG--LPRVGLRDDFFALGGHSLLATQIVSRTRqACDVELPLRALFEA-----------SELGAF 1701
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5159 AEEVPAFSLLGGRAADTAQVSQDAAAMCSVDASS-----VEDMYPCSPLqeglmsltakragdYIMQSVLELRVDVDEDA 5233
Cdd:PRK05691  1702 AEQVARIQAAGERNSQGAIARVDRSQPVPLSYSQqrmwfLWQMEPDSPA--------------YNVGGMARLSGVLDVDR 1767
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5234 FRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEE--KIQWTESKRLEEYLREDKAVSmgLGDR------------LARYA 5299
Cdd:PRK05691  1768 FEAALQALILRHETLRTTFPSVDGVPVQQVAEDSglRMDWQDFSALPADARQQRLQQ--LADSeahqpfdlergpLLRAC 1845
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5300 LIKepYDGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGAVPERQPSFNAF-IQYLG-----QQDLEAATL-----YWQ 5368
Cdd:PRK05691  1846 LVK--AAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLpVQYLDysvwqRQWLESGERqrqldYWK 1923
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5369 TALADCKAALfpTLPPTVTQPVADT----TVEYQCPP-------PSQSATDITTSTLVRAAWAIVTSRYTSSDDVVFGAT 5437
Cdd:PRK05691  1924 AQLGNEHPLL--ELPADRPRPPVQShrgeLYRFDLSPelaarvrAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAP 2001
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5438 VTGRNAPIAgvEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAHEQTGLQRIAKMSPGARHACG---FQTLLV 5514
Cdd:PRK05691  2002 VANRIRPES--EGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYnplFQVMCN 2079
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5515 VQP------------TDDVLGSDDMLGEWRSYSEMQDFTTyalMVQCTLAKDRvevtASFD----ARVIEQWvvekmlrq 5578
Cdd:PRK05691  2080 VQRwefqqsrqlagmTVEYLVNDARATKFDLNLEVTDLDG---RLGCCLTYSR----DLFDepriARMAEHW-------- 2144
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5579 fgfvmQQLAEA---GAEKTVSDIETTTLEDRQQLWAWNQNVP--PAIERCVHDLFTEQAKARPHAPAIcAWDGE-LTYGE 5652
Cdd:PRK05691  2145 -----QNLLEAllgDPQQRLAELPLLAAAEQQQLLDSLAGEAgeARLDQTLHGLFAAQAARTPQAPAL-TFAGQtLSYAE 2218
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5653 LDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSA----- 5727
Cdd:PRK05691  2219 LDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRalfea 2298
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5728 -----QHSARWIGTNHQVVtVSAGSLGQLSTLvnpvglpAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFG 5802
Cdd:PRK05691  2299 lgelpAGVARWCLEDDAAA-LAAYSDAPLPFL-------SLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFG 2370
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5803 ITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSD-RRNDLVKAISTMDVSCALLTPSVARLL------EPSSVPt 5875
Cdd:PRK05691  2371 MRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQwGAEEICQLIREQQVSILGFTPSYGSQLaqwlagQGEQLP- 2449
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5876 LQMLVLQGEQVSFADWNRWPASVQT---INGYGPTECSI----CCNTYSGKQGFKSGIIGTSV-ASVSWVVDpenhDRLA 5947
Cdd:PRK05691  2450 VRMCITGGEALTGEHLQRIRQAFAPqlfFNAYGPTETVVmplaCLAPEQLEEGAASVPIGRVVgARVAYILD----ADLA 2525
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5948 PL--GSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypGHPGrqGRLYKTGDLVRYDANGNLVCLGRKDSQVKL 6025
Cdd:PRK05691  2526 LVpqGATGELYVGGAGLAQGYHDRPGLTAERFVADPF-------AADG--GRLYRTGDLVRLRADGLVEYVGRIDHQVKI 2596
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6026 RGQRVELGEVEHHVRE--CLPEARQLAVEviLPSGQKdhamLAAFvqleegtqnalLDKEASGEDSMAQVVFLASVEEEL 6103
Cdd:PRK05691  2597 RGFRIELGEIESRLLEhpAVREAVVLALD--TPSGKQ----LAGY-----------LVSAVAGQDDEAQAALREALKAHL 2659
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6104 AKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQIAnmqtssqdpkrQPSTEAEQTMQKLWAQVLGIElnG 6183
Cdd:PRK05691  2660 KQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQ-----------APRSELEQQLAQIWREVLNVE--R 2726
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6184 IGLDDSFFRLGGDSIAAMKLVGEARRIGLQLSVADIFRYARLVDLASLDTSQcnsaigevpafsllGGRAADTAQVSQDA 6263
Cdd:PRK05691  2727 VGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHS--------------EAAQAEQGPLQGAS 2792
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6264 aamcsvdassvedmyPCSPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSE--LGL 6341
Cdd:PRK05691  2793 ---------------GLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGrwQAE 2857
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6342 LQVVVEEKIQWTE-----SKRLEEYLREDKAVSMGLGdPLARYAIIKEAWGGKRWFVwTIHHALYDGWSLPRVLQAVKQA 6416
Cdd:PRK05691  2858 YRAVTAQELLWQVtvadfAECAALFADAQRSLDLQQG-PLLRALLVDGPQGQQRLLL-AIHHLVVDGVSWRVLLEDLQAL 2935
                         2890      2900      2910      2920      2930
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 6417 YNGAVLETQPSFNA-----------FIQYLSQQDLEATAAYWQTALADCEATL 6458
Cdd:PRK05691  2936 YRQLSAGAEPALPAktsafrdwaarLQAYAGSESLREELGWWQAQLGGPRAEL 2988
PRK12467 PRK12467
peptide synthase; Provisional
5217-7358 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 655.31  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5217 YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSElGLLQVVVEE------------KIQWTESKRLEEYLRED 5284
Cdd:PRK12467    72 YNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEE-GFRQVIDASlsltiplddlanEQGRARESQIEAYINEE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5285 KAVSMGLGD-RLARYALIKepYDGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGAVPERQPSFNAF-IQY----LGQQ 5358
Cdd:PRK12467   151 VARPFDLANgPLLRVRLLR--LADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALpIQYadyaIWQR 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5359 D-LEAAT-----LYWQTALADCKAAL-FPTLPPTVTQP-VADTTVEYQCPPPSQSA-------TDITTSTLVRAAWAIVT 5423
Cdd:PRK12467   229 SwLEAGErerqlAYWQEQLGGEHTVLeLPTDRPRPAVPsYRGARLRVDLPQALSAGlkalaqrEGVTLFMVLLASFQTLL 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5424 SRYTSSDDVVFGATVTGRNApiAGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAHEQTGL-QRIAKMSP- 5501
Cdd:PRK12467   309 HRYSGQSDIRIGVPNANRNR--VETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFeQLVEALQPe 386
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5502 -GARHACGFQTLLVVQPTddVLGSDDMLGEWRSYSEMQDFTTYALMVQCTLAKDRVEVTASFDAR------VIEQWVVEK 5574
Cdd:PRK12467   387 rSLSHSPLFQVMFNHQNT--ATGGRDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAftyatdLFEATTIER 464
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5575 MLRQFGFVMQQLAEAgAEKTVSDIETTTLEDRQ-QLWAWNQNVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGEL 5653
Cdd:PRK12467   465 LATHWRNLLEAIVAE-PRRRLGELPLLDAEERArELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAEL 543
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5654 DALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSAQHSARW 5733
Cdd:PRK12467   544 NRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQL 623
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5734 -IGTNHQVVTVS-AGSLGQLSTLVNPvGLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQ 5811
Cdd:PRK12467   624 pVPAGLRSLCLDePADLLCGYSGHNP-EVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLM 702
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5812 FASYTFDACMDEIITTLMYGGCICVPSDSDRRN--DLVKAISTMDVSCALLTPSVARLLEPSSVPTL----QMLVLQGEQ 5885
Cdd:PRK12467   703 VSTFAFDLGVTELFGALASGATLHLLPPDCARDaeAFAALMADQGVTVLKIVPSHLQALLQASRVALprpqRALVCGGEA 782
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5886 VSFADWNRWPA---SVQTINGYGPTECSICCNTYS-GKQGFKSGI--IGTSVASVSWVVdPENHDRLAPLGSIGELLVEG 5959
Cdd:PRK12467   783 LQVDLLARVRAlgpGARLINHYGPTETTVGVSTYElSDEERDFGNvpIGQPLANLGLYI-LDHYLNPVPVGVVGELYIGG 861
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5960 PILARGYLNDIQKTAAVFIDDPAwllegypGHPGrqGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHV 6039
Cdd:PRK12467   862 AGLARGYHRRPALTAERFVPDPF-------GADG--GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARL 932
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6040 REcLPEARQLAVEVILPSGqkdHAMLAAFVQleegtqnalldkEASGEDSMAQVVFLASVEEELAKRLPEHMVPTVFFSL 6119
Cdd:PRK12467   933 LA-QPGVREAVVLAQPGDA---GLQLVAYLV------------PAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLL 996
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6120 LHFPTTTSGKTDRKRLREIGASftaqqianmqtSSQDPKRQPSTEAEQTMQKLWAQVLGIElnGIGLDDSFFRLGGDSIA 6199
Cdd:PRK12467   997 DSLPLTPNGKLDRKALPKPDAS-----------AVQATFVAPQTELEKRLAAIWADVLKVE--RVGLTDNFFELGGHSLL 1063
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6200 AMKLVGEARR-IGLQLSVADIFRYARLVDLASLDTSQCNSAIGEVPafsllggraadtaQVSQDAAAmcsvdassvedmy 6278
Cdd:PRK12467  1064 ATQVISRVRQrLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALP-------------DVDRDQPL------------- 1117
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6279 PCSPLQEG---LMSLTAKRAGdYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGL------LQVVVEEK 6349
Cdd:PRK12467  1118 PLSYAQERqwfLWQLEPGSAA-YHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRqvihpvGSLTLEEP 1196
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6350 ---IQWTESKRLEEYLREDKAVSMGL-GDPLARYAIIKEAwGGKRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQ 6425
Cdd:PRK12467  1197 lllAADKDEAQLKVYVEAEARQPFDLeQGPLLRVGLLRLA-ADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQS 1275
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6426 PSFNAF-IQYL-----SQQDLEA-----TAAYWQTALADCEATL-FP---PLPSSVKQLVADTTVEHQCPLPSRSTSDTT 6490
Cdd:PRK12467  1276 LQLPALpIQYAdyavwQRQWMDAgerarQLAYWKAQLGGEQPVLeLPtdrPRPAVQSHRGARLAFELPPALAEGLRALAR 1355
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6491 TST-----LIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTsiDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEM 6565
Cdd:PRK12467  1356 REGvtlfmLLLASFQTLLHRYSGQDDIRVGVPIANRNRAET--EGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEA 1433
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6566 IAYEQTGLQQIAK-MGPDPQ--HACGFQTLL----VVQPAGDVLGS---------------DDTLGKWRGYSGLQDFMTY 6623
Cdd:PRK12467  1434 QAHQDLPFEQLVEaLQPERSlsHSPLFQVMFnhqrDDHQAQAQLPGlsveslswesqtaqfDLTLDTYESSEGLQASLTY 1513
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6624 AlgvrctlsaegvkiTASFDARVIehwvvEKMLGQFSFAMQQLAeASADRKVADIDITTTTDRQQ-LWAWNA---ELPLA 6699
Cdd:PRK12467  1514 A--------------TDLFEASTI-----ERLAGHWLNLLQGLV-ADPERRLGELDLLDEAERRQiLEGWNAthtGYPLA 1573
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6700 vdRCVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAF 6779
Cdd:PRK12467  1574 --RLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAY 1651
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6780 VPLDPDHP------------------------------------------------------------------------ 6787
Cdd:PRK12467  1652 VPLDPEYPrerlaymiedsgiellltqshlqarlplpdglrslvldqeddwlegysdsnpavnlapqnlayviytsgstg 1731
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6788 -----ASRHEDILRQ------------------------------------TGAQVILAS----------------AQNT 6810
Cdd:PRK12467  1732 rpkgaGNRHGALVNRlcatqeayqlsaadvvlqftsfafdvsvwelfwpliNGARLVIAPpgahrdpeqliqlierQQVT 1811
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6811 TLFQSSN----------------------------------------------------QTVVTVNRSSYILFPDENREA 6838
Cdd:PRK12467  1812 TLHFVPSmlqqllqmdeqvehplslrrvvcggealevealrpwlerlpdtglfnlygptETAVDVTHWTCRRKDLEGRDS 1891
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6839 YPFVRP----------SNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPAwlveghgkhpGRRG-RLYKTGDL 6907
Cdd:PRK12467  1892 VPIGQPianlstyildASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPF----------GTVGsRLYRTGDL 1961
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6908 VYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAGAaeqakTMVVAFLQLNDEArdallgg 6987
Cdd:PRK12467  1962 ARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLRE-QGGVREAVVIAQDGANG-----KQLVAYVVPTDPG------- 2028
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6988 nVPNDDNlsAQVVFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREIGASftaqqlaEMRTSSQGPKrqp 7067
Cdd:PRK12467  2029 -LVDDDE--AQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS-------ELQQAYVAPQ--- 2095
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7068 sTEAERTMQQLWARMLKVkaDSIGLDDSFFRLGGDSIVAMKLVGEARRTGLQLSVADVFRHPRLVDLAYVqnsqcssaae 7147
Cdd:PRK12467  2096 -SELEQRLAAIWQDVLGL--EQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAV---------- 2162
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7148 evpafsllgedvnpvqlSQDAAAMCSVAASIVKDIYPCSPLQEGLISLTAKRAGDYIMQSVLELRADVDEDVFCAAWEHV 7227
Cdd:PRK12467  2163 -----------------AQEGDGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQAL 2225
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7228 VQSTAALRTRIVQ--------------HSELGLLQVVVEEKiqwtesEALEEyLKEDKAVSMGLGD-PLAHYALVKEAWG 7292
Cdd:PRK12467  2226 LVHHDALRLGFVQedggwsamhrapeqERRPLLWQVVVADK------EELEA-LCEQAQRSLDLEEgPLLRAVLATLPDG 2298
                         2410      2420      2430      2440      2450      2460      2470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 7293 GKRwFVWTIHHALYDGGSLPLILH----AVKQVYSGAVLE---RQPSFNAFIQ----YLGQQDLEATAAYWQTALSD 7358
Cdd:PRK12467  2299 SQR-LLLVIHHLVVDGVSWRILLEdlqtAYRQLQGGQPVKlpaKTSAFKAWAErlqtYAASAALADELGYWQAQLQG 2374
PRK12467 PRK12467
peptide synthase; Provisional
6298-8408 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 641.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6298 YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSElGLLQVVVEE------------KIQWTESKRLEEYLRED 6365
Cdd:PRK12467    72 YNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEE-GFRQVIDASlsltiplddlanEQGRARESQIEAYINEE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6366 KAVSMGLGD-PLARYAIIKEAwGGKRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSFNAF-IQY----LSQQD 6439
Cdd:PRK12467   151 VARPFDLANgPLLRVRLLRLA-DDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALpIQYadyaIWQRS 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6440 -LEA-----TAAYWQTALADCEATLFPPL--PSSVKQLVADTTVEHQCPLPSRSTSDTTTST-------LIRAAWAIVAS 6504
Cdd:PRK12467   230 wLEAgererQLAYWQEQLGGEHTVLELPTdrPRPAVPSYRGARLRVDLPQALSAGLKALAQRegvtlfmVLLASFQTLLH 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6505 RYTSSDDVVFGTTITGRNAPVTsiDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEMIAYEQTGLQQIAK-MGP-- 6581
Cdd:PRK12467   310 RYSGQSDIRIGVPNANRNRVET--ERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEaLQPer 387
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6582 DPQHACGFQTLLVVQPagDVLGSDDTLGKWRGYSGLQDFMTYA------LGVRCTLSAEGVKITASFDARVIEHWVVEKM 6655
Cdd:PRK12467   388 SLSHSPLFQVMFNHQN--TATGGRDREGAQLPGLTVEELSWARhtaqfdLALDTYESAQGLWAAFTYATDLFEATTIERL 465
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6656 LGQFSFAMQQLAEAsADRKVADIDITTTTDRQ-QLWAWNAELPLAVDRCVHDLFTEQALARPNAPAVCAWDGELTYGELE 6734
Cdd:PRK12467   466 ATHWRNLLEAIVAE-PRRRLGELPLLDAEERArELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELN 544
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6735 ALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDILRQTGAQVILA--------- 6805
Cdd:PRK12467   545 RQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTqshllaqlp 624
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6806 --------------------SAQNTTLFQSSNQ----------------------------------------------- 6818
Cdd:PRK12467   625 vpaglrslcldepadllcgySGHNPEVALDPDNlayviytsgstgqpkgvaishgalanyvcviaerlqlaaddsmlmvs 704
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6819 ------------TVVTVNRSSYILFPDENREAYPFV-------------------------------------------- 6842
Cdd:PRK12467   705 tfafdlgvtelfGALASGATLHLLPPDCARDAEAFAalmadqgvtvlkivpshlqallqasrvalprpqralvcggealq 784
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6843 --------------------------------------RPSNA-------------------ALAPLGSIGELLVEGPIL 6865
Cdd:PRK12467   785 vdllarvralgpgarlinhygptettvgvstyelsdeeRDFGNvpigqplanlglyildhylNPVPVGVVGELYIGGAGL 864
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6866 ARGYLNDADKTAAAFVNDPAwlveghgKHPGrrGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREc 6945
Cdd:PRK12467   865 ARGYHRRPALTAERFVPDPF-------GADG--GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLA- 934
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6946 mPRATQMAVEVISPAGAAEQAKTMVVAFLQLNDEARDALLggnvpndDNLSAQvvfpakvdekLSNLLPSYMMPEVYFAV 7025
Cdd:PRK12467   935 -QPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQATR-------DELKAQ----------LRQVLPDYMVPAHLLLL 996
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7026 PQLPMMISGKTDRKRLREIGASftaqqlaemrtSSQGPKRQPSTEAERTMQQLWARMLKVkaDSIGLDDSFFRLGGDSIV 7105
Cdd:PRK12467   997 DSLPLTPNGKLDRKALPKPDAS-----------AVQATFVAPQTELEKRLAAIWADVLKV--ERVGLTDNFFELGGHSLL 1063
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7106 AMKLVGEARRT-GLQLSVADVFRHPRLVDLAYVQNSQCSSAAeevPAFSLLGEDvNPVQLSQDAAAmcsvaasivkdiyp 7184
Cdd:PRK12467  1064 ATQVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQ---PALPDVDRD-QPLPLSYAQER-------------- 1125
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7185 csplQEGLISLTAKRAGdYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSE--------LGLLQVVVEEKIQ 7256
Cdd:PRK12467  1126 ----QWFLWQLEPGSAA-YHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGrtrqvihpVGSLTLEEPLLLA 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7257 WTESEA-LEEYLKEDKAVSMGL-GDPLAHYALVKEAwGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFN 7334
Cdd:PRK12467  1201 ADKDEAqLKVYVEAEARQPFDLeQGPLLRVGLLRLA-ADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLP 1279
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7335 AF-IQYL------------GQQDLEAtaAYWQTALSDCEAVLFPPL--PSTVTQPVADTTVEYQCPP-LSKA------TL 7392
Cdd:PRK12467  1280 ALpIQYAdyavwqrqwmdaGERARQL--AYWKAQLGGEQPVLELPTdrPRPAVQSHRGARLAFELPPaLAEGlralarRE 1357
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7393 DTTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNApiAGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIA 7472
Cdd:PRK12467  1358 GVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNR--AETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQA 1435
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7473 H-----EQ--TGLQHIAKLGSGPRhacgFQTLLVVQPVDDvlGSDDMLGEWRSYSKMQDFTTyalmVQFTLA------AE 7539
Cdd:PRK12467  1436 HqdlpfEQlvEALQPERSLSHSPL----FQVMFNHQRDDH--QAQAQLPGLSVESLSWESQT----AQFDLTldtyesSE 1505
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7540 GVQITASFDARVIEHWVLEKMLRQFSFIMQQLAeASEDSKVADIDTTTPEDRQQ-LWAWNA---DVPPAieRCVHDLFAE 7615
Cdd:PRK12467  1506 GLQASLTYATDLFEASTIERLAGHWLNLLQGLV-ADPERRLGELDLLDEAERRQiLEGWNAthtGYPLA--RLVHQLIED 1582
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7616 QARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 7695
Cdd:PRK12467  1583 QAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRER 1662
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7696 HEEIFEQTGAQVVVASAQYSARWTSSS---CHVVTVSKALSSQLPAVVDSTNTSvrPENAAYIIFTSGSTGVPKGVVLEH 7772
Cdd:PRK12467  1663 LAYMIEDSGIELLLTQSHLQARLPLPDglrSLVLDQEDDWLEGYSDSNPAVNLA--PQNLAYVIYTSGSTGRPKGAGNRH 1740
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7773 RAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSV- 7849
Cdd:PRK12467  1741 GALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDpeQLIQLIERQQVTTLHFVPSMl 1820
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7850 -ARLLDPGLI---PSLKILAIGGE---QSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTK----QGFEPSTIGTSVAS 7918
Cdd:PRK12467  1821 qQLLQMDEQVehpLSLRRVVCGGEaleVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRrkdlEGRDSVPIGQPIAN 1900
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7919 VSW-VVDPENHnrLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNADGN 7997
Cdd:PRK12467  1901 LSTyILDASLN--PVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPF-------GTVG--SRLYRTGDLARYRADGV 1969
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7998 LVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAveVILPSGQKNHAMLAVFVQLGKGthiahleekaGGEDSMAQ 8077
Cdd:PRK12467  1970 IEYLGRIDHQVKIRGFRIELGEIEARLRE-QGGVREAV--VIAQDGANGKQLVAYVVPTDPG----------LVDDDEAQ 2036
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8078 VVFLTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGASftaqqlaETQTSSQGPKrqplTEAEQTMQQL 8157
Cdd:PRK12467  2037 VALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS-------ELQQAYVAPQ----SELEQRLAAI 2105
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8158 WARVLGIDAdiIGLDDSFFRLGGDSIAAMKLVGEARRTGLQLSVADIFRHPRLIDLaslkstfcnsvveevpafsllspv 8237
Cdd:PRK12467  2106 WQDVLGLEQ--VGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSL------------------------ 2159
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8238 mkdAMFSVTEPFGPSLRIDDITDVVPASYIQQFYIATGVrAPREAFNYP-FIDLSDAVDIQVLQASCSALLEHFPILRTH 8316
Cdd:PRK12467  2160 ---AAVAQEGDGTVSIDQGPVTGDLPLLPIQQMFFADDI-PERHHWNQSvLLEPREALDAELLEAALQALLVHHDALRLG 2235
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8317 FVYFQGklyQVIPRHQDL-----------PFSIFEVNGALAEESQaihiRDLD-QTSPLglpTSFTLVRNASGMNRLIIR 8384
Cdd:PRK12467  2236 FVQEDG---GWSAMHRAPeqerrpllwqvVVADKEELEALCEQAQ----RSLDlEEGPL---LRAVLATLPDGSQRLLLV 2305
                         2410      2420
                   ....*....|....*....|....
gi 1820002560 8385 LSHAQYDGVCMPVIWASLASIYQQ 8408
Cdd:PRK12467  2306 IHHLVVDGVSWRILLEDLQTAYRQ 2329
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1510-2750 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 618.02  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1510 SPLQEGLMSLTAKRAGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQVVIEENIQWTEPKSLEE 1589
Cdd:COG1020     34 LLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEA 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1590 YLSEDKAVSVGLGDPLARYAFVKEACGGKRWFVWTIHHAVYDGWSLPLILHAVKQVY-----------SGGVLQWQPSFN 1658
Cdd:COG1020    114 AAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYlaayagaplplPPLPIQYADYAL 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1659 AFIQYLGQQDLEATVAYWQTALADCEAVL-FPTLPPTVT-QPVADATVEYQCPP-LSKA------TSDTTTSTLIRAAWA 1729
Cdd:COG1020    194 WQREWLQGEELARQLAYWRQQLAGLPPLLeLPTDRPRPAvQSYRGARVSFRLPAeLTAAlralarRHGVTLFMVLLAAFA 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1730 IVTSRYTTSDDVVFGTTVTGRNTPvtGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAHEQTG---LQRIA 1806
Cdd:COG1020    274 LLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPferLVEEL 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1807 KMGQGPQHACSFQTLLVVQPVDDVLDNTLG-EWRDHSELQEFTTYTLMLQCMLAAEGVQITASFDTRVIEKWVVEKMLRQ 1885
Cdd:COG1020    352 QPERDLSRNPLFQVMFVLQNAPADELELPGlTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGH 431
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1886 FSFIMQQLAeAGAEKTVSDIETTTPEDRQQLWA-WNQ-EVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDAL 1963
Cdd:COG1020    432 LVTLLEALA-ADPDQPLGDLPLLTAAERQQLLAeWNAtAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNAR 510
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1964 SSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSAQHSARWIGT 2043
Cdd:COG1020    511 ANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPEL 590
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2044 NHQVVTVSAGSLEQFSTLvNPVdLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLRALQFTAYT 2123
Cdd:COG1020    591 GVPVLALDALALAAEPAT-NPP-VPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLS 668
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2124 FDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSSVARLL---DPCLVPSLKVLVLGGEQVNSTDW 2198
Cdd:COG1020    669 FDASVWEIFGALLSGATLVLAPPEARRDpaALAELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELV 748
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2199 GKW---PSSVQTINGYGPTECCVFCTGYTgIQGFQSGN----IGTSIASVS-WVVDPenHGRLAPLGSIGELLVEGPILA 2270
Cdd:COG1020    749 RRWrarLPGARLVNLYGPTETTVDSTYYE-VTPPDADGgsvpIGRPIANTRvYVLDA--HLQPVPVGVPGELYIGGAGLA 825
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2271 RGYLNDVDKTQAAFIDDPAwlleGYPGhegrqGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKCl 2350
Cdd:COG1020    826 RGYLNRPELTAERFVADPF----GFPG-----ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQH- 895
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2351 PEANQlAVeVVPPSGERDHAMLAAFIRLDDETRNSPLIIKYAednstaqivfltgieeeLSERLPQHMVPTVFFALVHFP 2430
Cdd:COG1020    896 PGVRE-AV-VVAREDAPGDKRLVAYVVPEAGAAAAAALLRLA-----------------LALLLPPYMVPAAVVLLLPLP 956
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2431 TTTSGKTDRKRLREIGASFTAQqlaemrtssegpkRQPSTEAERTMQQLWAQVLGIELESIGLDDSFFRLGGDSITAMQI 2510
Cdd:COG1020    957 LTGNGKLDRLALPAPAAAAAAA-------------AAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLAL 1023
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2511 SSSARALHLSVSTGDILKKKTIALIAREILPSTSTFSRSVWRDPVNNAFDLTPIQHLYLTLDPSGRSSFDQCFF---LEL 2587
Cdd:COG1020   1024 ARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLAlllLLL 1103
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2588 RNRVQPQLLVTALTALVQRHSMLRARFQRQTGGRWQQYISEHDSSSLIVNHIHTRDTTEIVEALRQSRGSLDIERGPVLA 2667
Cdd:COG1020   1104 LLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLA 1183
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2668 AVLCDAGERQSLFVAIHHLVVDLVSWRILLEELEDLLLGQTLPPALSTPFQAWHAAQAKYIEEHVPPSAVAQVELDPDQL 2747
Cdd:COG1020   1184 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALA 1263

                   ...
gi 1820002560 2748 SYW 2750
Cdd:COG1020   1264 LAL 1266
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
7199-8439 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 601.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7199 RAGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVVVEEKIQWTESEALEEYLKEDKA----VS 7274
Cdd:COG1020     47 LLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALapfdLL 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7275 MGLGDPLAHYALVKEAWGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAFIQY-------LGQQDLEA 7347
Cdd:COG1020    127 RGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYalwqrewLQGEELAR 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7348 TAAYWQTALSDCEAVLFPPL--PSTVTQPVADTTVEYQCPP-LSKA------TLDTTTSTLIRAAWAIVTSCYTSSDDVV 7418
Cdd:COG1020    207 QLAYWRQQLAGLPPLLELPTdrPRPAVQSYRGARVSFRLPAeLTAAlralarRHGVTLFMVLLAAFALLLARYSGQDDVV 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7419 YGTTVTGRNAPiaGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTG---LQHIAKLGSGPRHACGFQ 7495
Cdd:COG1020    287 VGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPferLVEELQPERDLSRNPLFQ 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7496 TLLVVQ--PVDDVlgsdDMLG-EWRSYSKMQDFTTYALMVQFTLAAEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLA 7572
Cdd:COG1020    365 VMFVLQnaPADEL----ELPGlTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALA 440
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7573 eASEDSKVADIDTTTPEDRQQLWA-WNA-DVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLV 7650
Cdd:COG1020    441 -ADPDQPLGDLPLLTAAERQQLLAeWNAtAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLR 519
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7651 QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSK 7730
Cdd:COG1020    520 ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDA 599
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7731 ALSSQLPAvvDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEII 7810
Cdd:COG1020    600 LALAAEPA--TNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIF 677
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7811 TTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL---DPGLIPSLKILAIGGEQSSSADWNRW---PGS 7882
Cdd:COG1020    678 GALLSGATLVLAPPEARRDpaALAELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELVRRWrarLPG 757
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7883 VQKIHVYGPTECCIFCTGYTTKQGF---EPSTIGTSVASVS-WVVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKT 7958
Cdd:COG1020    758 ARLVNLYGPTETTVDSTYYEVTPPDadgGSVPIGRPIANTRvYVLDA--HLQPVPVGVPGELYIGGAGLARGYLNRPELT 835
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7959 EAAFIDDPAwlleGYPGhpgrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQlAVeV 8038
Cdd:COG1020    836 AERFVADPF----GFPG-----ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQH-PGVRE-AV-V 903
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8039 ILPSGQKNHAMLAVFVQLGKGTHIAHLEEkaggedsmaqvvfltgtEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRK 8118
Cdd:COG1020    904 VAREDAPGDKRLVAYVVPEAGAAAAAALL-----------------RLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8119 RLREIGAsftaqqlaetqtssQGPKRQPLTEAEQTMQQLWARVLGIDADIIGLDDSFFRLGGDSIAAMKLVGEARRTGLQ 8198
Cdd:COG1020    967 ALPAPAA--------------AAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLL 1032
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8199 LSVADIFRHPRLIDLASLKSTFCNSVVEEVPAfsllspvmkdamfsvtepfgpsLRIDDITDVVPASYIQQFYIATGVRA 8278
Cdd:COG1020   1033 LLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLA----------------------AAAAPLPLPPLLLSLLALLLALLLLL 1090
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8279 PREAFNYPFIDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIPRHQDLPFSIFEVNGAL----AEESQAIHI 8354
Cdd:COG1020   1091 ALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLlaaaAAAAELLAA 1170
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8355 RDLDQTSPLGLPTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQEPLLSTTGFHSYLAYVHNQRSASINY 8434
Cdd:COG1020   1171 AALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALA 1250

                   ....*
gi 1820002560 8435 WSRLL 8439
Cdd:COG1020   1251 ALAAL 1255
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
5201-6503 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 597.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5201 PLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEEKIQWTE------- 5273
Cdd:COG1020     28 WLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLvdleala 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5274 ----SKRLEEYLREDKAVSMGLGDRLARYALIKEPYDGGKRWFVWtIHHALYDGWSLPRILQAVKQIYSGAVPERQPSFN 5349
Cdd:COG1020    108 eaaaEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHI-ISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPI 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5350 AFIQY-------LGQQDLEAATLYWQTALADCKAAL-FPTLPPTVTQPVADTTVEYQCPPPSQSA--------TDITTST 5413
Cdd:COG1020    187 QYADYalwqrewLQGEELARQLAYWRQQLAGLPPLLeLPTDRPRPAVQSYRGARVSFRLPAELTAalralarrHGVTLFM 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5414 LVRAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAHEQTG- 5492
Cdd:COG1020    267 VLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPf 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5493 --LQRIAKMSPGARHACGFQTLLVVQPTDDvlGSDDMLG-EWRSYSEMQDFTTYALMVQCTLAKDRVEVTASFDARVIEQ 5569
Cdd:COG1020    345 erLVEELQPERDLSRNPLFQVMFVLQNAPA--DELELPGlTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDA 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5570 WVVEKMLRQFGFVMQQLAeAGAEKTVSDIETTTLEDRQQLWA-WNQN-VPPAIERCVHDLFTEQAKARPHAPAICAWDGE 5647
Cdd:COG1020    423 ATIERMAGHLVTLLEALA-ADPDQPLGDLPLLTAAERQQLLAeWNATaAPYPADATLHELFEAQAARTPDAVAVVFGDQS 501
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSA 5727
Cdd:COG1020    502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQS 581
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5728 QHSARWIGTNHQVVTVSAGSLGQLSTLvNPVgLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLS 5807
Cdd:COG1020    582 ALAARLPELGVPVLALDALALAAEPAT-NPP-VPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGD 659
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5808 RVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRN--DLVKAISTMDVSCALLTPSVARLL---EPSSVPTLQMLVLQ 5882
Cdd:COG1020    660 RVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDpaALAELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVG 739
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5883 GEQVSFADWNRW---PASVQTINGYGPTECSICCNTY--SGKQGFKSGI-IGTSVASVS-WVVDPenHDRLAPLGSIGEL 5955
Cdd:COG1020    740 GEALPPELVRRWrarLPGARLVNLYGPTETTVDSTYYevTPPDADGGSVpIGRPIANTRvYVLDA--HLQPVPVGVPGEL 817
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5956 LVEGPILARGYLNDIQKTAAVFIDDPAwlleGYPGhpgrqGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEV 6035
Cdd:COG1020    818 YIGGAGLARGYLNRPELTAERFVADPF----GFPG-----ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEI 888
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6036 EHHVREClPEARQlAVeVILPSGQKDHAMLAAFVQLEEGTQNAlldkeasgedsmaqvvfLASVEEELAKRLPEHMVPTV 6115
Cdd:COG1020    889 EAALLQH-PGVRE-AV-VVAREDAPGDKRLVAYVVPEAGAAAA-----------------AALLRLALALLLPPYMVPAA 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6116 FFSLLHFPTTTSGKTDRKRLREIGAsftaqqianmqtssQDPKRQPSTEAEQTMQKLWAQVLGIELNGIGLDDSFFRLGG 6195
Cdd:COG1020    949 VVLLLPLPLTGNGKLDRLALPAPAA--------------AAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGG 1014
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6196 DSIAAMKLVGEARRIGLQLSVADIFRYARLVDLASLDTSQCNSAIGEVPAfslLGGRAADTAQVSQDAAAMCSVDASSVE 6275
Cdd:COG1020   1015 LGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLA---AAAAPLPLPPLLLSLLALLLALLLLLA 1091
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6276 DMYPCSPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEEKIQWTES 6355
Cdd:COG1020   1092 LLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAA 1171
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6356 KRLEEYLREDKAVSMGLGDPLARYAIIKEAWggkRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSFNAFIQYL 6435
Cdd:COG1020   1172 ALLLLLALLLLALLLLLLLLLLLLLLLLLLL---LLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLA 1248
                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 6436 SQQDLEATAAYWQTALADCEATLFPPLPSSVKQLVADTTVEHQCPLPSRSTSDTTTSTLIRAAWAIVA 6503
Cdd:COG1020   1249 LAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLL 1316
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
428-1729 3.34e-180

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 596.45  E-value: 3.34e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  428 SPLQEGLMSLTTKRAGDYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQVVVEEKMQWTESESLEE 507
Cdd:COG1020     34 LLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEA 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  508 YLNEDKAASMGLGDRLARYALIKESCGGKRWFVWTIHHALYDGWSLPLVLDAVKQVY----SGAALERQPSFNTFIQYV- 582
Cdd:COG1020    114 AAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYlaayAGAPLPLPPLPIQYADYAl 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  583 ------SQQDVKAAAAYWQTALADCEAVLFPPLPSTVTQPVADTTVKYQCPPSPEVT--------SSNITTSTLIRAAWA 648
Cdd:COG1020    194 wqrewlQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTaalralarRHGVTLFMVLLAAFA 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  649 IIASRYTSSEDIVFGTTVTGRNAPitGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTG---LQRIM 725
Cdd:COG1020    274 LLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPferLVEEL 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  726 KMGPGPQHACGFQTLLVVH--PTDDVLSSDDTLGEWHSRSDSelqyfTTYALTIQCTLAVEGVQITASFDARVVEHWVVE 803
Cdd:COG1020    352 QPERDLSRNPLFQVMFVLQnaPADELELPGLTLEPLELDSGT-----AKFDLTLTVVETGDGLRLTLEYNTDLFDAATIE 426
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  804 KMLGQFSFVMQQLAeAGVEKKVADIETTTLEDRQQLWV-WNA-DMPPAVDRCIHDLFAEQARARPDASAVCAWDGELTYG 881
Cdd:COG1020    427 RMAGHLVTLLEALA-ADPDQPLGDLPLLTAAERQQLLAeWNAtAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYA 505
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  882 ELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSQHAM 961
Cdd:COG1020    506 ELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAA 585
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  962 LFASSERHQVTVSKVSTSQLPTvvNFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQ 1041
Cdd:COG1020    586 RLPELGVPVLALDALALAAEPA--TNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQ 663
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1042 FASYTFDACIAEIITTLLYGGCICVPSESDRRN--NLAKAISTMDVNCALLTPSVARLL---EPSAVPSLKRLVLQGEQV 1116
Cdd:COG1020    664 FASLSFDASVWEIFGALLSGATLVLAPPEARRDpaALAELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEAL 743
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1117 SFADWNRW---PGSVQTINGYGPTECSVCCNTY--SGKQGFKSGI-IGTSVASLS-WVVDAgnHNRLAPLGSIGELLVEG 1189
Cdd:COG1020    744 PPELVRRWrarLPGARLVNLYGPTETTVDSTYYevTPPDADGGSVpIGRPIANTRvYVLDA--HLQPVPVGVPGELYIGG 821
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1190 PILARGYLNDIDKTEAAFIDDPAwllegyeGHAGrrGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHV 1269
Cdd:COG1020    822 AGLARGYLNRPELTAERFVADPF-------GFPG--ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAAL 892
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1270 REClPEARQlAVeVILPSGQKEHALLAAFIQLDKGNHNALFEEkasgedsmaqvvfltgvEEELAKRLPEHMVPTILFTV 1349
Cdd:COG1020    893 LQH-PGVRE-AV-VVAREDAPGDKRLVAYVVPEAGAAAAAALL-----------------RLALALLLPPYMVPAAVVLL 952
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1350 KAMPITTSGKIDRKRlqdigasftvqqLAEMRTSSQGPKRQPSTEVEQTMQQLWAQVLSIEPNSIGLDDSFFRLGGDSIV 1429
Cdd:COG1020    953 LPLPLTGNGKLDRLA------------LPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLL 1020
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1430 AMKLVGEARRTGLQLSVADIFRHPRLVDLARVQNSQFSSAAEEVPAFSLLGEDVNAVQLSQDAAAMCSVAAGIVEDIYPC 1509
Cdd:COG1020   1021 LALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLL 1100
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1510 SPLQEGLMSLTAKRAGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQVVIEEniqwtepKSLEE 1589
Cdd:COG1020   1101 LLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELL-------AAAAL 1173
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1590 YLSEDKAVSVGLGDPLARYAFVKEACGGKRWFVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQWQPSFNAFIQYLGQQDL 1669
Cdd:COG1020   1174 LLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALA 1253
                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1670 EATVAYWQTALADCEAVLFPTLPPTVTQPVADATVEYQCPPLSKATSDTTTSTLIRAAWA 1729
Cdd:COG1020   1254 ALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALAL 1313
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
4120-5420 6.83e-180

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 595.30  E-value: 6.83e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4120 PLQEGLMSLTAKRAGDYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELGLLQVVVEERIQWTESESLEEY 4199
Cdd:COG1020     28 WLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALA 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4200 PREDKAV-----------SMGVGDRLARYALIKEPYDGGKRWFVWtMHHALYDGWSLPRILHAVKQAYSGVVLERQPSFN 4268
Cdd:COG1020    108 EAAAEAAaaaealapfdlLRGPLLRLLLLLLLLLLLLLLLALHHI-ISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPI 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4269 AFIQY-------LSQQDPEAAAAYWQTALVDCKAAL-FPTLPPTVTQPVADTTVEYQCPPPSQSA--------TDITTST 4332
Cdd:COG1020    187 QYADYalwqrewLQGEELARQLAYWRQQLAGLPPLLeLPTDRPRPAVQSYRGARVSFRLPAELTAalralarrHGVTLFM 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4333 LARAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQATDMIAHEQTG- 4411
Cdd:COG1020    267 VLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPf 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4412 --LQRIAKMSPGARHACGFQTLLVVQPTDDvlGSDDMLG-EWRSYSEMQDFTTYALMVQCVLVKDRVGVTASFDARVIEQ 4488
Cdd:COG1020    345 erLVEELQPERDLSRNPLFQVMFVLQNAPA--DELELPGlTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDA 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4489 WVVEKMLRQFGFVMQQLAdAGEEKKVAGIETTTTGDRQQLWA-WNQ-DVPPAIERCVHDQFAEQARARPDTPAICAWDGE 4566
Cdd:COG1020    423 ATIERMAGHLVTLLEALA-ADPDQPLGDLPLLTAAERQQLLAeWNAtAAPYPADATLHELFEAQAARTPDAVAVVFGDQS 501
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLASA 4646
Cdd:COG1020    502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQS 581
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4647 QYATLWTSLGRSVVIVSEASTSQLPvvTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHT 4726
Cdd:COG1020    582 ALAARLPELGVPVLALDALALAAEP--ATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGD 659
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4727 RVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRN--NLAKAINAMDVNWALLTPSVARML---DPCVVQSLKILVLG 4801
Cdd:COG1020    660 RVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDpaALAELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVG 739
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4802 GEQVNSADWDRW---PKSIQTINAYGPTECSICCTTY---SGKQGFKSGTIGTSIVSVS-WVVDPenHNRLAPLGSIGEL 4874
Cdd:COG1020    740 GEALPPELVRRWrarLPGARLVNLYGPTETTVDSTYYevtPPDADGGSVPIGRPIANTRvYVLDA--HLQPVPVGVPGEL 817
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4875 LVEGPILARGYLNDMEKTEAAFIDDPAwlleGYGGhsgrqGRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEV 4954
Cdd:COG1020    818 YIGGAGLARGYLNRPELTAERFVADPF----GFPG-----ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEI 888
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4955 EHHVRECltEAKQLAVeVIVPEGEGGYAMLAAFVQLGDDtyntlvkekaggdsltvQVVFLDRVEEELAKRVPEHMMLTT 5034
Cdd:COG1020    889 EAALLQH--PGVREAV-VVAREDAPGDKRLVAYVVPEAG-----------------AAAAAALLRLALALLLPPYMVPAA 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5035 FFTLEAMPTTTSGKIDRKRLREIGAsftaqqlaemrtssQGPKRQPSTEAERTMQQLWTRVLGIELNGIGLDDSFFRLGG 5114
Cdd:COG1020    949 VVLLLPLPLTGNGKLDRLALPAPAA--------------AAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGG 1014
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5115 DSIAAMKLVGEARRTGLQLSVADVFRHPRLVDLAYVQNSECSSAAEEVPAfslLGGRAADTAQVSQDAAAMCSVDASSVE 5194
Cdd:COG1020   1015 LGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLA---AAAAPLPLPPLLLSLLALLLALLLLLA 1091
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5195 DMYPCSPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEEKIQWTES 5274
Cdd:COG1020   1092 LLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAA 1171
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5275 KRLEEYLREDKAVSMGLGDRLARYALIKEPYDGGkrwfVWTIHHALYDGWSLPRILQAVKQIYSGAVPERQPSFNAFIQY 5354
Cdd:COG1020   1172 ALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLL----LLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALL 1247
                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 5355 LGQQDLEAATLYWQTALADCKAALFPTLPPTVTQPVADTTVEYQCPPPSQSATDITTSTLVRAAWA 5420
Cdd:COG1020   1248 ALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALAL 1313
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
3155-4344 7.37e-176

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 583.74  E-value: 7.37e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3155 HAIIDAHSRGILMHDLQEAYDA-------NLNPQSTSFRDFASYIKQQSQ----EEAGRYWAEYLDGVEPCFFPSLGDSG 3223
Cdd:COG1020    151 HIISDGLSDGLLLAELLRLYLAayagaplPLPPLPIQYADYALWQREWLQgeelARQLAYWRQQLAGLPPLLELPTDRPR 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3224 GANTIPR----TVEVPSIDSSAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPihNVNSIFGPLIS 3299
Cdd:COG1020    231 PAVQSYRgarvSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVN 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3300 ILPCRIHLHKQLTVLEALKTVQENYASSLSFQTFPLASMHSFLG----LGTSALFNTALSLQRIDDiGPCSASEITLKMK 3375
Cdd:COG1020    309 TLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQperdLSRNPLFQVMFVLQNAPA-DELELPGLTLEPL 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3376 E-GLDPTEYNITLSAGYSKDAIDISMTFRAGCMDLVQAKRLASNFSQAIKAVTTEPHSRIYSLDILTYNESKKIW-GWNA 3453
Cdd:COG1020    388 ElDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLaEWNA 467
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3454 -DVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVL 3532
Cdd:COG1020    468 tAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVL 547
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3533 KAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSKALSSQLPAvvDSTNTSVRPENAAYIIFT 3612
Cdd:COG1020    548 KAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPA--TNPPVPVTPDDLAYVIYT 625
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3613 SGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAIS 3690
Cdd:COG1020    626 SGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDpaALAELLA 705
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3691 TMDVNWAFLTPSVARLL---DPGLIPSLKILAIGGEQSSSADWNRW---PGSVQKIHVYGPTECCIFCTGYTTKQGF--- 3761
Cdd:COG1020    706 RHRVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELVRRWrarLPGARLVNLYGPTETTVDSTYYEVTPPDadg 785
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3762 EPSTIGTSVASVS-WVVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwlleGYPGhpgrqGRLYKT 3840
Cdd:COG1020    786 GSVPIGRPIANTRvYVLDA--HLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPF----GFPG-----ARLYRT 854
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3841 GDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQlAVeVILPSGQKDHAMLAAFVQLEEGTQNAlld 3920
Cdd:COG1020    855 GDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQH-PGVRE-AV-VVAREDAPGDKRLVAYVVPEAGAAAA--- 928
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3921 keaggedsmaqvvfLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGAsftaqqlaemrtssQGPKRQP 4000
Cdd:COG1020    929 --------------AALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAA--------------AAAAAAA 980
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4001 STEAEQTMQQLWAQVLSLGADIIGLDDSFFRLGGDSIAAMKLVGEARRMGLHLSVADIFRHPKLADFAGIQITQCSSGTE 4080
Cdd:COG1020    981 APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAA 1060
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4081 EVPAYSLLGEDEDVMQvckdvaamcsVDASAITDVYPCSPLQEGLMSLTAKRAGDYIMQTVLELRADVnEDAFRAAWELV 4160
Cdd:COG1020   1061 APLAAAAAPLPLPPLL----------LSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALL-LALLAALRARR 1129
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4161 VQLTAVLRTRIVQHSELGLLQVVVEERIQWTESESLEEYPREDKAVSMGVGDRLARYALIKEPYDGGKRWFVWT-MHHAL 4239
Cdd:COG1020   1130 AVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLlLLLLL 1209
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4240 YDGWSLPRILHAVKQAYSGVVLERQPSFNAFIQYLSQQDPEAAAAYWQTALVDCKAALFPTLPPTVTQPVADTTVEYQCP 4319
Cdd:COG1020   1210 LLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAA 1289
                         1210      1220
                   ....*....|....*....|....*
gi 1820002560 4320 PPSQSATDITTSTLARAAWAIVTSR 4344
Cdd:COG1020   1290 RTARALALLLLLALLLLLALALALL 1314
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
5196-5590 3.31e-174

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 543.04  E-value: 3.31e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5196 MYPCSPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVV-EEKIQWTES 5274
Cdd:cd19545      1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVkESPISWTES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5275 KRLEEYLREDKAVSMGLGDRLARYALIKEPydGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGAVPERQPSFNAFIQY 5354
Cdd:cd19545     81 TSLDEYLEEDRAAPMGLGGPLVRLALVEDP--DTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRFVKY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5355 LGQQDLEAATLYWQTALADCKAALFPTLPPTVTQPVADTTVEYQCPPPSQSATDITTSTLVRAAWAIVTSRYTSSDDVVF 5434
Cdd:cd19545    159 LRQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSASSGVTLATVLRAAWALVLSRYTGSDDVVF 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5435 GATVTGRNAPIAGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAHEQTGLQRIAKMSPGARHACGFQTLLV 5514
Cdd:cd19545    239 GVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDARAACNFQTLLV 318
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 5515 VQPTDDVLGSDDM-LGEWRSYSEMQDFTTYALMVQCTLAKDRVEVTASFDARVIEQWVVEKMLRQFGFVMQQLAEAG 5590
Cdd:cd19545    319 VQPALPSSTSESLeLGIEEESEDLEDFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
PRK12316 PRK12316
peptide synthase; Provisional
20-1772 9.03e-174

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 610.04  E-value: 9.03e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   20 HIPSLRILVMGGEQVNSADWDRWPSSVQT---INGYGPTECCIVCTGYTSEQDFTTGT----IGTSIASVS-WVVDPKDH 91
Cdd:PRK12316  2259 RPPAVRVYCFGGEAVPAASLRLAWEALRPvylFNGYGPTEAVVTPLLWKCRPQDPCGAayvpIGRALGNRRaYILDADLN 2338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   92 grLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawlleghggYAGRQGRLYKTGDLVRYDADGNLVCLGRKDSQV 171
Cdd:PRK12316  2339 --LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDP---------FSASGERLYRTGDLARYRADGVVEYLGRIDHQV 2407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  172 KLRGQRVELGEVEHHVR--ECLPEAkqlaveVVLPLGQKNHATLAAFiqldkgthnallkekVGGDDsiARVVFLAGVEE 249
Cdd:PRK12316  2408 KIRGFRIELGEIEARLQahPAVREA------VVVAQDGASGKQLVAY---------------VVPDD--AAEDLLAELRA 2464
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  250 ELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASFTAQQLAEmrtssqgpkrqPSTEAERTMQQLWARVLGIEp 329
Cdd:PRK12316  2465 WLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVA-----------PQEGLEQRLAAIWQAVLKVE- 2532
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  330 dSIGLDDSFFRLGGDSIAAIKLVGEARRT-GLQPSVADIFRHPTLAALA-SLETNQYNITIEETPPLSLLGENADVAQVR 407
Cdd:PRK12316  2533 -QVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAaSLESGQTSRAPVLQKVTRVQPLPLSHAQQR 2611
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  408 deaaamcsvdgsaiedmylcsplQEGLMSLTTKRAGdYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSE-- 485
Cdd:PRK12316  2612 -----------------------QWFLWQLEPESAA-YHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEqt 2667
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  486 ------LGLLQVVVEEKMQWTESESLEEYLNEDKAASMGLGDRLARYALIkESCGGKRWFVWTIHHALYDGWSLPLVLDA 559
Cdd:PRK12316  2668 rqvilpNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLL-ALDGQEHVLVITQHHIVSDGWSMQVMVDE 2746
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  560 VKQVYSGAALERQPSFNTF-IQYVS----QQDVKAAA------AYWQTALADCEAVLFPPL--PSTVTQPVADTTVKYQC 626
Cdd:PRK12316  2747 LVQAYAGARRGEQPTLPPLpLQYADyaawQRAWMDSGegarqlDYWRERLGGEQPVLELPLdrPRPALQSHRGARLDVAL 2826
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  627 PPSPE------VTSSNITTSTLIRAAWAIIASRYTSSEDIVFGTTVTGRNAPitGVEAMVGPTIATVPLRVRPRKGQTVS 700
Cdd:PRK12316  2827 DVALSrellalARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQVLRAQVDAQLAFR 2904
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  701 AFLENLQQQATEMIAYEQTGL-QRIMKMGP--GPQHACGFQTLLVvhpTDDVLSSDDTLGEWHSRSDSELQYFTTYALTI 777
Cdd:PRK12316  2905 DLLGQVKEQALGAQAHQDLPFeQLVEALQPerSLSHSPLFQVMYN---HQSGERAAAQLPGLHIESFAWDGAATQFDLAL 2981
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  778 QCTLAVEGVQITASFDARVVEHWVVEKMLGQFSFVMQQLAEaGVEKKVADIETTTLEDRQQ-LWVWN---ADMPPAvdRC 853
Cdd:PRK12316  2982 DTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVE-NPQRSVDELAMLDAEERGQlLEAWNataAEYPLE--RG 3058
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 933
Cdd:PRK12316  3059 VHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLD 3138
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 PGHPASRHEEIFKQIGAQVVLTssQHAMLFASSERHQVTVSKVSTSQLPTvvNFAKSPVDPGNTAYIIFTSGTTGIPKGV 1013
Cdd:PRK12316  3139 PEYPEERLAYMLEDSGAQLLLS--QSHLRLPLAQGVQVLDLDRGDENYAE--ANPAIRTMPENLAYVIYTSGSTGKPKGV 3214
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1014 VLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNN--LAKAISTMDVNCALLT 1091
Cdd:PRK12316  3215 GIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPalLVELINSEGVDVLHAY 3294
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1092 PSVARLLEPSAVP----SLKRLVLQGEQVSFADWNRWPGSVQTINGYGPTECSVCCNTYSGKQGFKSGI-IGTSVASLSW 1166
Cdd:PRK12316  3295 PSMLQAFLEEEDAhrctSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAVpIGRPIANRAC 3374
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1167 VVDAGNHNRlAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawLLEGyeghagrrGRLYKTGDLVRCDADGNLVCL 1246
Cdd:PRK12316  3375 YILDGSLEP-VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDP--FVPG--------ERLYRTGDLARYRADGVIEYI 3443
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1247 GRKDSQVKVRGQRVELGEIEHHVRE--CLPEARQLAVEvilpsGQKehalLAAFIQLDKGNHNALFEEKASgedsmaqvv 1324
Cdd:PRK12316  3444 GRVDHQVKIRGFRIELGEIEARLLEhpWVREAVVLAVD-----GRQ----LVAYVVPEDEAGDLREALKAH--------- 3505
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1325 fltgveeeLAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDIGASFTVQQLAemrtssqgpkrQPSTEVEQTMQQLWA 1404
Cdd:PRK12316  3506 --------LKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVNELERRLAAIWA 3566
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1405 QVLSIEpnSIGLDDSFFRLGGDSIVAMKLVGEARRTGLQLSVADIFRHPRLVDLARVQNSQFSSAAEEVPafsLLGEDvn 1484
Cdd:PRK12316  3567 DVLKLE--QVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGP---VSGET-- 3639
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1485 avqlsqdaaamcsvaagivediyPCSPLQEGLMSLTAKRAGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQ 1564
Cdd:PRK12316  3640 -----------------------LLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVE 3696
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1565 ---HSELGLLQVVIEENIQW---TEPKSLEEYLSEDKAVSVGLGD-PLARYAFVKEACGGKRwFVWTIHHAVYDGWSLPL 1637
Cdd:PRK12316  3697 dagGWTAEHLPVELGGALLWraeLDDAEELERLGEEAQRSLDLADgPLLRALLATLADGSQR-LLLVIHHLVVDGVSWRI 3775
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1638 ILHAVKQVYsGGVLQWQP--------SFNAFIQ----YLGQQDLEATVAYWQTALADCEAVLfPTLPP---------TVT 1696
Cdd:PRK12316  3776 LLEDLQQAY-QQLLQGEAprlpaktsSFKAWAErlqeHARGEALKAELAYWQEQLQGVSSEL-PCDHPqgalqnrhaASV 3853
                         1770      1780      1790      1800      1810      1820      1830
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 1697 QPVADATVEYQCPPLSKATSDTTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNTPVTGVE--AMVGPTIATVPVRL 1772
Cdd:PRK12316  3854 QTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDlsRTVGWFTSLFPVRL 3931
PRK12467 PRK12467
peptide synthase; Provisional
2-1682 3.19e-173

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 607.16  E-value: 3.19e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL----EPSHIPSLRILVMGGE--QVN-SADWDRWPSSVQTINGYGPTECCIVCTGYT---SEQDFT 71
Cdd:PRK12467   747 GVTVLKIVPSHLQALlqasRVALPRPQRALVCGGEalQVDlLARVRALGPGARLINHYGPTETTVGVSTYElsdEERDFG 826
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   72 TGTIGTSIASVSWVVdpKDHG-RLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAwlleghgGYAGrqGRLYKTG 150
Cdd:PRK12467   827 NVPIGQPLANLGLYI--LDHYlNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPF-------GADG--GRLYRTG 895
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  151 DLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQlavEVVLPLGQKNHATLAAFI----QLDKGTHNA 226
Cdd:PRK12467   896 DLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLA-QPGVRE---AVVLAQPGDAGLQLVAYLvpaaVADGAEHQA 971
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  227 LLKEkvggddsiarvvflagVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASftaqqlaemrtSSQGPK 306
Cdd:PRK12467   972 TRDE----------------LKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAS-----------AVQATF 1024
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  307 RQPSTEAERTMQQLWARVLGIEPdsIGLDDSFFRLGGDSIAAIKLVGEARRT-GLQPSVADIFRHPTLAALASLETNQyn 385
Cdd:PRK12467  1025 VAPQTELEKRLAAIWADVLKVER--VGLTDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQ-- 1100
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  386 iTIEETPPLSLLGENADV----AQVRdeaaamcsvdgsaiedmylcsplQEGLMSLTTKRAGDYIMQdVLELRADVDEHA 461
Cdd:PRK12467  1101 -QQGAQPALPDVDRDQPLplsyAQER-----------------------QWFLWQLEPGSAAYHIPQ-ALRLKGPLDIEA 1155
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  462 FRAAWEYVVQSIAVLRTRIVQHSelGLLQVVVEEKMQWTESESLEEYLNEDKAASMGLGDR------------LARYALI 529
Cdd:PRK12467  1156 LERSFDALVARHESLRTTFVQED--GRTRQVIHPVGSLTLEEPLLLAADKDEAQLKVYVEAearqpfdleqgpLLRVGLL 1233
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  530 KeSCGGKRWFVWTIHHALYDGWSLPLVLDAVKQVYSGAALERQPSFNTF-IQYVS----QQDVKAAA------AYWQTAL 598
Cdd:PRK12467  1234 R-LAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALpIQYADyavwQRQWMDAGerarqlAYWKAQL 1312
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  599 ADCEAVLFPPL--PSTVTQPVADTTVKYQCPPS------PEVTSSNITTSTLIRAAWAIIASRYTSSEDIVFGTTVTGRN 670
Cdd:PRK12467  1313 GGEQPVLELPTdrPRPAVQSHRGARLAFELPPAlaeglrALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRN 1392
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  671 APITgvEAMVGPTIATVPLRVRpRKGQTvsAFLENLQQ--------QATEMIAYEQ--TGLQRIMKMGpgpqHACGFQTL 740
Cdd:PRK12467  1393 RAET--EGLIGFFVNTQVLRAE-VDGQA--SFQQLLQQvkqaaleaQAHQDLPFEQlvEALQPERSLS----HSPLFQVM 1463
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  741 LVvHPTDDVLSSDDTLG------EWHSRSdselqyfTTYALTIQCTLAVEGVQITASFDARVVEHWVVEKMLGQFSFVMQ 814
Cdd:PRK12467  1464 FN-HQRDDHQAQAQLPGlsveslSWESQT-------AQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQ 1535
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  815 QLAeAGVEKKVADIETTTLEDRQQ-LWVWNA---DMPPAvdRCIHDLFAEQARARPDASAVCAWDGELTYGELDELSSKL 890
Cdd:PRK12467  1536 GLV-ADPERRLGELDLLDEAERRQiLEGWNAthtGYPLA--RLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRL 1612
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  891 AAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSQHAMLFASSERHQ 970
Cdd:PRK12467  1613 AHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLR 1692
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  971 VTVSKVSTSQLPT--VVNFAkSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFD 1048
Cdd:PRK12467  1693 SLVLDQEDDWLEGysDSNPA-VNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFD 1771
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1049 ACIAEIITTLLYGGCICV--PSESDRRNNLAKAISTMDVNCALLTPSV--ARLLEPSAV---PSLKRLVLQGEQV---SF 1118
Cdd:PRK12467  1772 VSVWELFWPLINGARLVIapPGAHRDPEQLIQLIERQQVTTLHFVPSMlqQLLQMDEQVehpLSLRRVVCGGEALeveAL 1851
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1119 ADWNRWPGSVQTINGYGPTECSV------CcnTYSGKQGFKSGIIGTSVASLSW-VVDAGNHnrLAPLGSIGELLVEGPI 1191
Cdd:PRK12467  1852 RPWLERLPDTGLFNLYGPTETAVdvthwtC--RRKDLEGRDSVPIGQPIANLSTyILDASLN--PVPIGVAGELYLGGVG 1927
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1192 LARGYLNDIDKTEAAFIDDPawllegyEGHAGrrGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVRE 1271
Cdd:PRK12467  1928 LARGYLNRPALTAERFVADP-------FGTVG--SRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLRE 1998
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1272 cLPEARQLAVEVILPSGQKEhaLLAAFIQLDKGnhnalfeekaSGEDSMAQVVFLTGVEEELAKRLPEHMVPTILFTVKA 1351
Cdd:PRK12467  1999 -QGGVREAVVIAQDGANGKQ--LVAYVVPTDPG----------LVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLAR 2065
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1352 MPITTSGKIDRKRLQDIGASftvqqlaEMRTSSQGPKrqpsTEVEQTMQQLWAQVLSIEpnSIGLDDSFFRLGGDSIVAM 1431
Cdd:PRK12467  2066 MPLTPNGKLDRKALPAPDAS-------ELQQAYVAPQ----SELEQRLAAIWQDVLGLE--QVGLHDNFFELGGDSIISI 2132
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1432 KLVGEARRTGLQLSVADIFRHPRLVDLARVqnsqfssaaeevpafsllgedvnavqlSQDAAAMCSVAAGIVEDIYPCSP 1511
Cdd:PRK12467  2133 QVVSRARQAGIRFTPKDLFQHQTVQSLAAV---------------------------AQEGDGTVSIDQGPVTGDLPLLP 2185
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1512 LQEGLMSLTAKRAGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQH------SELGLLQVviEENIQWTEP- 1584
Cdd:PRK12467  2186 IQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEdggwsaMHRAPEQE--RRPLLWQVVv 2263
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1585 --KSLEEYLSEDKAVSVGLGD-PLARYAFVKEACGGKRwFVWTIHHAVYDGWSLPLILH----AVKQVYSGGVLQWQPSF 1657
Cdd:PRK12467  2264 adKEELEALCEQAQRSLDLEEgPLLRAVLATLPDGSQR-LLLVIHHLVVDGVSWRILLEdlqtAYRQLQGGQPVKLPAKT 2342
                         1770      1780      1790
                   ....*....|....*....|....*....|..
gi 1820002560 1658 NAF-------IQYLGQQDLEATVAYWQTALAD 1682
Cdd:PRK12467  2343 SAFkawaerlQTYAASAALADELGYWQAQLQG 2374
PRK05691 PRK05691
peptide synthase; Validated
4567-7363 9.91e-173

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 606.01  E-value: 9.91e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLvQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEhifrQTGAQVVLASA 4646
Cdd:PRK05691    41 LSYRDLDLRARTIAAAL-QARASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRHH----QERLLSIIADA 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4647 QYATLWTS--LGRSVVIVSEASTSQLP-----------VVTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSC 4713
Cdd:PRK05691   116 EPRLLLTVadLRDSLLQMEELAAANAPellcvdtldpaLAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANE 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4714 LGHGQAFGIT---DHTRVLQFASYTFDACIAEIITTLLCcGCICVPSDS----DRRNNLAKAINAM--------DVNWAL 4778
Cdd:PRK05691   196 QLIRHGFGIDlnpDDVIVSWLPLYHDMGLIGGLLQPIFS-GVPCVLMSPayflERPLRWLEAISEYggtisggpDFAYRL 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4779 LTPSVAR-MLDPCVVQSLKILVLGGEQVNSADWDRWPKSIQT--------INAYGPTECSICCTTYSGKQGFKS------ 4843
Cdd:PRK05691   275 CSERVSEsALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAAcgfdpdsfFASYGLAEATLFVSGGRRGQGIPAleldae 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4844 ---------GTiGTSIVSVSW--------VVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAFIDdpawlleg 4906
Cdd:PRK05691   355 alarnraepGT-GSVLMSCGRsqpghavlIVDPQSLEVLGD-NRVGEIWASGPSIAHGYWRNPEASAKTFVE-------- 424
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4907 yggHSGRqgRLYKTGDLvRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVRECLTEAKQ-----LAVEVIVPEGEGGY 4981
Cdd:PRK05691   425 ---HDGR--TWLRTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKgrvaaFAVNHQGEEGIGIA 498
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4982 AMLAAFVQlgddtyntlvkekaggDSLTVQVVfLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRK--RLR-EIG 5058
Cdd:PRK05691   499 AEISRSVQ----------------KILPPQAL-IKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSacRLRlADG 561
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5059 -----ASFTAQQLAEMRTSSQGPkrqpsTEAERTMQQLWTRVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRT-GLQ 5132
Cdd:PRK05691   562 sldsyALFPALQAVEAAQTAASG-----DELQARIAAIWCEQLKVE--QVAADDHFFLLGGNSIAATQVVARLRDElGID 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5133 LSVADVFRHPRLvdlayvqnsecssaaeevPAFSllggrAADTAQVSQDAAAMCSVDASSVEDMYPCSPLQEGLMSL--T 5210
Cdd:PRK05691   635 LNLRQLFEAPTL------------------AAFS-----AAVARQLAGGGAAQAAIARLPRGQALPQSLAQNRLWLLwqL 691
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5211 AKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEEKIQW--TESKRLEEYLREDKAVS 5288
Cdd:PRK05691   692 DPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALqrIDLSDLPEAEREARAAQ 771
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5289 MGLGDRLARYALIKEPY--------DGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGAV----------PERQPSFNA 5350
Cdd:PRK05691   772 IREEEARQPFDLEKGPLlrvtlvrlDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACqgqtaelaplPLGYADYGA 851
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5351 F-IQYLGQQDLEAATLYWQTALADCKAAL-FPT------------------LPPTVTQPVADTTVEYQCpppsqsatdiT 5410
Cdd:PRK05691   852 WqRQWLAQGEAARQLAYWKAQLGDEQPVLeLATdhprsarqahsaaryslrVDASLSEALRGLAQAHQA----------T 921
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5411 TSTLVRAAWAIVTSRYTSSDDVVFGatVTGRNAPIAGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAHEQ 5490
Cdd:PRK05691   922 LFMVLLAAFQALLHRYSGQGDIRIG--VPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQD 999
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5491 TGLQRIAKMSPGARHACGFQTLLVVQPTDdvLGS----DDMLGE---WRSYSEMQDfttyalmVQCTLAKDRV-EVTASF 5562
Cdd:PRK05691  1000 LPFEQLVEALPQAREQGLFQVMFNHQQRD--LSAlrrlPGLLAEelpWHSREAKFD-------LQLHSEEDRNgRLTLSF 1070
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5563 D--ARVIEQWVVEKMLRQFGFVMQQLAEAgAEKTVSDIETTTLEDRQQLWAWNQNVPPAIERCVHDLFTEQAKARPHAPA 5640
Cdd:PRK05691  1071 DyaAELFDAATIERLAEHFLALLEQVCED-PQRALGDVQLLDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIA 1149
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5641 IcAWDGE-LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTG 5719
Cdd:PRK05691  1150 L-VWDGGsLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG 1228
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5720 AQVVVTsaqHSARwIGTNHQVVTVSAGSLGQL---STLVNPVGLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWG 5796
Cdd:PRK05691  1229 VELLLT---QSHL-LERLPQAEGVSAIALDSLhldSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQW 1304
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5797 RGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRND--LVKAISTMDVSCALLTPSVARLL--EPSS 5872
Cdd:PRK05691  1305 MQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPqrIAELVQQYGVTTLHFVPPLLQLFidEPLA 1384
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5873 VP--TLQMLVLQGEQVSFADWNR----WPAsVQTINGYGPTECSICCNTY--SGKQGFKSGiIGTSVASV-SWVVDPENH 5943
Cdd:PRK05691  1385 AActSLRRLFSGGEALPAELRNRvlqrLPQ-VQLHNRYGPTETAINVTHWqcQAEDGERSP-IGRPLGNVlCRVLDAELN 1462
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5944 drLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypGHPGrqGRLYKTGDLVRYDANGNLVCLGRKDSQV 6023
Cdd:PRK05691  1463 --LLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPL-------GEDG--ARLYRTGDRARWNADGALEYLGRLDQQV 1531
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6024 KLRGQRVELGEVehhvreclpEARQLAVEVIlpsGQkdhamlaAFVQLEEGTQNALLDKEASGEDsmAQVVFLASVEEEL 6103
Cdd:PRK05691  1532 KLRGFRVEPEEI---------QARLLAQPGV---AQ-------AAVLVREGAAGAQLVGYYTGEA--GQEAEAERLKAAL 1590
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6104 AKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASfTAQQIAnmqtssqdpkrqPSTEAEQTMQKLWAQVLGieLNG 6183
Cdd:PRK05691  1591 AAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ-QREHVE------------PRTELQQQIAAIWREVLG--LPR 1655
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6184 IGLDDSFFRLGGDSIAAMKLVGEAR-RIGLQLSVADIFRYARLVDLASldtsqcnsaigEVPAFSLLGGRAADTAQVSQD 6262
Cdd:PRK05691  1656 VGLRDDFFALGGHSLLATQIVSRTRqACDVELPLRALFEASELGAFAE-----------QVARIQAAGERNSQGAIARVD 1724
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6263 AAAMCSVDASS-----VEDMYPCSPLqeglmsltakragdYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHS 6337
Cdd:PRK05691  1725 RSQPVPLSYSQqrmwfLWQMEPDSPA--------------YNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVD 1790
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6338 ELGLLQVVVEE--KIQWTESKRLEEYLREDKAVSmgLGD------------PLARYAIIKEAwGGKRWFVWTIHHALYDG 6403
Cdd:PRK05691  1791 GVPVQQVAEDSglRMDWQDFSALPADARQQRLQQ--LADseahqpfdlergPLLRACLVKAA-EREHYFVLTLHHIVTEG 1867
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6404 WSL---PRVLQAVKQAY---NGAVLETQPsfnafIQYL-----SQQDLEA-----TAAYWQTALADcEATLF-------- 6459
Cdd:PRK05691  1868 WAMdifARELGALYEAFlddRESPLEPLP-----VQYLdysvwQRQWLESgerqrQLDYWKAQLGN-EHPLLelpadrpr 1941
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6460 PPLPSSVKQLvadttveHQCPLPSRSTSDTTTSTLIR---------AAWAIVASRYTSSDDVVFGTTITGRNAPVTsiDA 6530
Cdd:PRK05691  1942 PPVQSHRGEL-------YRFDLSPELAARVRAFNAQRgltlfmtmtATLAALLYRYSGQRDLRIGAPVANRIRPES--EG 2012
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6531 IVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEMIAYEQTGLQQIAKMGPDPQHACG---FQTLLVVQP---------A 6598
Cdd:PRK05691  2013 LIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYnplFQVMCNVQRwefqqsrqlA 2092
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6599 G---DVLGSDDTLGKWRGYSGLQDfMTYALGVRCTLSaegvkiTASFD----ARVIEHWvvekmlgqfsfamQQLAEASA 6671
Cdd:PRK05691  2093 GmtvEYLVNDARATKFDLNLEVTD-LDGRLGCCLTYS------RDLFDepriARMAEHW-------------QNLLEALL 2152
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6672 D---RKVADIDITTTTDRQQLWAWNAELPL--AVDRCVHDLFTEQALARPNAPAVcAWDGE-LTYGELEALSTKLAGHLV 6745
Cdd:PRK05691  2153 GdpqQRLAELPLLAAAEQQQLLDSLAGEAGeaRLDQTLHGLFAAQAARTPQAPAL-TFAGQtLSYAELDARANRLARALR 2231
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6746 QLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR----------------------------------- 6790
Cdd:PRK05691  2232 ERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERlhymiedsgiglllsdralfealgelpagvarwcl 2311
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6791 ----------------------HEDILRQT-------------------------------------------------- 6798
Cdd:PRK05691  2312 eddaaalaaysdaplpflslpqHQAYLIYTsgstgkpkgvvvshgeiamhcqavierfgmraddcelhfysinfdaaser 2391
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6799 -------GAQVILAS------------------------------------AQNTTL----------------------- 6812
Cdd:PRK05691  2392 llvpllcGARVVLRAqgqwgaeeicqlireqqvsilgftpsygsqlaqwlaGQGEQLpvrmcitggealtgehlqrirqa 2471
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6813 FQSS--------NQTVVTVNRSsyiLFPDE---------------NREAYpfVRPSNAALAPLGSIGELLVEGPILARGY 6869
Cdd:PRK05691  2472 FAPQlffnaygpTETVVMPLAC---LAPEQleegaasvpigrvvgARVAY--ILDADLALVPQGATGELYVGGAGLAQGY 2546
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6870 LNDADKTAAAFVNDPAwlveghgKHPGrrGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRA 6949
Cdd:PRK05691  2547 HDRPGLTAERFVADPF-------AADG--GRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLE-HPAV 2616
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6950 TQMAVEVISPAGAAEQAKTMVVAFLQLNDEARDALlggnvpnddnlsaqvvfPAKVDEKLSNLLPSYMMPEVYFAVPQLP 7029
Cdd:PRK05691  2617 REAVVLALDTPSGKQLAGYLVSAVAGQDDEAQAAL-----------------REALKAHLKQQLPDYMVPAHLILLDSLP 2679
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7030 MMISGKTDRKRLreigasfTAQQLAEMRTSSQgpkrQPSTEAERTMQQLWARMLKVkaDSIGLDDSFFRLGGDSIVAMKL 7109
Cdd:PRK05691  2680 LTANGKLDRRAL-------PAPDPELNRQAYQ----APRSELEQQLAQIWREVLNV--ERVGLGDNFFELGGDSILSIQV 2746
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7110 VGEARRTGLQLSVADVFRHPRLVDLAYVQNSQCSSAAEEVPafsLLGEDvnpvqlsqdaaamcsvaasivkdiyPCSPLQ 7189
Cdd:PRK05691  2747 VSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGP---LQGAS-------------------------GLTPIQ 2798
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7190 EGLISLTAKRAGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSE--LGLLQVVVEEKIQWT-------ES 7260
Cdd:PRK05691  2799 HWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGrwQAEYRAVTAQELLWQvtvadfaEC 2878
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7261 EALeeYLKEDKAVSMGLGdPLAHYALVKEAWGGKRWFVwTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNA----- 7335
Cdd:PRK05691  2879 AAL--FADAQRSLDLQQG-PLLRALLVDGPQGQQRLLL-AIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAktsaf 2954
                         3210      3220      3230
                   ....*....|....*....|....*....|....
gi 1820002560 7336 ------FIQYLGQQDLEATAAYWQTALSDCEAVL 7363
Cdd:PRK05691  2955 rdwaarLQAYAGSESLREELGWWQAQLGGPRAEL 2988
PRK05691 PRK05691
peptide synthase; Validated
3149-5378 1.70e-172

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 605.24  E-value: 1.70e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3149 LCLDINHAIIDAHSRGILMHDLQEAYDA-------NLNPQSTSFRDFASYIKQQ-SQEEAGR---YWAEYLDGVEPCFFP 3217
Cdd:PRK05691   803 LLVTLHHIVADGWSLNILLDEFSRLYAAacqgqtaELAPLPLGYADYGAWQRQWlAQGEAARqlaYWKAQLGDEQPVLEL 882
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3218 SLGDSGGA---NTIPR-TVEVPSIDSSAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRdlPIHNVNSI 3293
Cdd:PRK05691   883 ATDHPRSArqaHSAARySLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANR--PRLETQGL 960
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3294 FGPLISILPCRIHLHKQLTVLEALKTVQENYASSLSFQTFPLASM-HSFLGLGTSALFNTALSLQRIDDIGPCS-----A 3367
Cdd:PRK05691   961 VGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLvEALPQAREQGLFQVMFNHQQRDLSALRRlpgllA 1040
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3368 SEITLKMKEG-----LDPTEYN---ITLSAGYSKDAIDISMTfragcmdlvqaKRLASNFSQAIKAVTTEPHSRIYSLDI 3439
Cdd:PRK05691  1041 EELPWHSREAkfdlqLHSEEDRngrLTLSFDYAAELFDAATI-----------ERLAEHFLALLEQVCEDPQRALGDVQL 1109
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3440 LTYNESKKIWGWNADVPPAIERCVHDLFTEQAKARPHAPAIcAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCF 3518
Cdd:PRK05691  1110 LDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIAL-VWDGGsLDYAELHAQANRLAHYLRDKGVGPDVCVAIAA 1188
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3519 EKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSKALS-----SQLPAV 3593
Cdd:PRK05691  1189 ERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHldswpSQAPGL 1268
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3594 vdstntSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCI 3673
Cdd:PRK05691  1269 ------HLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRL 1342
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3674 CVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL----DPGLIPSLKILAIGGEQSSSADWNR----WPGsVQKIHVY 3743
Cdd:PRK05691  1343 VLAGPGEHRDpqRIAELVQQYGVTTLHFVPPLLQLFidepLAAACTSLRRLFSGGEALPAELRNRvlqrLPQ-VQLHNRY 1421
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3744 GPTECCIFCTGY-TTKQGFEPSTIGTSVASV-SWVVDPENHnrLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPA 3821
Cdd:PRK05691  1422 GPTETAINVTHWqCQAEDGERSPIGRPLGNVlCRVLDAELN--LLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPL 1499
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3822 wllegypGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvreclpeARQLAVEVIlpsGQkdh 3901
Cdd:PRK05691  1500 -------GEDG--ARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQ---------ARLLAQPGV---AQ--- 1555
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3902 amlaAFVQLEEGTQNALLDKEAGGEDsmAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASf 3981
Cdd:PRK05691  1556 ----AAVLVREGAAGAQLVGYYTGEA--GQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ- 1628
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3982 taqqlaemrtssQGPKRQPSTEAEQTMQQLWAQVLSLGAdiIGLDDSFFRLGGDSIAAMKLVGEAR-RMGLHLSVADIFR 4060
Cdd:PRK05691  1629 ------------QREHVEPRTELQQQIAAIWREVLGLPR--VGLRDDFFALGGHSLLATQIVSRTRqACDVELPLRALFE 1694
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4061 HPKLADFAgiqitqcssgtEEVPAYSLLGEDEDVmqvckdvAAMCSVDASaitDVYPCSPLQEGLMSL--TAKRAGDYIM 4138
Cdd:PRK05691  1695 ASELGAFA-----------EQVARIQAAGERNSQ-------GAIARVDRS---QPVPLSYSQQRMWFLwqMEPDSPAYNV 1753
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4139 QTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELGLLQVVVEE--RIQWTESESLEEYPREDKAVSMGvgDR--- 4213
Cdd:PRK05691  1754 GGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSglRMDWQDFSALPADARQQRLQQLA--DSeah 1831
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4214 ---------LARYALIKepYDGGKRWFVWTMHHALYDGWSLPRILHAVKQAYSGVVLERQPSFNAF-IQYL-----SQQD 4278
Cdd:PRK05691  1832 qpfdlergpLLRACLVK--AAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLpVQYLdysvwQRQW 1909
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4279 PEAAA-----AYWQTALVDCKAALfpTLPPTVTQPVADT----TVEYQCPP-------PSQSATDITTSTLARAAWAIVT 4342
Cdd:PRK05691  1910 LESGErqrqlDYWKAQLGNEHPLL--ELPADRPRPPVQShrgeLYRFDLSPelaarvrAFNAQRGLTLFMTMTATLAALL 1987
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4343 SRYTSSDDVVFGATVTGRNAPIAggEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQATDMIAHEQTGLQRIAKMSPGA 4422
Cdd:PRK05691  1988 YRYSGQRDLRIGAPVANRIRPES--EGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPP 2065
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4423 RHACG---FQTLLVVQptddvlgsddmlgEWrsysEMQDFTTYALMVQCVLVKD-----------------RVG--VTAS 4480
Cdd:PRK05691  2066 RSAAYnplFQVMCNVQ-------------RW----EFQQSRQLAGMTVEYLVNDaratkfdlnlevtdldgRLGccLTYS 2128
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4481 FD-------ARVIEQW--VVEKMLrqfgfvmqqladAGEEKKVAGIETTTTGDRQQLWAWNQDVP--PAIERCVHDQFAE 4549
Cdd:PRK05691  2129 RDlfdepriARMAEHWqnLLEALL------------GDPQQRLAELPLLAAAEQQQLLDSLAGEAgeARLDQTLHGLFAA 2196
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4550 QARARPDTPAIcAWDGE-LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 4628
Cdd:PRK05691  2197 QAARTPQAPAL-TFAGQtLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLE 2275
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4629 RHEHIFRQTGAQVVLAsaqYATLWTSLGRSVVIVS----EASTSQLPVVTKTADPSVN-PGNAAYAIFTSGSTGIPKGVV 4703
Cdd:PRK05691  2276 RLHYMIEDSGIGLLLS---DRALFEALGELPAGVArwclEDDAAALAAYSDAPLPFLSlPQHQAYLIYTSGSTGKPKGVV 2352
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4704 LEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSD-RRNNLAKAINAMDVNWALLTPS 4782
Cdd:PRK05691  2353 VSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQwGAEEICQLIREQQVSILGFTPS 2432
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4783 VARMLDPCVVQ-----SLKILVLGGEQVNSADWDRWPKSIQT---INAYGPTECSI----CCTTYSGKQGFKSGTIGTSI 4850
Cdd:PRK05691  2433 YGSQLAQWLAGqgeqlPVRMCITGGEALTGEHLQRIRQAFAPqlfFNAYGPTETVVmplaCLAPEQLEEGAASVPIGRVV 2512
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4851 VS-VSWVVDPEnhnrLAPL--GSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygGHSGrqGRLYKTGDLVRYD 4927
Cdd:PRK05691  2513 GArVAYILDAD----LALVpqGATGELYVGGAGLAQGYHDRPGLTAERFVADPF-------AADG--GRLYRTGDLVRLR 2579
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4928 ADGNLVYLGRKDSQVKLRGQRVELGEVEHHVRE--CLTEAKQLAVEviVPEGEggyaMLAAFvqlgddtyntLVKEKAGG 5005
Cdd:PRK05691  2580 ADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEhpAVREAVVLALD--TPSGK----QLAGY----------LVSAVAGQ 2643
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5006 DSlTVQVVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLreigasfTAQQLAEMRTSSQgpkrQPSTEAE 5085
Cdd:PRK05691  2644 DD-EAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL-------PAPDPELNRQAYQ----APRSELE 2711
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5086 RTMQQLWTRVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRTGLQLSVADVFRHPRLVDLAYVQNSECSSAAEEVPaf 5165
Cdd:PRK05691  2712 QQLAQIWREVLNVE--RVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGP-- 2787
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5166 slLGGRAADTaqvsqdaaamcsvdassvedmypcsPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLT 5245
Cdd:PRK05691  2788 --LQGASGLT-------------------------PIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHH 2840
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5246 AALRTRIVQHSE--LGLLQVVVEEKIQWTE-----SKRLEEYLREDKAVSMGLGDrLARYALIKEPyDGGKRWFVwTIHH 5318
Cdd:PRK05691  2841 DALRLRFSQADGrwQAEYRAVTAQELLWQVtvadfAECAALFADAQRSLDLQQGP-LLRALLVDGP-QGQQRLLL-AIHH 2917
                         2330      2340      2350      2360      2370      2380      2390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 5319 ALYDGWS---LPRILQAVKQIYSGAVPERQPS-------FNAFIQ-YLGQQDLEAATLYWQTALADCKAAL 5378
Cdd:PRK05691  2918 LVVDGVSwrvLLEDLQALYRQLSAGAEPALPAktsafrdWAARLQaYAGSESLREELGWWQAQLGGPRAEL 2988
PRK05691 PRK05691
peptide synthase; Validated
5937-8408 1.80e-169

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 595.22  E-value: 1.80e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5937 VVDPENHDRLAPlGSIGELLVEGPILARGYLNDIQKTAAVFI--DDPAWLLEGYPGHPgRQGRLYKTGDLvrydangnlv 6014
Cdd:PRK05691   383 IVDPQSLEVLGD-NRVGEIWASGPSIAHGYWRNPEASAKTFVehDGRTWLRTGDLGFL-RDGELFVTGRL---------- 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6015 clgrKDSQVkLRGQRVELGEVEHHVRECLPEARQLAVEVILPSGQKDHAMLAAfVQLEEGTQNALLDKEASgeDSMAQVV 6094
Cdd:PRK05691   451 ----KDMLI-VRGHNLYPQDIEKTVEREVEVVRKGRVAAFAVNHQGEEGIGIA-AEISRSVQKILPPQALI--KSIRQAV 522
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6095 FLASVEeelakrlpehmVPTVFFsLLH---FPTTTSGKTDRK--RLREIGASFTA-QQIANMQTSSQDPKRQPSTEAEQT 6168
Cdd:PRK05691   523 AEACQE-----------APSVVL-LLNpgaLPKTSSGKLQRSacRLRLADGSLDSyALFPALQAVEAAQTAASGDELQAR 590
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6169 MQKLWAQVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEAR-RIGLQLSVADIFRYARLvdlasldtsqcnsaigevPAFS 6247
Cdd:PRK05691   591 IAAIWCEQLKVE--QVAADDHFFLLGGNSIAATQVVARLRdELGIDLNLRQLFEAPTL------------------AAFS 650
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6248 llggrAADTAQVSQDAAAMCSVDASSVEDMYPCSPLQEGLMSL--TAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQL 6325
Cdd:PRK05691   651 -----AAVARQLAGGGAAQAAIARLPRGQALPQSLAQNRLWLLwqLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVER 725
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6326 TAALRTRIVQHSELGLLQVVVEEKIQW----------TESKRLEEYLREDKA---VSMGLGdPLARYAIIKEAWGGKRWF 6392
Cdd:PRK05691   726 HESLRTRFYERDGVALQRIDAQGEFALqridlsdlpeAEREARAAQIREEEArqpFDLEKG-PLLRVTLVRLDDEEHQLL 804
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6393 VwTIHHALYDGWSLPRVLQAVKQAYNGAV----LETQP---SFNAFI----QYLSQQDLEATAAYWQTALADCEATLFPP 6461
Cdd:PRK05691   805 V-TLHHIVADGWSLNILLDEFSRLYAAACqgqtAELAPlplGYADYGawqrQWLAQGEAARQLAYWKAQLGDEQPVLELA 883
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6462 -------------------LPSSVKQLVADTTVEHQCPLpsrstsdtttSTLIRAAWAIVASRYTSSDDVVFGttITGRN 6522
Cdd:PRK05691   884 tdhprsarqahsaaryslrVDASLSEALRGLAQAHQATL----------FMVLLAAFQALLHRYSGQGDIRIG--VPNAN 951
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6523 APVTSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEMIAYEQTGLQQIAKMGPDPQHACGFQTLLVVQpagdvl 6602
Cdd:PRK05691   952 RPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQGLFQVMFNHQ------ 1025
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6603 gsDDTLGKWRGYSGL--QDFMTYALGVRCTL---SAEGV--KITASFD--ARVIEHWVVEKMLGQFSFAMQQLAEAsADR 6673
Cdd:PRK05691  1026 --QRDLSALRRLPGLlaEELPWHSREAKFDLqlhSEEDRngRLTLSFDyaAELFDAATIERLAEHFLALLEQVCED-PQR 1102
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6674 KVADIDITTTTDRQQLWAWNAELPLAVDRCVHDLFTEQALARPNAPAVcAWDGE-LTYGELEALSTKLAGHLVQLGVKPE 6752
Cdd:PRK05691  1103 ALGDVQLLDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIAL-VWDGGsLDYAELHAQANRLAHYLRDKGVGPD 1181
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6753 DVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDILRQTGAQVILASA------------------------- 6807
Cdd:PRK05691  1182 VCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQShllerlpqaegvsaialdslhldsw 1261
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6808 --------------------------------------------QNTTLFQSSN-------------------------- 6817
Cdd:PRK05691  1262 psqapglhlhgdnlayviytsgstgqpkgvgnthaalaerlqwmQATYALDDSDvlmqkapisfdvsvwecfwplitgcr 1341
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6818 ------------QTVVTVNRSSYI-----------LFPDE-------------------------------------NR- 6836
Cdd:PRK05691  1342 lvlagpgehrdpQRIAELVQQYGVttlhfvppllqLFIDEplaaactslrrlfsggealpaelrnrvlqrlpqvqlhNRy 1421
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6837 -------------------EAYPFVRP----------SNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPAwl 6887
Cdd:PRK05691  1422 gptetainvthwqcqaedgERSPIGRPlgnvlcrvldAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPL-- 1499
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6888 veghgkhpGRRG-RLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAGAAEqa 6966
Cdd:PRK05691  1500 --------GEDGaRLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA-QPGVAQAAVLVREGAAGAQ-- 1568
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6967 ktmVVAFLQLNDEARDAllggnvpnddnlsaqvvfPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREIGA 7046
Cdd:PRK05691  1569 ---LVGYYTGEAGQEAE------------------AERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVW 1627
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7047 SftaqqlaemrtssQGPKRQPSTEAERTMQQLWARMLKVKadSIGLDDSFFRLGGDSIVAMKLVGEAR-RTGLQLSVADV 7125
Cdd:PRK05691  1628 Q-------------QREHVEPRTELQQQIAAIWREVLGLP--RVGLRDDFFALGGHSLLATQIVSRTRqACDVELPLRAL 1692
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7126 FRHPRLVDLA-YVQNSQCSSAAEEVPAFSLLGEDvNPVQLSQDAAAMCsvaasIVKDIYPCSPLqeglisltakragdYI 7204
Cdd:PRK05691  1693 FEASELGAFAeQVARIQAAGERNSQGAIARVDRS-QPVPLSYSQQRMW-----FLWQMEPDSPA--------------YN 1752
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7205 MQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVVVEE--KIQWTESEALEEYLKEDKAVSmgLGD--- 7279
Cdd:PRK05691  1753 VGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSglRMDWQDFSALPADARQQRLQQ--LADsea 1830
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7280 ---------PLAHYALVKEAwGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAF-IQYLG-----QQD 7344
Cdd:PRK05691  1831 hqpfdlergPLLRACLVKAA-EREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLpVQYLDysvwqRQW 1909
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7345 LEA-----TAAYWQTALSDCEAVLfpPLPSTVTQPVADT----TVEYQCPP-------LSKATLDTTTSTLIRAAWAIVT 7408
Cdd:PRK05691  1910 LESgerqrQLDYWKAQLGNEHPLL--ELPADRPRPPVQShrgeLYRFDLSPelaarvrAFNAQRGLTLFMTMTATLAALL 1987
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7409 SCYTSSDDVVYGTTVTGRNAPIAgvEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIAKLGSGP 7488
Cdd:PRK05691  1988 YRYSGQRDLRIGAPVANRIRPES--EGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPP 2065
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7489 RHACG---FQTLLVVQpvddvlgsddmlgEW-----RSYSKMQdfTTY----ALMVQFTLAAE--------GVQITASFD 7548
Cdd:PRK05691  2066 RSAAYnplFQVMCNVQ-------------RWefqqsRQLAGMT--VEYlvndARATKFDLNLEvtdldgrlGCCLTYSRD 2130
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7549 -------ARVIEHW--VLEKMLrqfsfimqqlaeASEDSKVADIDTTTPEDRQQLWAWNADVP--PAIERCVHDLFAEQA 7617
Cdd:PRK05691  2131 lfdepriARMAEHWqnLLEALL------------GDPQQRLAELPLLAAAEQQQLLDSLAGEAgeARLDQTLHGLFAAQA 2198
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7618 RARPGAPAIcAWDGE-LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 7696
Cdd:PRK05691  2199 ARTPQAPAL-TFAGQtLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERL 2277
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7697 EEIFEQTGAQVVVASA----------QYSARWTssschVVTVSKALSSQLPAVVDSTNTsvrPENAAYIIFTSGSTGVPK 7766
Cdd:PRK05691  2278 HYMIEDSGIGLLLSDRalfealgelpAGVARWC-----LEDDAAALAAYSDAPLPFLSL---PQHQAYLIYTSGSTGKPK 2349
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7767 GVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSD-RRNSLAKAISTMDVNWAFL 7845
Cdd:PRK05691  2350 GVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQwGAEEICQLIREQQVSILGF 2429
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7846 TPSVARLLDPGLIPSLKILAI-----GGEQSSSADWNRWPGSVQK---IHVYGPTECCIF----CTGYTTKQGFEPSTIG 7913
Cdd:PRK05691  2430 TPSYGSQLAQWLAGQGEQLPVrmcitGGEALTGEHLQRIRQAFAPqlfFNAYGPTETVVMplacLAPEQLEEGAASVPIG 2509
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7914 TSV-ASVSWVVDPEnhnrLAPL--GSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLV 7990
Cdd:PRK05691  2510 RVVgARVAYILDAD----LALVpqGATGELYVGGAGLAQGYHDRPGLTAERFVADPF-------AADG--GRLYRTGDLV 2576
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7991 QYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVRE--CLPEARQLAVEviLPSGQknhamlavfvQLgkgthIAHLEEK 8068
Cdd:PRK05691  2577 RLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEhpAVREAVVLALD--TPSGK----------QL-----AGYLVSA 2639
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8069 AGGEDSMAQVVFLTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGASFTAQQLAetqtssqgpkrQPLT 8148
Cdd:PRK05691  2640 VAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQ-----------APRS 2708
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8149 EAEQTMQQLWARVLGIDAdiIGLDDSFFRLGGDSIAAMKLVGEARRTGLQLSVADIFRHPRLIDLASLKSTFCNSVVEEV 8228
Cdd:PRK05691  2709 ELEQQLAQIWREVLNVER--VGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQG 2786
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8229 PafslLSpvmkdamfsvtepfGPSlridditdvvPASYIQQFYIATGVRAPREAFNYPFIDLSDAVDIQVLQASCSALLE 8308
Cdd:PRK05691  2787 P----LQ--------------GAS----------GLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVE 2838
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8309 HFPILRTHFVYFQGKL---YQVIPRHQDL---PFSIFEVNGALAEESQaihiRDLD-QTSPL--GLptsftLVRNASGMN 8379
Cdd:PRK05691  2839 HHDALRLRFSQADGRWqaeYRAVTAQELLwqvTVADFAECAALFADAQ----RSLDlQQGPLlrAL-----LVDGPQGQQ 2909
                         2810      2820
                   ....*....|....*....|....*....
gi 1820002560 8380 RLIIRLSHAQYDGVCMPVIWASLASIYQQ 8408
Cdd:PRK05691  2910 RLLLAIHHLVVDGVSWRVLLEDLQALYRQ 2938
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
4115-4509 1.10e-167

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 524.17  E-value: 1.10e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4115 VYPCSPLQEGLMSLTAKRAGDYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELGLLQVVV-EERIQWTES 4193
Cdd:cd19545      1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVkESPISWTES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4194 ESLEEYPREDKAVSMGVGDRLARYALIKEPydGGKRWFVWTMHHALYDGWSLPRILHAVKQAYSGVVLERQPSFNAFIQY 4273
Cdd:cd19545     81 TSLDEYLEEDRAAPMGLGGPLVRLALVEDP--DTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRFVKY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4274 LSQQDPEAAAAYWQTALVDCKAALFPTLPPTVTQPVADTTVEYQCPPPSQSATDITTSTLARAAWAIVTSRYTSSDDVVF 4353
Cdd:cd19545    159 LRQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSASSGVTLATVLRAAWALVLSRYTGSDDVVF 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4354 GATVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQATDMIAHEQTGLQRIAKMSPGARHACGFQTLLV 4433
Cdd:cd19545    239 GVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDARAACNFQTLLV 318
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 4434 VQPTDDVLGSDDM-LGEWRSYSEMQDFTTYALMVQCVLVKDRVGVTASFDARVIEQWVVEKMLRQFGFVMQQLADAG 4509
Cdd:cd19545    319 VQPALPSSTSESLeLGIEEESEDLEDFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
6277-6669 7.03e-167

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 521.86  E-value: 7.03e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6277 MYPCSPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVV-EEKIQWTES 6355
Cdd:cd19545      1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVkESPISWTES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6356 KRLEEYLREDKAVSMGLGDPLARYAIIKEAwGGKRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSFNAFIQYL 6435
Cdd:cd19545     81 TSLDEYLEEDRAAPMGLGGPLVRLALVEDP-DTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRFVKYL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6436 SQQDLEATAAYWQTALADCEATLFPPLPSSVKQLVADTTVEHQCPLPSRSTSDTTTSTLIRAAWAIVASRYTSSDDVVFG 6515
Cdd:cd19545    160 RQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSASSGVTLATVLRAAWALVLSRYTGSDDVVFG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6516 TTITGRNAPVTSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEMIAYEQTGLQQIAKMGPDPQHACGFQTLLVV 6595
Cdd:cd19545    240 VTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDARAACNFQTLLVV 319
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 6596 QPAGDVLGSDD-TLGKWRGYSGLQDFMTYALGVRCTLSAEGVKITASFDARVIEHWVVEKMLGQFSFAMQQLAEA 6669
Cdd:cd19545    320 QPALPSSTSESlELGIEEESEDLEDFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASA 394
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
7182-7574 1.88e-164

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 514.92  E-value: 1.88e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7182 IYPCSPLQEGLISLTAKRAGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVVV-EEKIQWTES 7260
Cdd:cd19545      1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVkESPISWTES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7261 EALEEYLKEDKAVSMGLGDPLAHYALVKEAwGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAFIQYL 7340
Cdd:cd19545     81 TSLDEYLEEDRAAPMGLGGPLVRLALVEDP-DTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRFVKYL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7341 GQQDLEATAAYWQTALSDCEAVLFPPLPSTVTQPVADTTVEYQCPPLSKATLDTTTSTLIRAAWAIVTSCYTSSDDVVYG 7420
Cdd:cd19545    160 RQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSASSGVTLATVLRAAWALVLSRYTGSDDVVFG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7421 TTVTGRNAPIAGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIAKLGSGPRHACGFQTLLVV 7500
Cdd:cd19545    240 VTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDARAACNFQTLLVV 319
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 7501 QPVDDVLGSDDM-LGEWRSYSKMQDFTTYALMVQFTLAAEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLAEA 7574
Cdd:cd19545    320 QPALPSSTSESLeLGIEEESEDLEDFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASA 394
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
1506-1897 2.10e-162

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 509.15  E-value: 2.10e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1506 IYPCSPLQEGLMSLTAKRAGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQVVI-EENIQWTEP 1584
Cdd:cd19545      1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVkESPISWTES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1585 KSLEEYLSEDKAVSVGLGDPLARYAFVKEAcGGKRWFVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQWQPSFNAFIQYL 1664
Cdd:cd19545     81 TSLDEYLEEDRAAPMGLGGPLVRLALVEDP-DTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRFVKYL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1665 GQQDLEATVAYWQTALADCEAVLFPTLPPTVTQPVADATVEYQCPPLSKATSDTTTSTLIRAAWAIVTSRYTTSDDVVFG 1744
Cdd:cd19545    160 RQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSASSGVTLATVLRAAWALVLSRYTGSDDVVFG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1745 TTVTGRNTPVTGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAHEQTGLQRIAKMGQGPQHACSFQTLLVV 1824
Cdd:cd19545    240 VTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDARAACNFQTLLVV 319
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 1825 QPVDDVLDNTLGE---WRDHSELQEFTTYTLMLQCMLAAEGVQITASFDTRVIEKWVVEKMLRQFSFIMQQLAEAG 1897
Cdd:cd19545    320 QPALPSSTSESLElgiEEESEDLEDFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
424-820 1.51e-160

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 503.75  E-value: 1.51e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  424 MYLCSPLQEGLMSLTTKRAGDYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQVVV-EEKMQWTES 502
Cdd:cd19545      1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVkESPISWTES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  503 ESLEEYLNEDKAASMGLGDRLARYALIKEScGGKRWFVWTIHHALYDGWSLPLVLDAVKQVYSGAALERQPSFNTFIQYV 582
Cdd:cd19545     81 TSLDEYLEEDRAAPMGLGGPLVRLALVEDP-DTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRFVKYL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  583 SQQDVKAAAAYWQTALADCEAVLFPPLPSTVTQPVADTTVKYQCPpSPEVTSSNITTSTLIRAAWAIIASRYTSSEDIVF 662
Cdd:cd19545    160 RQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSIS-LPSSASSGVTLATVLRAAWALVLSRYTGSDDVVF 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  663 GTTVTGRNAPITGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTGLQRIMKMGPGPQHACGFQTLLV 742
Cdd:cd19545    239 GVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDARAACNFQTLLV 318
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560  743 VHPTDDvlSSDDTLGEWHSRSDSE-LQYFTTYALTIQCTLAVEGVQITASFDARVVEHWVVEKMLGQFSFVMQQLAEAG 820
Cdd:cd19545    319 VQPALP--SSTSESLELGIEEESEdLEDFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
PRK12467 PRK12467
peptide synthase; Provisional
5176-6229 1.49e-149

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 529.35  E-value: 1.49e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5176 AQVSQDAAAMCSVDASSVEDMYPCSPLQEGLM--SLTAKRAGDYIMQsvleLRVDV---DEDAFRAAWEHVVQLTAALRT 5250
Cdd:PRK12467  2626 AGLSQEQLDRLPVAVGDIEDIYPLSPMQQGMLfhTLYEGGAGDYINQ----MRVDVeglDVERFRTAWQAVIDRHEILRS 2701
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5251 RIVQHSELGL-LQVVVEE------KIQWTESKRLEEYLRedkavSMGLGDRLARYALIKEPY--------DGGKRWFVWT 5315
Cdd:PRK12467  2702 GFLWDGELEEpLQVVYKQarlpfsRLDWRDRADLEQALD-----ALAAADRQQGFDLLSAPLlrltlvrtGEDRHHLIYT 2776
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5316 IHHALYDGWSLPRILQAVKQIYSG-AVPERQPSFNAFIQYLGQQDLEAATLYWQTALADCK--AALFPTLPPTVTQPVAD 5392
Cdd:PRK12467  2777 NHHILMDGWSGSQLLGEVLQRYFGqPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEepTRLARALYPAPAEAVAG 2856
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5393 TTVEYQCPPPSQS--------ATDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGVEAMVGPTIATVPLRVC 5464
Cdd:PRK12467  2857 HGAHYLHLDATQTrqliefarRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIAS 2936
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5465 LQKDQTVSTLLECLQQQSTDMIAHEQTGLQRIAKMSPGARHACgFQTLLVVQ--PTDDVL---GSDDM-LGEWRSysemQ 5538
Cdd:PRK12467  2937 PRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEAL-FDSILVFEnyPISEALkqgAPSGLrFGAVSS----R 3011
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5539 DFTTYALMVQCTLAkDRVEVTASFDARVIEQWVVEKMLRQFGFVMQQLAEAGAEkTVSDIETTTLEDRQQLW-AWN-QNV 5616
Cdd:PRK12467  3012 EQTNYPLTLAVGLG-DTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAA-RLGELPTLAAHERRQVLhAWNaTAA 3089
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5617 PPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAG 5696
Cdd:PRK12467  3090 AYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAG 3169
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5697 GAFVPLDPDHPASRHEDTFRHTGAQVVVTSAQHSARW-IGTNHQVVTVSAGSLGQLSTlVNPVGLpAIPENAVYIMFTSG 5775
Cdd:PRK12467  3170 GAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLpAPAGDTALTLDRLDLNGYSE-NNPSTR-VMGENLAYVIYTSG 3247
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5776 STGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVpSDSDRRN--DLVKAISTM 5853
Cdd:PRK12467  3248 STGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV-RDNDLWDpeELWQAIHAH 3326
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5854 DVSCALLTPSVARLL----EPSSVPTLQMLVLQGEQV---SFADWNRWPASVQTINGYGPTECSI------CcnTYSGKQ 5920
Cdd:PRK12467  3327 RISIACFPPAYLQQFaedaGGADCASLDIYVFGGEAVppaAFEQVKRKLKPRGLTNGYGPTEAVVtvtlwkC--GGDAVC 3404
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5921 GFKSGIIGTSVASVSWVVdPENHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPawllegypgHPGRQGRLYK 6000
Cdd:PRK12467  3405 EAPYAPIGRPVAGRSIYV-LDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP---------FSGSGGRLYR 3474
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6001 TGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAVEVILPSGQKDhamLAAFVQLeegtqnall 6080
Cdd:PRK12467  3475 TGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQ-HPSVREAVVLARDGAGGKQ---LVAYVVP--------- 3541
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6081 dkEASGEDsmaqvvFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQIAnmqtssqdpkrq 6160
Cdd:PRK12467  3542 --ADPQGD------WRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA------------ 3601
                         1050      1060      1070      1080      1090      1100      1110
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6161 PSTEAEQTMQKLWAQVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARR-IGLQLSVADIFRYARLVDLA 6229
Cdd:PRK12467  3602 PRSEVEQQLAAIWADVLGVE--QVGVTDNFFELGGDSLLALQVLSRIRQsLGLKLSLRDLMSAPTIAELA 3669
PRK12467 PRK12467
peptide synthase; Provisional
4107-5158 1.06e-148

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 526.27  E-value: 1.06e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4107 VDASAITDVYPCSPLQEGLM--SLTAKRAGDYIMQTVLELRAdVNEDAFRAAWELVVQLTAVLRTRIVQHSELGL-LQVV 4183
Cdd:PRK12467  2638 VAVGDIEDIYPLSPMQQGMLfhTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGELEEpLQVV 2716
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4184 VEE------RIQWTE----SESLEEYPREDKAVSMGVGDR-LARYALIKEpyDGGKRWFVWTMHHALYDGWSLPRILHAV 4252
Cdd:PRK12467  2717 YKQarlpfsRLDWRDradlEQALDALAAADRQQGFDLLSApLLRLTLVRT--GEDRHHLIYTNHHILMDGWSGSQLLGEV 2794
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4253 KQAYSGVVLERQPS-FNAFIQYLSQQDPEAAAAYWQTALVDCK--AALFPTLPPTVTQPVADTTVEYQCPPPSQS----- 4324
Cdd:PRK12467  2795 LQRYFGQPPPAREGrYRDYIAWLQAQDAEASEAFWKEQLAALEepTRLARALYPAPAEAVAGHGAHYLHLDATQTrqlie 2874
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4325 ---ATDITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQA 4401
Cdd:PRK12467  2875 farRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQN 2954
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4402 TDMIAHEQTGLQRIAKMSPGARHACgFQTLLVVQ--PTDDVL---GSDDM-LGEWRSysemQDFTTYALMVqCVLVKDRV 4475
Cdd:PRK12467  2955 LALREFEHTPLADIQRWAGQGGEAL-FDSILVFEnyPISEALkqgAPSGLrFGAVSS----REQTNYPLTL-AVGLGDTL 3028
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4476 GVTASFDARVIEQWVVEKMLRQFGFVMQQLADAGEEKkVAGIETTTTGDRQQLW-AWN-QDVPPAIERCVHDQFAEQARA 4553
Cdd:PRK12467  3029 ELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAAR-LGELPTLAAHERRQVLhAWNaTAAAYPSERLVHQLIEAQVAR 3107
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4554 RPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHI 4633
Cdd:PRK12467  3108 TPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYM 3187
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4634 FRQTGAQVVLASAQyatLWTSLG-----RSVVIVSEASTSQLPvvtKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKA 4708
Cdd:PRK12467  3188 IEDSGVKLLLTQAH---LLEQLPapagdTALTLDRLDLNGYSE---NNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGA 3261
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4709 VVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVpSDSDRRN--NLAKAINAMDVNWALLTPSVARM 4786
Cdd:PRK12467  3262 LANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV-RDNDLWDpeELWQAIHAHRISIACFPPAYLQQ 3340
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4787 L----DPCVVQSLKILVLGGEQV---NSADWDRWPKSIQTINAYGPTECSICCTTY----SGKQGFKSGTIGTSIVSVSW 4855
Cdd:PRK12467  3341 FaedaGGADCASLDIYVFGGEAVppaAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWkcggDAVCEAPYAPIGRPVAGRSI 3420
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4856 VVDPENHNRlAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawllegyggHSGRQGRLYKTGDLVRYDADGNLVYL 4935
Cdd:PRK12467  3421 YVLDGQLNP-VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP---------FSGSGGRLYRTGDLARYRADGVIEYL 3490
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4936 GRKDSQVKLRGQRVELGEVEHHVREclTEAKQLAVeVIVPEGEGGyAMLAAFVqlgddtyntlVKEKAGGDsltvqvvFL 5015
Cdd:PRK12467  3491 GRIDHQVKIRGFRIELGEIEARLLQ--HPSVREAV-VLARDGAGG-KQLVAYV----------VPADPQGD-------WR 3549
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5016 DRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREIGASFTAQQLAemrtssqgpkrqPSTEAERTMQQLWTRV 5095
Cdd:PRK12467  3550 ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA------------PRSEVEQQLAAIWADV 3617
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 5096 LGIElnGIGLDDSFFRLGGDSIAAMKLVGEARR-TGLQLSVADVFRHPRLVDLA-YVQNSECSSA 5158
Cdd:PRK12467  3618 LGVE--QVGVTDNFFELGGDSLLALQVLSRIRQsLGLKLSLRDLMSAPTIAELAgYSPLGDVPVN 3680
PRK12316 PRK12316
peptide synthase; Provisional
5176-6231 1.47e-148

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 526.45  E-value: 1.47e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5176 AQVSQDAAAMCSVDASSVEDMYPCSPLQEGLM--SLTAKRAGDYIMQsvleLRVDV---DEDAFRAAWEHVVQLTAALRT 5250
Cdd:PRK12316  4082 AGLDQARLDALPLPLGEIEDIYPLSPMQQGMLfhSLYEQEAGDYINQ----MRVDVqglDVERFRAAWQAALDRHDVLRS 4157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5251 RIVQHSELGLLQVVVEEKIQ-------WTESKRLEEYLREDKAVSMGLGDRLARYALIK---EPYDGGKRWFVWTIHHAL 5320
Cdd:PRK12316  4158 GFVWQGELGRPLQVVHKQVSlpfaeldWRGRADLQAALDALAAAERERGFDLQRAPLLRlvlVRTAEGRHHLIYTNHHIL 4237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5321 YDGWSLPRILQAVKQIYSGAVPERQPS-FNAFIQYLGQQDLEAATLYWQTALADCKAalfPT-LPPTVTQP-------VA 5391
Cdd:PRK12316  4238 MDGWSNSQLLGEVLERYSGRPPAQPGGrYRDYIAWLQRQDAAASEAFWREQLAALDE---PTrLAQAIARAdlrsangYG 4314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5392 DTTVEYQcppPSQSA--------TDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGVEAMVGPTIATVPLRV 5463
Cdd:PRK12316  4315 EHVRELD---ATATArlrefartQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIA 4391
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5464 CLQKDQTVSTLLECLQQQSTDMIAHEQTGL---QRIAKMSPGARhacgFQTLLVVQ--PTDDVLGSDDMLGEWRSYSEMQ 5538
Cdd:PRK12316  4392 TPRAQQSVVEWLQQVQRQNLALREHEHTPLyeiQRWAGQGGEAL----FDSLLVFEnyPVSEALQQGAPGGLRFGEVTNH 4467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5539 DFTTYALMVQCTLAkDRVEVTASFDARVIEQWVVEKMLRQFGFVMQQLAEaGAEKTVSDIETTTLEDRQQLWA-WNQNVP 5617
Cdd:PRK12316  4468 EQTNYPLTLAVGLG-ETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAE-DPQRRLGELQLLEKAEQQRIVAlWNRTDA 4545
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5618 --PAiERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKA 5695
Cdd:PRK12316  4546 gyPA-TRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKA 4624
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5696 GGAFVPLDPDHPASRHEDTFRHTGAQVVVTSAQHSARwigtnhqvVTVSAGslgqLSTLV-------------NPVgLPA 5762
Cdd:PRK12316  4625 GGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQR--------LPIPDG----LASLAldrdedwegfpahDPA-VRL 4691
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5763 IPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDR 5842
Cdd:PRK12316  4692 HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW 4771
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5843 RND-LVKAISTMDVSCALLTPSVARLL-----EPSSVPTLQMLVLQGEQVSFADWNRWPAS---VQTINGYGPTECSICC 5913
Cdd:PRK12316  4772 DPErLYAEIHEHRVTVLVFPPVYLQQLaehaeRDGEPPSLRVYCFGGEAVAQASYDLAWRAlkpVYLFNGYGPTETTVTV 4851
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5914 NTYSGKQGFKSGI----IGTSVASVS-WVVDpeNHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegy 5988
Cdd:PRK12316  4852 LLWKARDGDACGAaympIGTPLGNRSgYVLD--GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF------ 4923
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5989 pGHPGrqGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVRE--CLPEARQLAVEVilPSGQKdhamLA 6066
Cdd:PRK12316  4924 -GAPG--GRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREhpAVREAVVIAQEG--AVGKQ----LV 4994
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6067 AFVqleegtqnaLLDKEASGEDSMAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQ 6146
Cdd:PRK12316  4995 GYV---------VPQDPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQA 5065
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6147 IAnmqtssqdpkrQPSTEAEQTMQKLWAQVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEAR-RIGLQLSVADIFRYARL 6225
Cdd:PRK12316  5066 YV-----------APRSELEQQVAAIWAEVLQLE--RVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTL 5132

                   ....*.
gi 1820002560 6226 VDLASL 6231
Cdd:PRK12316  5133 AAFVEL 5138
PRK12467 PRK12467
peptide synthase; Provisional
368-1469 1.75e-147

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 522.41  E-value: 1.75e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  368 FRHPTLAALASLETNQYNITIEE---------TP---PLsllgenADVAQVRDEAAAmcsVDGSAIEDMYLCSPLQEGLM 435
Cdd:PRK12467  2587 FDEATIQRLADAYAEELRALIEHccsndqrgvTPsdfPL------AGLSQEQLDRLP---VAVGDIEDIYPLSPMQQGML 2657
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  436 --SLTTKRAGDYIMQdvleLRADV---DEHAFRAAWEYVVQSIAVLRTRIVQHSELGL-LQVVVEE------KMQWTESE 503
Cdd:PRK12467  2658 fhTLYEGGAGDYINQ----MRVDVeglDVERFRTAWQAVIDRHEILRSGFLWDGELEEpLQVVYKQarlpfsRLDWRDRA 2733
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  504 SLEEYLNEDKAASMGLGDRLA-----RYALIKesCGGKRW-FVWTIHHALYDGWSLPLVLDAVKQVYSGAALERQPS-FN 576
Cdd:PRK12467  2734 DLEQALDALAAADRQQGFDLLsapllRLTLVR--TGEDRHhLIYTNHHILMDGWSGSQLLGEVLQRYFGQPPPAREGrYR 2811
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  577 TFIQYVSQQDVKAAAAYWQTALADCE--AVLFPPLPSTVTQPVADTTVKYQcpPSPEVTSSN---------ITTSTLIRA 645
Cdd:PRK12467  2812 DYIAWLQAQDAEASEAFWKEQLAALEepTRLARALYPAPAEAVAGHGAHYL--HLDATQTRQliefarrhrVTLNTLVQG 2889
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  646 AWAIIASRYTSSEDIVFGTTVTGRNAPITGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTGLQRIM 725
Cdd:PRK12467  2890 AWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQ 2969
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  726 KMGPGPQHACgFQTLLVV--HPTDDVLS----SDDTLGEWHSRSDSelQYFTTYALTIQCTLAVEGVQITASFDARVVEh 799
Cdd:PRK12467  2970 RWAGQGGEAL-FDSILVFenYPISEALKqgapSGLRFGAVSSREQT--NYPLTLAVGLGDTLELEFSYDRQHFDAAAIE- 3045
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  800 wvveKMLGQFSFVMQQLAEAGvEKKVADIETTTLEDRQQL---WVWNADMPPAvDRCIHDLFAEQARARPDASAVCAWDG 876
Cdd:PRK12467  3046 ----RLAESFDRLLQAMLNNP-AARLGELPTLAAHERRQVlhaWNATAAAYPS-ERLVHQLIEAQVARTPEAPALVFGDQ 3119
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTs 956
Cdd:PRK12467  3120 QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT- 3198
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  957 SQHAM--LFASSERHQVTVSKVSTSQLPTvvNFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYT 1034
Cdd:PRK12467  3199 QAHLLeqLPAPAGDTALTLDRLDLNGYSE--NNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELD 3276
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1035 DHARVLQFASYTFDACIAEIITTLLYGGCICV-PSESDRRNNLAKAISTMDVNCALLTPSVARLL----EPSAVPSLKRL 1109
Cdd:PRK12467  3277 ANDRVLLFMSFSFDGAQERFLWTLICGGCLVVrDNDLWDPEELWQAIHAHRISIACFPPAYLQQFaedaGGADCASLDIY 3356
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1110 VLQGEQV---SFADWNRWPGSVQTINGYGPTECSV------CcnTYSGKQGFKSGIIGTSVASLSWVVDAGNHNRlAPLG 1180
Cdd:PRK12467  3357 VFGGEAVppaAFEQVKRKLKPRGLTNGYGPTEAVVtvtlwkC--GGDAVCEAPYAPIGRPVAGRSIYVLDGQLNP-VPVG 3433
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1181 SIGELLVEGPILARGYLNDIDKTEAAFIDDPawllegyegHAGRRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRV 1260
Cdd:PRK12467  3434 VAGELYIGGVGLARGYHQRPSLTAERFVADP---------FSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRI 3504
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1261 ELGEIEHHVREcLPEARQLAVEVILPSGQKEhalLAAFIQLDkgnhnalfeekASGEDSMAQvvfltgVEEELAKRLPEH 1340
Cdd:PRK12467  3505 ELGEIEARLLQ-HPSVREAVVLARDGAGGKQ---LVAYVVPA-----------DPQGDWRET------LRDHLAASLPDY 3563
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1341 MVPTILFTVKAMPITTSGKIDRKRLQDIGASFTVQQLAemrtssqgpkrqPSTEVEQTMQQLWAQVLSIEpnSIGLDDSF 1420
Cdd:PRK12467  3564 MVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA------------PRSEVEQQLAAIWADVLGVE--QVGVTDNF 3629
                         1130      1140      1150      1160      1170
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 1421 FRLGGDSIVAMKLVGEARR-TGLQLSVADIFRHPRLVDLA-RVQNSQFSSA 1469
Cdd:PRK12467  3630 FELGGDSLLALQVLSRIRQsLGLKLSLRDLMSAPTIAELAgYSPLGDVPVN 3680
PRK12467 PRK12467
peptide synthase; Provisional
7158-8214 1.20e-146

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 519.72  E-value: 1.20e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7158 DVNPVQLSQDAAAMCSVAASIVKDIYPCSPLQEGLI--SLTAKRAGDYIMQsvleLRADV---DEDVFCAAWEHVVQSTA 7232
Cdd:PRK12467  2622 DFPLAGLSQEQLDRLPVAVGDIEDIYPLSPMQQGMLfhTLYEGGAGDYINQ----MRVDVeglDVERFRTAWQAVIDRHE 2697
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7233 ALRTRIVQHSELGL-LQVVVEE------KIQWTE----SEALEEYLKEDKAVSMGLGD-PLAHYALVKEawGGKRW-FVW 7299
Cdd:PRK12467  2698 ILRSGFLWDGELEEpLQVVYKQarlpfsRLDWRDradlEQALDALAAADRQQGFDLLSaPLLRLTLVRT--GEDRHhLIY 2775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7300 TIHHALYDGGSLPLILHAVKQVYSGAVLERQPS-FNAFIQYLGQQDLEATAAYWQTALSDCE--AVLFPPLPSTVTQPVA 7376
Cdd:PRK12467  2776 TNHHILMDGWSGSQLLGEVLQRYFGQPPPAREGrYRDYIAWLQAQDAEASEAFWKEQLAALEepTRLARALYPAPAEAVA 2855
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7377 ---------DTTVEYQCPPLSKAtLDTTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPIAGVEAMVGPTIATVPVR 7447
Cdd:PRK12467  2856 ghgahylhlDATQTRQLIEFARR-HRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVI 2934
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7448 LRVQRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIAKLGSGPRHACgFQTLLVVQ--PVDDVL---GSDDM-LGEWRSysk 7521
Cdd:PRK12467  2935 ASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEAL-FDSILVFEnyPISEALkqgAPSGLrFGAVSS--- 3010
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7522 mQDFTTYALMVQFTLAaEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLAEASEdSKVADIDTTTPEDRQQLW-AWNAD 7600
Cdd:PRK12467  3011 -REQTNYPLTLAVGLG-DTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPA-ARLGELPTLAAHERRQVLhAWNAT 3087
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7601 -VPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLK 7679
Cdd:PRK12467  3088 aAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLK 3167
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7680 AGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARW-TSSSCHVVTVSK-ALSSQLPAVVDstnTSVRPENAAYIIF 7757
Cdd:PRK12467  3168 AGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLpAPAGDTALTLDRlDLNGYSENNPS---TRVMGENLAYVIY 3244
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7758 TSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVpSDSDRRN--SLAKAI 7835
Cdd:PRK12467  3245 TSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV-RDNDLWDpeELWQAI 3323
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7836 STMDVNWAFLTPSVARLL----DPGLIPSLKILAIGGE---QSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFE 7908
Cdd:PRK12467  3324 HAHRISIACFPPAYLQQFaedaGGADCASLDIYVFGGEavpPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAV 3403
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7909 PST----IGTSVASVSWVVDPENHNRlAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPawllegypgHPGRQGRLY 7984
Cdd:PRK12467  3404 CEApyapIGRPVAGRSIYVLDGQLNP-VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP---------FSGSGGRLY 3473
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7985 KTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVevilpsgqknhamLAVFVQLGKGThIAH 8064
Cdd:PRK12467  3474 RTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQ-HPSVREAVV-------------LARDGAGGKQL-VAY 3538
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8065 LEEKAGGEDSMAQVvfltgtEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGASFTAQQLAetqtssqgpkr 8144
Cdd:PRK12467  3539 VVPADPQGDWRETL------RDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA----------- 3601
                         1050      1060      1070      1080      1090      1100      1110
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 8145 qPLTEAEQTMQQLWARVLGIDAdiIGLDDSFFRLGGDSIAAMKLVGEARR-TGLQLSVADIFRHPRLIDLA 8214
Cdd:PRK12467  3602 -PRSEVEQQLAAIWADVLGVEQ--VGVTDNFFELGGDSLLALQVLSRIRQsLGLKLSLRDLMSAPTIAELA 3669
PRK12316 PRK12316
peptide synthase; Provisional
4107-5160 2.56e-146

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 519.13  E-value: 2.56e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4107 VDASAITDVYPCSPLQEGLM--SLTAKRAGDYIMQTvlelRADV---NEDAFRAAWELVVQLTAVLRTRIVQHSELGLLQ 4181
Cdd:PRK12316  4094 LPLGEIEDIYPLSPMQQGMLfhSLYEQEAGDYINQM----RVDVqglDVERFRAAWQAALDRHDVLRSGFVWQGELGRPL 4169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4182 VVVEERIQWTESEsLEEYPREDKAVSM---GVGDRLARYALIKEPY--------DGGKRWFVWTMHHALYDGWSLPRILH 4250
Cdd:PRK12316  4170 QVVHKQVSLPFAE-LDWRGRADLQAALdalAAAERERGFDLQRAPLlrlvlvrtAEGRHHLIYTNHHILMDGWSNSQLLG 4248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4251 AVKQAYSGVVLERQPS-FNAFIQYLSQQDPEAAAAYWQTALVDCKAalfPT-LPPTVTQP-------VADTTVEYQcppP 4321
Cdd:PRK12316  4249 EVLERYSGRPPAQPGGrYRDYIAWLQRQDAAASEAFWREQLAALDE---PTrLAQAIARAdlrsangYGEHVRELD---A 4322
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4322 SQSA--------TDITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQTVFAF 4393
Cdd:PRK12316  4323 TATArlrefartQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEW 4402
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4394 LQGVQQQATDMIAHEQTGL---QRIAKMSPGARhacgFQTLLVVQ--PTDDVLGSDDMLGEWRSYSEMQDFTTYALMVQc 4468
Cdd:PRK12316  4403 LQQVQRQNLALREHEHTPLyeiQRWAGQGGEAL----FDSLLVFEnyPVSEALQQGAPGGLRFGEVTNHEQTNYPLTLA- 4477
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4469 VLVKDRVGVTASFDARVIEQWVVEKMLRQFGFVMQQLAdAGEEKKVAGIETTTTGDRQQLWA-WNQ-DVPPAIERCVHDQ 4546
Cdd:PRK12316  4478 VGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMA-EDPQRRLGELQLLEKAEQQRIVAlWNRtDAGYPATRCVHQL 4556
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHP 4626
Cdd:PRK12316  4557 VAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYP 4636
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4627 ASRHEHIFRQTGAQVVLA-SAQYATLWTSLG-RSVVIVSEASTSQLPvvtkTADPSVN--PGNAAYAIFTSGSTGIPKGV 4702
Cdd:PRK12316  4637 RERLAYMMEDSGAALLLTqSHLLQRLPIPDGlASLALDRDEDWEGFP----AHDPAVRlhPDNLAYVIYTSGSTGRPKGV 4712
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4703 VLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDS-DRRNNLAKAINAMDVNWALLTP 4781
Cdd:PRK12316  4713 AVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSlWDPERLYAEIHEHRVTVLVFPP 4792
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4782 SVARML--DPCV---VQSLKILVLGGEQVNSADWDRWPKSIQTI---NAYGPTECSICCTTYSGKQGFKSGT----IGTS 4849
Cdd:PRK12316  4793 VYLQQLaeHAERdgePPSLRVYCFGGEAVAQASYDLAWRALKPVylfNGYGPTETTVTVLLWKARDGDACGAaympIGTP 4872
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4850 IVSVS-WVVDpeNHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawllegYGGHSgrqGRLYKTGDLVRYDA 4928
Cdd:PRK12316  4873 LGNRSgYVLD--GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDP------FGAPG---GRLYRTGDLARYRA 4941
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4929 DGNLVYLGRKDSQVKLRGQRVELGEVEHHVREclTEAKQLAVeVIVPEGEGGyAMLAAFVqlgddtyntLVKEKAGGDSL 5008
Cdd:PRK12316  4942 DGVIDYLGRVDHQVKIRGFRIELGEIEARLRE--HPAVREAV-VIAQEGAVG-KQLVGYV---------VPQDPALADAD 5008
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5009 TVQVVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREIGASFTAQQLAemrtssqgpkrQPSTEAERTM 5088
Cdd:PRK12316  5009 EAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYV-----------APRSELEQQV 5077
                         1050      1060      1070      1080      1090      1100      1110
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 5089 QQLWTRVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEAR-RTGLQLSVADVFRHPRLVdlAYVQNSECSSAAE 5160
Cdd:PRK12316  5078 AAIWAEVLQLE--RVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTLA--AFVELAAAAGSGD 5146
PRK12316 PRK12316
peptide synthase; Provisional
7158-8220 4.27e-144

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 511.81  E-value: 4.27e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7158 DVNPVQLSQDAAAMCSVAASIVKDIYPCSPLQEGLI--SLTAKRAGDYIMQsvleLRADV---DEDVFCAAWEHVVQSTA 7232
Cdd:PRK12316  4078 DFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLfhSLYEQEAGDYINQ----MRVDVqglDVERFRAAWQAALDRHD 4153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7233 ALRTRIVQHSELGLLQVVVEEKIQ-------WTESEALEEYLKEDKAVSMGLG-----DPLAHYALVKEAWGGKRwFVWT 7300
Cdd:PRK12316  4154 VLRSGFVWQGELGRPLQVVHKQVSlpfaeldWRGRADLQAALDALAAAERERGfdlqrAPLLRLVLVRTAEGRHH-LIYT 4232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7301 IHHALYDGGSLPLILHAVKQVYSGAVLERQPS-FNAFIQYLGQQDLEATAAYWQTALSDCEAvlfpplPSTVTQPVA--- 7376
Cdd:PRK12316  4233 NHHILMDGWSNSQLLGEVLERYSGRPPAQPGGrYRDYIAWLQRQDAAASEAFWREQLAALDE------PTRLAQAIArad 4306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7377 --------DTTVEYQcpPLSKATLD-------TTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPIAGVEAMVGPTI 7441
Cdd:PRK12316  4307 lrsangygEHVRELD--ATATARLRefartqrVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFI 4384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7442 ATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTGL---QHIAKLGSGPRhacgFQTLLVVQ--PVDDVLGSDDMLGEW 7516
Cdd:PRK12316  4385 NTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLyeiQRWAGQGGEAL----FDSLLVFEnyPVSEALQQGAPGGLR 4460
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7517 RSYSKMQDFTTYalmvQFTLA---AEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLAEASEdSKVADIDTTTPEDRQQ 7593
Cdd:PRK12316  4461 FGEVTNHEQTNY----PLTLAvglGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQ-RRLGELQLLEKAEQQR 4535
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7594 LWA-WNA-DVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTV 7671
Cdd:PRK12316  4536 IVAlWNRtDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMM 4615
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7672 VAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARwtssschvVTVSKALSSqlpAVVD---------S 7742
Cdd:PRK12316  4616 VGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQR--------LPIPDGLAS---LALDrdedwegfpA 4684
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7743 TNTSVR--PENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCIC 7820
Cdd:PRK12316  4685 HDPAVRlhPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVV 4764
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7821 VPSDS-DRRNSLAKAISTMDVNWAFLTPSVARLL-----DPGLIPSLKILAIGGEQSSSADWNRWPGSVQKI---HVYGP 7891
Cdd:PRK12316  4765 IRDDSlWDPERLYAEIHEHRVTVLVFPPVYLQQLaehaeRDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVylfNGYGP 4844
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7892 TECCIFCTGYTTKQGFEPST----IGTSVASVS-WVVDpeNHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDP 7966
Cdd:PRK12316  4845 TETTVTVLLWKARDGDACGAaympIGTPLGNRSgYVLD--GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDP 4922
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7967 AwllegypGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVRE--CLPEARQLAVEVilPSGQ 8044
Cdd:PRK12316  4923 F-------GAPG--GRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREhpAVREAVVIAQEG--AVGK 4991
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8045 KnhamLAVFVqLGKGTHIAhleekaggEDSMAQVVFLTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIG 8124
Cdd:PRK12316  4992 Q----LVGYV-VPQDPALA--------DADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPD 5058
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8125 ASFTAQQLAetqtssqgpkrQPLTEAEQTMQQLWARVLGIDAdiIGLDDSFFRLGGDSIAAMKLVGEAR-RTGLQLSVAD 8203
Cdd:PRK12316  5059 ASLLQQAYV-----------APRSELEQQVAAIWAEVLQLER--VGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRE 5125
                         1130
                   ....*....|....*..
gi 1820002560 8204 IFRHPRLIDLASLKSTF 8220
Cdd:PRK12316  5126 LFQTPTLAAFVELAAAA 5142
PRK12316 PRK12316
peptide synthase; Provisional
401-1481 1.23e-142

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 506.80  E-value: 1.23e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  401 ADVAQVRDEAAAMCSvdgSAIEDMYLCSPLQEGLM--SLTTKRAGDYIMQdvleLRADV---DEHAFRAAWEYVVQSIAV 475
Cdd:PRK12316  4082 AGLDQARLDALPLPL---GEIEDIYPLSPMQQGMLfhSLYEQEAGDYINQ----MRVDVqglDVERFRAAWQAALDRHDV 4154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  476 LRTRIVQHSELGLLQVVVEEKMQ-------WTESESLEEYLNEDKAASMGLGDRLARYALIK----ESCGGKRWFVWTIH 544
Cdd:PRK12316  4155 LRSGFVWQGELGRPLQVVHKQVSlpfaeldWRGRADLQAALDALAAAERERGFDLQRAPLLRlvlvRTAEGRHHLIYTNH 4234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  545 HALYDGWSLPLVLDAVKQVYSGAALERQPS-FNTFIQYVSQQDVKAAAAYWQTALADCEAvlfpplPSTVTQPVAD---T 620
Cdd:PRK12316  4235 HILMDGWSNSQLLGEVLERYSGRPPAQPGGrYRDYIAWLQRQDAAASEAFWREQLAALDE------PTRLAQAIARadlR 4308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  621 TVKYQCPPSPEVTSS------------NITTSTLIRAAWAIIASRYTSSEDIVFGTTVTGRNAPITGVEAMVGPTIATVP 688
Cdd:PRK12316  4309 SANGYGEHVRELDATatarlrefartqRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLP 4388
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  689 LRVRPRKGQTVSAFLENLQQQATEMIAYEQTGL---QRIMKMGPGPQhacgFQTLLV--VHPTDDVLSSDDTLGEWHSRS 763
Cdd:PRK12316  4389 VIATPRAQQSVVEWLQQVQRQNLALREHEHTPLyeiQRWAGQGGEAL----FDSLLVfeNYPVSEALQQGAPGGLRFGEV 4464
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  764 DSELQyfTTYALTIQCTLAvEGVQITASFDARVVEHWVVEKMLGQFSFVMQQLAEAGvEKKVADIETTTLEDRQQ-LWVW 842
Cdd:PRK12316  4465 TNHEQ--TNYPLTLAVGLG-ETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDP-QRRLGELQLLEKAEQQRiVALW 4540
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  843 NA-DMPPAVDRCIHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLA 921
Cdd:PRK12316  4541 NRtDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLA 4620
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  922 VLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSqHAM--LFASSERHQVTVSKVSTSQLPTVVNFAkSPVDPGNTAY 999
Cdd:PRK12316  4621 VLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS-HLLqrLPIPDGLASLALDRDEDWEGFPAHDPA-VRLHPDNLAY 4698
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1000 IIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICV--PSESDRRNNLA 1077
Cdd:PRK12316  4699 VIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIrdDSLWDPERLYA 4778
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1078 KaISTMDVNCALLTPSVARLL-----EPSAVPSLKRLVLQGEQVSFADWNRWPGS---VQTINGYGPTECSVCCNTYSGK 1149
Cdd:PRK12316  4779 E-IHEHRVTVLVFPPVYLQQLaehaeRDGEPPSLRVYCFGGEAVAQASYDLAWRAlkpVYLFNGYGPTETTVTVLLWKAR 4857
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1150 QGFKSGI----IGTSVASLS-WVVDagNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAwlleGYEGhagr 1224
Cdd:PRK12316  4858 DGDACGAaympIGTPLGNRSgYVLD--GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF----GAPG---- 4927
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1225 rGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVRE--CLPEARQLAVEVilPSGQKehalLAAFIQLD 1302
Cdd:PRK12316  4928 -GRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREhpAVREAVVIAQEG--AVGKQ----LVGYVVPQ 5000
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1303 kgnhnalfeEKASGEDSMAQVVFLTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDIGASFTVQQLAemrt 1382
Cdd:PRK12316  5001 ---------DPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYV---- 5067
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1383 ssqgpkrQPSTEVEQTMQQLWAQVLSIEpnSIGLDDSFFRLGGDSIVAMKLVGEAR-RTGLQLSVADIFRHPRLVDLARV 1461
Cdd:PRK12316  5068 -------APRSELEQQVAAIWAEVLQLE--RVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTLAAFVEL 5138
                         1130      1140
                   ....*....|....*....|.
gi 1820002560 1462 QNSQFSSAAEEVPAF-SLLGE 1481
Cdd:PRK12316  5139 AAAAGSGDDEKFDDLeELLSE 5159
PRK12316 PRK12316
peptide synthase; Provisional
7164-8621 1.41e-141

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 503.34  E-value: 1.41e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7164 LSQDAAAMCSVAASIVKDIYPCSPLQEGLI--SLTAKRAGDYIMQsvleLRADV---DEDVFCAAWEHVVQSTAALRTRI 7238
Cdd:PRK12316  1538 LSQAQLDALPLPAGEIADIYPLSPMQQGMLfhSLYEQEAGDYINQ----LRVDVqglDPDRFRAAWQATVDRHEILRSGF 1613
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7239 VQHSELGLLQVVVEEKIQ-------WTESE----ALEEYLKEDKAVSMGLG-DPLAHYALVKEawGGKRW-FVWTIHHAL 7305
Cdd:PRK12316  1614 LWQDGLEQPLQVIHKQVElpfaeldWRGREdlgqALDALAQAERQKGFDLTrAPLLRLVLVRT--GEGRHhLIYTNHHIL 1691
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7306 YDGGSLPLILHAVKQVYSG-AVLERQPSFNAFIQYLGQQDLEATAAYWQTALSDCEAvlfpplPSTVTQPVA-----DTT 7379
Cdd:PRK12316  1692 MDGWSNAQLLGEVLQRYAGqPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEE------PTRLAQAARtedgqVGY 1765
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7380 VEYQ--CPPLSKATLDT-------TTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPIAGVEAMVGPTIATVPVRLRV 7450
Cdd:PRK12316  1766 GDHQqlLDPAQTRALAEfaraqkvTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAP 1845
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7451 QRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIAKLgSGPRHACGFQTLLVVQ--PVDDVL--GSDDMLGEWRSYSKMQdfT 7526
Cdd:PRK12316  1846 RPDQSVADWLQEVQALNLALREHEHTPLYDIQRW-AGQGGEALFDSLLVFEnyPVAEALkqGAPAGLVFGRVSNHEQ--T 1922
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7527 TYALMVQFTLAaEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLAEASEDSkVADIDTTTPEDRQQLWA-WNADVPPA- 7604
Cdd:PRK12316  1923 NYPLTLAVTLG-ETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAA-LGELALLDAGERQRILAdWDRTPEAYp 2000
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7605 IERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAF 7684
Cdd:PRK12316  2001 RGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY 2080
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7685 VPLDPDHPASRHEEIFEQTGAQVVVASAQYSARW---TSSSCHVVTVSKALS---SQLPAVvdstntSVRPENAAYIIFT 7758
Cdd:PRK12316  2081 VPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLplpAGVARLPLDRDAEWAdypDTAPAV------QLAGENLAYVIYT 2154
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7759 SGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRR-NSLAKAIST 7837
Cdd:PRK12316  2155 SGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDpEQLYDEMER 2234
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7838 MDVNWAFLTPSVARLLDP-----GLIPSLKILAIGGEQSSSADWNRWPGSVQK---IHVYGPTECCIFCTGYTTKQ---- 7905
Cdd:PRK12316  2235 HGVTILDFPPVYLQQLAEhaerdGRPPAVRVYCFGGEAVPAASLRLAWEALRPvylFNGYGPTEAVVTPLLWKCRPqdpc 2314
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7906 GFEPSTIGTSVASVS-WVVDPENHnrLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLY 7984
Cdd:PRK12316  2315 GAAYVPIGRALGNRRaYILDADLN--LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPF-------SASG--ERLY 2383
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7985 KTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVR--ECLPEARQLAVEVilPSGQknhamlavfvQLgkgthI 8062
Cdd:PRK12316  2384 RTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQahPAVREAVVVAQDG--ASGK----------QL-----V 2446
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8063 AHLEEKAGGEDsmaqvvFLTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGASfTAQQLAETqtssqgp 8142
Cdd:PRK12316  2447 AYVVPDDAAED------LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVS-QLRQAYVA------- 2512
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8143 krqPLTEAEQTMQQLWARVLGIDAdiIGLDDSFFRLGGDSIAAMKLVGEARRT-GLQLSVADIFRHPRLIDLASlkstfc 8221
Cdd:PRK12316  2513 ---PQEGLEQRLAAIWQAVLKVEQ--VGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAA------ 2581
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8222 nsvveevpafsllspVMKDAMFSVTEPFGPSLRIDDItdvvPASYIQQFYIATGVRAP-REAFNYP-FIDLSDAVDIQVL 8299
Cdd:PRK12316  2582 ---------------SLESGQTSRAPVLQKVTRVQPL----PLSHAQQRQWFLWQLEPeSAAYHLPsALHLRGVLDQAAL 2642
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8300 QASCSALLEHFPILRTHFVYFQGKLYQVIPRHQDLPFSIFEVNGALAEESQAIHIRDLDQTSPL--GLPTSFTLVRNASG 8377
Cdd:PRK12316  2643 EQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLarGPLLRVRLLALDGQ 2722
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8378 MNRLIIRLSHAQYDGVCMPVIWASLASIYQQ----EPLLSTTGFHSYLAYVHNQRS--------ASINYWSRLLKGSHIT 8445
Cdd:PRK12316  2723 EHVLVITQHHIVSDGWSMQVMVDELVQAYAGarrgEQPTLPPLPLQYADYAAWQRAwmdsgegaRQLDYWRERLGGEQPV 2802
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8446 NITSKLRPKLGKDT-------TIRSVKVERVIRTPQLPTGLTMASLVSSAWAVVLSHISGEEDVVYGLVVAGRN------ 8512
Cdd:PRK12316  2803 LELPLDRPRPALQShrgarldVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNraeter 2882
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8513 ------SDLPSITEV-----------SVQDQYISLGESDSIGLDDIVQHCTDWPAKSE---FDSIIQHQNIEEQPEIQFA 8572
Cdd:PRK12316  2883 ligffvNTQVLRAQVdaqlafrdllgQVKEQALGAQAHQDLPFEQLVEALQPERSLSHsplFQVMYNHQSGERAAAQLPG 2962
                         1530      1540      1550      1560
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 8573 GETTKLQWFKNSFAVSRQLFVFSHPrgNSLTITITGNTGILTDQCAEKL 8621
Cdd:PRK12316  2963 LHIESFAWDGAATQFDLALDTWESA--EGLGASLTYATDLFDARTVERL 3009
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
3475-3974 2.52e-139

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 445.05  E-value: 2.52e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 3634
Cdd:cd05930     81 EDSGAKLVL-------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3635 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL----D 3708
Cdd:cd05930    124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDpeALADLLAEEGITVLHLTPSLLRLLlqelE 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3709 PGLIPSLKILAIGGEQSSSADWNRWPGSVQK---IHVYGPTECCIFCTGYTTKQGF---EPSTIGTSVASVS-WVVDPen 3781
Cdd:cd05930    204 LAALPSLRLVLVGGEALPPDLVRRWRELLPGarlVNLYGPTEATVDATYYRVPPDDeedGRVPIGRPIPNTRvYVLDE-- 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3782 HNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllegyPGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDSQ 3861
Cdd:cd05930    282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPN--------PFGPG--ERMYRTGDLVRWLPDGNLEFLGRIDDQ 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3862 VKVRGQRVELGEVEHHVREcLPEARQlAVeVILPSGQKDHAMLAAFVQLEEGtqnalldkeaggedsmaQVVFLASVEEE 3941
Cdd:cd05930    352 VKIRGYRIELGEIEAALLA-HPGVRE-AA-VVAREDGDGEKRLVAYVVPDEG-----------------GELDEEELRAH 411
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 3942 LAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd05930    412 LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
1943-2442 6.81e-137

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 438.11  E-value: 6.81e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1943 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIF 2022
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2023 RQTGAQVVVTSaqhsarwigtnhqvvtvsagsleqfstlvnpvdlpakPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCL 2102
Cdd:cd05930     81 EDSGAKLVLTD-------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2103 GHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSSVARLL----D 2176
Cdd:cd05930    124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDpeALADLLAEEGITVLHLTPSLLRLLlqelE 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2177 PCLVPSLKVLVLGGEQVNSTDWGKWPSS---VQTINGYGPTECCVFCTGYTGIQGFQSGN---IGTSIASVS-WVVDPen 2249
Cdd:cd05930    204 LAALPSLRLVLVGGEALPPDLVRRWRELlpgARLVNLYGPTEATVDATYYRVPPDDEEDGrvpIGRPIPNTRvYVLDE-- 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2250 HGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPawllegypghEGRQGRLYKTGDLVRYSSDGNLVCLGRKDSQ 2329
Cdd:cd05930    282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNP----------FGPGERMYRTGDLVRWLPDGNLEFLGRIDDQ 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2330 VKVRGQRVELGEVEHHMRKcLPEANQlAVeVVPPSGERDHAMLAAFIRLDDETRNSPliikyaednstaqivflTGIEEE 2409
Cdd:cd05930    352 VKIRGYRIELGEIEAALLA-HPGVRE-AA-VVAREDGDGEKRLVAYVVPDEGGELDE-----------------EELRAH 411
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 2410 LSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd05930    412 LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
866-1365 2.25e-136

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 436.57  E-value: 2.25e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  866 PDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIF 945
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  946 KQIGAQVVLTssqhamlfasserhqvtvskvstsqlptvvnfakspvDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCL 1025
Cdd:cd05930     81 EDSGAKLVLT-------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1026 GHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRN--NLAKAISTMDVNCALLTPSVARLL----E 1099
Cdd:cd05930    124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDpeALADLLAEEGITVLHLTPSLLRLLlqelE 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1100 PSAVPSLKRLVLQGEQVSFADWNRWPGS---VQTINGYGPTECSVCCNTYSGKQGFKSGI---IGTSVASLS-WVVDAgn 1172
Cdd:cd05930    204 LAALPSLRLVLVGGEALPPDLVRRWRELlpgARLVNLYGPTEATVDATYYRVPPDDEEDGrvpIGRPIPNTRvYVLDE-- 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1173 HNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawllegyeghAGRRGRLYKTGDLVRCDADGNLVCLGRKDSQ 1252
Cdd:cd05930    282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNP----------FGPGERMYRTGDLVRWLPDGNLEFLGRIDDQ 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1253 VKVRGQRVELGEIEHHVREcLPEARQlAVeVILPSGQKEHALLAAFIQLDKGnhnalfeekasgedsmaQVVFLTGVEEE 1332
Cdd:cd05930    352 VKIRGYRIELGEIEAALLA-HPGVRE-AA-VVAREDGDGEKRLVAYVVPDEG-----------------GELDEEELRAH 411
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 1333 LAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd05930    412 LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
4555-5054 2.34e-136

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 436.57  E-value: 2.34e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4555 PDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIF 4634
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4635 RQTGAQVVLasaqyatlwtslgrsvvivseastsqlpvvtktadpsVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCL 4714
Cdd:cd05930     81 EDSGAKLVL-------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4715 GHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRN--NLAKAINAMDVNWALLTPSVARML----D 4788
Cdd:cd05930    124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDpeALADLLAEEGITVLHLTPSLLRLLlqelE 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4789 PCVVQSLKILVLGGEQVNSADWDRWPKS---IQTINAYGPTECSICCTTYSGKQGFKSG---TIGTSI--VSVsWVVDPe 4860
Cdd:cd05930    204 LAALPSLRLVLVGGEALPPDLVRRWRELlpgARLVNLYGPTEATVDATYYRVPPDDEEDgrvPIGRPIpnTRV-YVLDE- 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4861 nHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawllegygghSGRQGRLYKTGDLVRYDADGNLVYLGRKDS 4940
Cdd:cd05930    282 -NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNP----------FGPGERMYRTGDLVRWLPDGNLEFLGRIDD 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4941 QVKLRGQRVELGEVEHHVREC--LTEAKqlaveVIVPEGEGGYAMLAAFVQLGDDtyntlvkekaggdsltvQVVFLDRV 5018
Cdd:cd05930    351 QVKIRGYRIELGEIEAALLAHpgVREAA-----VVAREDGDGEKRLVAYVVPDEG-----------------GELDEEEL 408
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1820002560 5019 EEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd05930    409 RAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
4568-4961 4.38e-136

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 434.39  E-value: 4.38e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4568 TYGELDTLSSKLASHLVQL-GVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLASA 4646
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4647 QYATLWTSLGRSVVIVS---EASTSQLPVvTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGIT 4723
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDpleLAALDDAPA-PPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4724 DHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRR---NNLAKAINAMDVNWALLTPSVARMLDPCVVQ---SLKI 4797
Cdd:TIGR01733  160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERddaALLAALIAEHPVTVLNLTPSLLALLAAALPPalaSLRL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4798 LVLGGEQVNSADWDRW---PKSIQTINAYGPTECSICCTTYS----GKQGFKSGTIGTSIVSVS-WVVDPenHNRLAPLG 4869
Cdd:TIGR01733  240 VILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLvdpdDAPRESPVPIGRPLANTRlYVLDD--DLRPVPVG 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4870 SIGELLVEGPILARGYLNDMEKTEAAFIDDPAWllegygghSGRQGRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRV 4949
Cdd:TIGR01733  318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRI 389
                          410
                   ....*....|..
gi 1820002560 4950 ELGEVEHHVREC 4961
Cdd:TIGR01733  390 ELGEIEAALLRH 401
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
7621-8120 2.41e-135

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 433.49  E-value: 2.41e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7621 PGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 7700
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7701 EQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 7780
Cdd:cd05930     81 EDSGAKLVL-------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7781 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL----D 7854
Cdd:cd05930    124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDpeALADLLAEEGITVLHLTPSLLRLLlqelE 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7855 PGLIPSLKILAIGGEQSSSADWNRWPGSVQK---IHVYGPTECCIFCTGYTTKQGF---EPSTIGTSVASVS-WVVDPen 7927
Cdd:cd05930    204 LAALPSLRLVLVGGEALPPDLVRRWRELLPGarlVNLYGPTEATVDATYYRVPPDDeedGRVPIGRPIPNTRvYVLDE-- 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7928 HNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllegyPGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDSQ 8007
Cdd:cd05930    282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPN--------PFGPG--ERMYRTGDLVRWLPDGNLEFLGRIDDQ 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8008 VKVRGQRVELGEVEHHVREcLPEARQlAVeVILPSGQKNHAMLAVFVQLGKGTHIAHLEEKaggedsmaqvvfltgteEE 8087
Cdd:cd05930    352 VKIRGYRIELGEIEAALLA-HPGVRE-AA-VVAREDGDGEKRLVAYVVPDEGGELDEEELR-----------------AH 411
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 8088 LAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd05930    412 LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1956-2349 3.07e-135

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 431.69  E-value: 3.07e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1956 TYGELDALSSKLASHLVQL-GVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSA 2034
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2035 QHSAR--WIGTNHQVVTVSAGSLEQFSTLVNPVDLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTN 2112
Cdd:TIGR01733   81 ALASRlaGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2113 LLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD---NLAKAITDMQVNWGYLTSSVARLLDPCLVP---SLKVL 2186
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDdaaLLAALIAEHPVTVLNLTPSLLALLAAALPPalaSLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2187 VLGGEQVNSTDWGKW---PSSVQTINGYGPTECCVFCTGYT----GIQGFQSGNIGTSIASVS-WVVDPenHGRLAPLGS 2258
Cdd:TIGR01733  241 ILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLvdpdDAPRESPVPIGRPLANTRlYVLDD--DLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2259 IGELLVEGPILARGYLNDVDKTQAAFIDDPAWLlegypgheGRQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVE 2338
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAG--------GDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIE 390
                          410
                   ....*....|.
gi 1820002560 2339 LGEVEHHMRKC 2349
Cdd:TIGR01733  391 LGEIEAALLRH 401
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
3488-3890 4.03e-135

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 431.30  E-value: 4.03e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3488 TYGELDALSSKLASHLVQL-GVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASA 3566
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3567 QYSAR--WTSSSCHVVTVSKALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITN 3644
Cdd:TIGR01733   81 ALASRlaGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3645 LSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRR---NSLAKAISTMDVNWAFLTPSVARLLDPGLIP---SLKIL 3718
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERddaALLAALIAEHPVTVLNLTPSLLALLAAALPPalaSLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3719 AIGGEQSSSADWNRW---PGSVQKIHVYGPTECCIFCTGYTT----KQGFEPSTIGTSVASVS-WVVDPenHNRLAPLGS 3790
Cdd:TIGR01733  241 ILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLVdpddAPRESPVPIGRPLANTRlYVLDD--DLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3791 MGELLMEGPILARGYLNDVDKTEAAFIDDPAWllegypghPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVE 3870
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIE 390
                          410       420
                   ....*....|....*....|
gi 1820002560 3871 LGEVEHHVREClPEARQLAV 3890
Cdd:TIGR01733  391 LGEIEAALLRH-PGVREAVV 409
PRK05691 PRK05691
peptide synthase; Validated
23-1687 3.21e-134

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 478.89  E-value: 3.21e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDR----WPSsVQTINGYGPTECCIVCTGY-TSEQDFTTGTIGTSIASV-SWVVDpkDHGRLAP 96
Cdd:PRK05691  1389 SLRRLFSGGEALPAELRNRvlqrLPQ-VQLHNRYGPTETAINVTHWqCQAEDGERSPIGRPLGNVlCRVLD--AELNLLP 1465
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   97 LGSVGELLVEGPILARGYLSDPEKTAAVFINNPawlleghggYAGRQGRLYKTGDLVRYDADGNLVCLGRKDSQVKLRGQ 176
Cdd:PRK05691  1466 PGVAGELCIGGAGLARGYLGRPALTAERFVPDP---------LGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGF 1536
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  177 RVELGEVEHHVREcLPEAKQLAVevvlplgqknhatlaafiqldkgthnaLLKEKVGGDDSIARVVFLAGVEEE------ 250
Cdd:PRK05691  1537 RVEPEEIQARLLA-QPGVAQAAV---------------------------LVREGAAGAQLVGYYTGEAGQEAEaerlka 1588
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  251 -LAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASftaqqlaemrtssQGPKRQPSTEAERTMQQLWARVLGIeP 329
Cdd:PRK05691  1589 aLAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ-------------QREHVEPRTELQQQIAAIWREVLGL-P 1654
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  330 DsIGLDDSFFRLGGDSIAAIKLVGEAR-RTGLQPSVADIFRHPTLAALAsletnqynitiEETPPLSLLGEnadvaqvRD 408
Cdd:PRK05691  1655 R-VGLRDDFFALGGHSLLATQIVSRTRqACDVELPLRALFEASELGAFA-----------EQVARIQAAGE-------RN 1715
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  409 EAAAMCSVDGSaiedmylcsplQEGLMSLTTKR----------AGDYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRT 478
Cdd:PRK05691  1716 SQGAIARVDRS-----------QPVPLSYSQQRmwflwqmepdSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRT 1784
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  479 RIVQHSELGLLQVVVEE--KMQWTESESLEEYLNEDKAASmgLGDR------------LARYALIKEScGGKRWFVWTIH 544
Cdd:PRK05691  1785 TFPSVDGVPVQQVAEDSglRMDWQDFSALPADARQQRLQQ--LADSeahqpfdlergpLLRACLVKAA-EREHYFVLTLH 1861
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  545 HALYDGWSLPLVLDAVKQVYSGAALERQPSFNTF-IQY----VSQQDVKAAA------AYWQTALADCEAVLfpPLPSTV 613
Cdd:PRK05691  1862 HIVTEGWAMDIFARELGALYEAFLDDRESPLEPLpVQYldysVWQRQWLESGerqrqlDYWKAQLGNEHPLL--ELPADR 1939
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  614 TQPVADTTVK--YQCPPSPEVTS--------SNITTSTLIRAAWAIIASRYTSSEDIVFGTTVTGRNAPITgvEAMVGPT 683
Cdd:PRK05691  1940 PRPPVQSHRGelYRFDLSPELAArvrafnaqRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPES--EGLIGAF 2017
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  684 IATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTGLQRIMKMGPGPQHAcgfqtllVVHPTDDVLSSddtLGEWHSRS 763
Cdd:PRK05691  2018 LNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSA-------AYNPLFQVMCN---VQRWEFQQ 2087
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  764 DSEL-----QYFTTYALTIQCTLAVE--------GVQITASFD-------ARVVEHWvvekmlgqfsfvmQQLAEAGVE- 822
Cdd:PRK05691  2088 SRQLagmtvEYLVNDARATKFDLNLEvtdldgrlGCCLTYSRDlfdepriARMAEHW-------------QNLLEALLGd 2154
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  823 --KKVADIETTTLEDRQQLWVWNADMP--PAVDRCIHDLFAEQARARPDASAVcAWDGE-LTYGELDELSSKLAAHLVQL 897
Cdd:PRK05691  2155 pqQRLAELPLLAAAEQQQLLDSLAGEAgeARLDQTLHGLFAAQAARTPQAPAL-TFAGQtLSYAELDARANRLARALRER 2233
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  898 GVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGaqVVLTSSQHAMLFASSERHQVTVSKVS 977
Cdd:PRK05691  2234 GVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSG--IGLLLSDRALFEALGELPAGVARWCL 2311
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  978 TSQLPTVVNFAKSPVD----PGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAE 1053
Cdd:PRK05691  2312 EDDAAALAAYSDAPLPflslPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASER 2391
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1054 IITTLLYGGCICVPSESD-RRNNLAKAISTMDVNCALLTPS----VARLLEPSAVPSLKRLVLQ-GEQVSFADWNRWPGS 1127
Cdd:PRK05691  2392 LLVPLLCGARVVLRAQGQwGAEEICQLIREQQVSILGFTPSygsqLAQWLAGQGEQLPVRMCITgGEALTGEHLQRIRQA 2471
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1128 VQT---INGYGPTECSV----CCNTYSGKQGFKSGIIGTSV-ASLSWVVDAGnhnrLAPL--GSIGELLVEGPILARGYL 1197
Cdd:PRK05691  2472 FAPqlfFNAYGPTETVVmplaCLAPEQLEEGAASVPIGRVVgARVAYILDAD----LALVpqGATGELYVGGAGLAQGYH 2547
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1198 NDIDKTEAAFIDDPAwllegyeGHAGrrGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVRE--CLPE 1275
Cdd:PRK05691  2548 DRPGLTAERFVADPF-------AADG--GRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEhpAVRE 2618
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1276 ARQLAVEviLPSGQKEHALLAAfiqldkgnhnalfeeKASGEDSMAQVVFLTGVEEELAKRLPEHMVPTILFTVKAMPIT 1355
Cdd:PRK05691  2619 AVVLALD--TPSGKQLAGYLVS---------------AVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLT 2681
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1356 TSGKIDRKRLqdigasfTVQQLAEMRTSSQgpkrQPSTEVEQTMQQLWAQVLSIEpnSIGLDDSFFRLGGDSIVAMKLVG 1435
Cdd:PRK05691  2682 ANGKLDRRAL-------PAPDPELNRQAYQ----APRSELEQQLAQIWREVLNVE--RVGLGDNFFELGGDSILSIQVVS 2748
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1436 EARRTGLQLSVADIFRHPRLVDLARVQNSQFSSAAEEvpafsllgedvnavqlsqdaaamcsvaaGIVEDIYPCSPLQEG 1515
Cdd:PRK05691  2749 RARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQ----------------------------GPLQGASGLTPIQHW 2800
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1516 LMSLTAKRAGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSE--LGLLQVVIEENIQWT-EPKSLEE--Y 1590
Cdd:PRK05691  2801 FFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGrwQAEYRAVTAQELLWQvTVADFAEcaA 2880
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1591 LSEDKAVSVGLGD-PLARYAFVKEACGGKRWFVwTIHHAVYDGWSLPLILHAVKQVYSGGVLQWQPSFNA---------- 1659
Cdd:PRK05691  2881 LFADAQRSLDLQQgPLLRALLVDGPQGQQRLLL-AIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAktsafrdwaa 2959
                         1770      1780
                   ....*....|....*....|....*....
gi 1820002560 1660 -FIQYLGQQDLEATVAYWQTALADCEAVL 1687
Cdd:PRK05691  2960 rLQAYAGSESLREELGWWQAQLGGPRAEL 2988
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
7634-8036 3.81e-134

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 428.61  E-value: 3.81e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7634 TYGELDVLSSNLAGHLVQL-GVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASA 7712
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7713 QYSAR--WTSSSCHVVTVSKALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITN 7790
Cdd:TIGR01733   81 ALASRlaGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7791 LSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRR---NSLAKAISTMDVNWAFLTPSVARLLDPGLIP---SLKIL 7864
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERddaALLAALIAEHPVTVLNLTPSLLALLAAALPPalaSLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7865 AIGGEQSSSADWNRW---PGSVQKIHVYGPTECCIFCTGYTT----KQGFEPSTIGTSVASVS-WVVDPenHNRLAPLGS 7936
Cdd:TIGR01733  241 ILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLVdpddAPRESPVPIGRPLANTRlYVLDD--DLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7937 MGELLMEGPILARGYLNDVDKTEAAFIDDPAWllegypghPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVE 8016
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIE 390
                          410       420
                   ....*....|....*....|
gi 1820002560 8017 LGEVEHHVREClPEARQLAV 8036
Cdd:TIGR01733  391 LGEIEAALLRH-PGVREAVV 409
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
5636-6135 1.34e-130

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 420.01  E-value: 1.34e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5636 PHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTF 5715
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5716 RHTGAQVVVTSaqhsarwigtnhqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCW 5795
Cdd:cd05930     81 EDSGAKLVLTD-------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5796 GRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRN--DLVKAISTMDVSCALLTPSVARLL----E 5869
Cdd:cd05930    124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDpeALADLLAEEGITVLHLTPSLLRLLlqelE 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5870 PSSVPTLQMLVLQGEQVSFADWNRWPAS---VQTINGYGPTECSICCNTYSGKQGFKSGI---IGTSVASVS-WVVDPen 5942
Cdd:cd05930    204 LAALPSLRLVLVGGEALPPDLVRRWRELlpgARLVNLYGPTEATVDATYYRVPPDDEEDGrvpIGRPIPNTRvYVLDE-- 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5943 HDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpawllegyPGHPGrqGRLYKTGDLVRYDANGNLVCLGRKDSQ 6022
Cdd:cd05930    282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPN--------PFGPG--ERMYRTGDLVRWLPDGNLEFLGRIDDQ 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6023 VKLRGQRVELGEVEHHVREcLPEARQlAVeVILPSGQKDHAMLAAFVQLEEGtqnalldkeasgedsmaQVVFLASVEEE 6102
Cdd:cd05930    352 VKIRGYRIELGEIEAALLA-HPGVRE-AA-VVAREDGDGEKRLVAYVVPDEG-----------------GELDEEELRAH 411
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 6103 LAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd05930    412 LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
5649-6051 1.76e-130

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 418.21  E-value: 1.76e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5649 TYGELDALSSKLAGHL-TQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSA 5727
Cdd:TIGR01733    1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5728 QHSAR--WIGTNHQVVTVSAGSLGQLSTLVNPVGLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITN 5805
Cdd:TIGR01733   81 ALASRlaGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5806 LSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRNDLVK---AISTMDVSCALLTPSVARLLEP---SSVPTLQML 5879
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlaaLIAEHPVTVLNLTPSLLALLAAalpPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5880 VLQGEQVSFADWNRW---PASVQTINGYGPTECSICCNTYS----GKQGFKSGIIGTSVASVS-WVVDPenHDRLAPLGS 5951
Cdd:TIGR01733  241 ILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLvdpdDAPRESPVPIGRPLANTRlYVLDD--DLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5952 IGELLVEGPILARGYLNDIQKTAAVFIDDPAWllegypghPGRQGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVE 6031
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIE 390
                          410       420
                   ....*....|....*....|
gi 1820002560 6032 LGEVEHHVREClPEARQLAV 6051
Cdd:TIGR01733  391 LGEIEAALLRH-PGVREAVV 409
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
879-1281 3.88e-130

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 417.05  E-value: 3.88e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  879 TYGELDELSSKLAAHLVQL-GVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSS 957
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  958 QHA--MLFASSERHQVTVSKVSTSQLPTVVNFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTD 1035
Cdd:TIGR01733   81 ALAsrLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1036 HARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRR---NNLAKAISTMDVNCALLTPSVARLLEPSAVP---SLKRL 1109
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERddaALLAALIAEHPVTVLNLTPSLLALLAAALPPalaSLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1110 VLQGEQVSFADWNRW---PGSVQTINGYGPTECSVCCNTYS----GKQGFKSGIIGTSVASLS-WVVDAgnHNRLAPLGS 1181
Cdd:TIGR01733  241 ILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLvdpdDAPRESPVPIGRPLANTRlYVLDD--DLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1182 IGELLVEGPILARGYLNDIDKTEAAFIDDPAWllegyeghAGRRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVE 1261
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIE 390
                          410       420
                   ....*....|....*....|
gi 1820002560 1262 LGEIEHHVREClPEARQLAV 1281
Cdd:TIGR01733  391 LGEIEAALLRH-PGVREAVV 409
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
6704-7049 9.91e-128

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 413.09  E-value: 9.91e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6704 VHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 6783
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6784 PDHPASRHEDILRQTGAQVILASAQNTT---LFQS-----------SNQTVVT----------VNR-------SSY---- 6828
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTSSPSDAayvIFTSgstgkpkgvviEHRALSTsalahgralgLTSesrvlqfASYtfdv 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6829 ----ILF-----------PDENR-----------------------------------------EA-------------- 6838
Cdd:cd05918    161 sileIFTtlaaggclcipSEEDRlndlagfinrlrvtwafltpsvarlldpedvpslrtlvlggEAltqsdvdtwadrvr 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6839 -----------------------------YPF------VRPSN-AALAPLGSIGELLVEGPILARGYLNDADKTAAAFVN 6882
Cdd:cd05918    241 linaygpaectiaatvspvvpstdprnigRPLgatcwvVDPDNhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6883 DPAWLvegHGKHPGRRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLRECMPRATQMAVEVISPAGA 6962
Cdd:cd05918    321 DPAWL---KQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDG 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6963 AEQAktMVVAFLQLNDEARDALLGGNVPNDDNLSAQVVFpAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLR 7042
Cdd:cd05918    398 SSSP--QLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALV-AELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALR 474

                   ....*..
gi 1820002560 7043 EIGASFT 7049
Cdd:cd05918    475 ELAESLS 481
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1-291 7.41e-127

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 410.78  E-value: 7.41e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    1 MRVNWALLTPSVARLLEPSHIPSLRILVMGGEQVNSADWDRWPSSVQTINGYGPTECCIVCTGYTSEQDFTTGTIGTSIA 80
Cdd:cd05918    194 LRVTWAFLTPSVARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLG 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   81 SVSWVVDPKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAWLLEGHGgyaGRQGRLYKTGDLVRYDADGN 160
Cdd:cd05918    274 ATCWVVDPDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQEGS---GRGRRLYRTGDLVRYNPDGS 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  161 LVCLGRKDSQVKLRGQRVELGEVEHHVRECLPEAKQLAVEVVLPLGQKNHATLAAFIQLDKGTHNALLKEKVGGDDSIAR 240
Cdd:cd05918    351 LEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEF 430
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  241 VVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASFT 291
Cdd:cd05918    431 RALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
PRK12467 PRK12467
peptide synthase; Provisional
1527-2689 6.45e-125

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 447.69  E-value: 6.45e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1527 YIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSElGLLQVVIEE-----------NIQWTEPKS-LEEYLSED 1594
Cdd:PRK12467    72 YNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEE-GFRQVIDASlsltiplddlaNEQGRARESqIEAYINEE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1595 KAVSVGLGD-PLARYAFVKEAcGGKRWFVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQWQPSFNAF-IQY----LGQQD 1668
Cdd:PRK12467   151 VARPFDLANgPLLRVRLLRLA-DDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALpIQYadyaIWQRS 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1669 -LEA-----TVAYWQTALADCEAVL-FPTLPPTVTQP-VADATVEYQCPPLSKATSDT-------TTSTLIRAAWAIVTS 1733
Cdd:PRK12467   230 wLEAgererQLAYWQEQLGGEHTVLeLPTDRPRPAVPsYRGARLRVDLPQALSAGLKAlaqregvTLFMVLLASFQTLLH 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1734 RYTTSDDVVFGTTVTGRNTPVTgvEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAHEQTGLQRIAKMGQgPQ 1813
Cdd:PRK12467   310 RYSGQSDIRIGVPNANRNRVET--ERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQ-PE 386
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1814 HACS----FQTLLVVQPVDDVLDNTLGEWRDHSELQEFTT------YTLMLQCMLAAEGVQITASFDTRVIEKWVVEKML 1883
Cdd:PRK12467   387 RSLShsplFQVMFNHQNTATGGRDREGAQLPGLTVEELSWarhtaqFDLALDTYESAQGLWAAFTYATDLFEATTIERLA 466
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1884 RQFSFIMQQLAEAGAEKTVSDIETTTPEDRQQLWAWNQEVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDAL 1963
Cdd:PRK12467   467 THWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQ 546
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1964 SSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSAQHSARW--- 2040
Cdd:PRK12467   547 ANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLpvp 626
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2041 IGTNHQVVTVSAGSLEQFSTlVNPvDLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLRALQFT 2120
Cdd:PRK12467   627 AGLRSLCLDEPADLLCGYSG-HNP-EVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVS 704
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2121 AYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSSVARLL--DPC--LVPSLKVLVLGGEQVN 2194
Cdd:PRK12467   705 TFAFDLGVTELFGALASGATLHLLPPDCARDaeAFAALMADQGVTVLKIVPSHLQALlqASRvaLPRPQRALVCGGEALQ 784
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2195 STDWGKW---PSSVQTINGYGPTECCVFCTGYT-GIQGFQSGN--IGTSIASVSWVVdPENHGRLAPLGSIGELLVEGPI 2268
Cdd:PRK12467   785 VDLLARVralGPGARLINHYGPTETTVGVSTYElSDEERDFGNvpIGQPLANLGLYI-LDHYLNPVPVGVVGELYIGGAG 863
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2269 LARGYLNDVDKTQAAFIDDPAwlleGYPGhegrqGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRK 2348
Cdd:PRK12467   864 LARGYHRRPALTAERFVPDPF----GADG-----GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLA 934
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2349 cLPEANQLAVEVVPPSGerdHAMLAAFirlddetrnsplIIKYAEDNSTAQIVFLTGIEEELSERLPQHMVPTVFFALVH 2428
Cdd:PRK12467   935 -QPGVREAVVLAQPGDA---GLQLVAY------------LVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDS 998
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2429 FPTTTSGKTDRKRLREIGASftaqqlaemrtSSEGPKRQPSTEAERTMQQLWAQVLGieLESIGLDDSFFRLGGDSITAM 2508
Cdd:PRK12467   999 LPLTPNGKLDRKALPKPDAS-----------AVQATFVAPQTELEKRLAAIWADVLK--VERVGLTDNFFELGGHSLLAT 1065
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2509 QISSSAR-ALHLSVSTGDILKKKTIALIAREIL---PSTSTFSRSVWRD---PVNNAFDLtpiQHLYLTLDPsGRSSFDQ 2581
Cdd:PRK12467  1066 QVISRVRqRLGIQVPLRTLFEHQTLAGFAQAVAaqqQGAQPALPDVDRDqplPLSYAQER---QWFLWQLEP-GSAAYHI 1141
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2582 CFFLELRNRVQPQLLVTALTALVQRHSMLRARFqRQTGGRWQQYIseHDSSSLIVNHIHTRDTTEIVEALR-----QSRG 2656
Cdd:PRK12467  1142 PQALRLKGPLDIEALERSFDALVARHESLRTTF-VQEDGRTRQVI--HPVGSLTLEEPLLLAADKDEAQLKvyveaEARQ 1218
                         1210      1220      1230
                   ....*....|....*....|....*....|....
gi 1820002560 2657 SLDIERGPVL-AAVLCDAGERQSLFVAIHHLVVD 2689
Cdd:PRK12467  1219 PFDLEQGPLLrVGLLRLAADEHVLVLTLHHIVSD 1252
PRK12467 PRK12467
peptide synthase; Provisional
7203-8512 2.87e-121

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 435.74  E-value: 2.87e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7203 YIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSElGLLQVVVEE-----------KIQWTESEA-LEEYLKED 7270
Cdd:PRK12467    72 YNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEE-GFRQVIDASlsltiplddlaNEQGRARESqIEAYINEE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7271 KAVSMGLGD-PLAHYALVKEAwGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAF-IQY----LGQQD 7344
Cdd:PRK12467   151 VARPFDLANgPLLRVRLLRLA-DDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALpIQYadyaIWQRS 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7345 -LEA-----TAAYWQTALSDCEAVLFPPL--PSTVTQPVADTTVEYQCPPLSKATLDT-------TTSTLIRAAWAIVTS 7409
Cdd:PRK12467   230 wLEAgererQLAYWQEQLGGEHTVLELPTdrPRPAVPSYRGARLRVDLPQALSAGLKAlaqregvTLFMVLLASFQTLLH 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7410 CYTSSDDVVYGTTVTGRNApiAGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAH-----EQ--TGLQHIA 7482
Cdd:PRK12467   310 RYSGQSDIRIGVPNANRNR--VETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHqdlpfEQlvEALQPER 387
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7483 KLGSGPRhacgFQTLLVVQPvdDVLGSDDMLGEWRSYSKMQDFTTYALMVQFTLA------AEGVQITASFDARVIEHWV 7556
Cdd:PRK12467   388 SLSHSPL----FQVMFNHQN--TATGGRDREGAQLPGLTVEELSWARHTAQFDLAldtyesAQGLWAAFTYATDLFEATT 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7557 LEKMLRQFSFIMQQLAEAsEDSKVADIDTTTPEDRQ-QLWAWNADVPPAIERCVHDLFAEQARARPGAPAICAWDGELTY 7635
Cdd:PRK12467   462 IERLATHWRNLLEAIVAE-PRRRLGELPLLDAEERArELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSY 540
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7636 GELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYS 7715
Cdd:PRK12467   541 AELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLL 620
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7716 ARW---TSSSCHVVTVSKALSSQLPAVvdSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLS 7792
Cdd:PRK12467   621 AQLpvpAGLRSLCLDEPADLLCGYSGH--NPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD 698
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7793 RVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL----DPGLIPSLKILAI 7866
Cdd:PRK12467   699 SMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDaeAFAALMADQGVTVLKIVPSHLQALlqasRVALPRPQRALVC 778
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7867 GGEQSSSADWNRW----PGsVQKIHVYGPTECCIFCTGYTTK---QGFEPSTIGTSVASVSWVVdPENHNRLAPLGSMGE 7939
Cdd:PRK12467   779 GGEALQVDLLARVralgPG-ARLINHYGPTETTVGVSTYELSdeeRDFGNVPIGQPLANLGLYI-LDHYLNPVPVGVVGE 856
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7940 LLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGE 8019
Cdd:PRK12467   857 LYIGGAGLARGYHRRPALTAERFVPDPF-------GADG--GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGE 927
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8020 VEHHVREcLPEARQLAVEVIlpSGQKNHAMLAVFVqlgkgthiahleeKAGGEDSMAQVVFLTGTEEELAKRLPKHMVPT 8099
Cdd:PRK12467   928 IEARLLA-QPGVREAVVLAQ--PGDAGLQLVAYLV-------------PAAVADGAEHQATRDELKAQLRQVLPDYMVPA 991
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8100 VFFALLHFPMTTSGKADRKRLREIGASftaqqlaetqtSSQGPKRQPLTEAEQTMQQLWARVLGIDAdiIGLDDSFFRLG 8179
Cdd:PRK12467   992 HLLLLDSLPLTPNGKLDRKALPKPDAS-----------AVQATFVAPQTELEKRLAAIWADVLKVER--VGLTDNFFELG 1058
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8180 GDSIAAMKLVGEARRT-GLQLSVADIFRHPRLidlaslkSTFCNSVVEEVP-AFSLLSPVMKDAmfsvtepfgpslridd 8257
Cdd:PRK12467  1059 GHSLLATQVISRVRQRlGIQVPLRTLFEHQTL-------AGFAQAVAAQQQgAQPALPDVDRDQ---------------- 1115
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8258 itdVVPASYIQ--QFYIATgVRAPREAFNYPF-IDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIPRHQDL 8334
Cdd:PRK12467  1116 ---PLPLSYAQerQWFLWQ-LEPGSAAYHIPQaLRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSL 1191
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8335 PFSIFEVNGALAE--------ESQAIHIRDLDQTSPLGLptsfTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIY 8406
Cdd:PRK12467  1192 TLEEPLLLAADKDeaqlkvyvEAEARQPFDLEQGPLLRV----GLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALY 1267
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8407 Q-----QEPLLSTTGFHsYLAYV--------HNQRSASINYWSRLLKGSH--ITNITSKLRPKLGKDTTIRSvkveRVIR 8471
Cdd:PRK12467  1268 AaysqgQSLQLPALPIQ-YADYAvwqrqwmdAGERARQLAYWKAQLGGEQpvLELPTDRPRPAVQSHRGARL----AFEL 1342
                         1370      1380      1390      1400      1410
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8472 TPQLPTGL---------TMASLVSSAWAVVLSHISGEEDVVYGLVVAGRN 8512
Cdd:PRK12467  1343 PPALAEGLralarregvTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRN 1392
PRK12316 PRK12316
peptide synthase; Provisional
5214-6458 2.92e-121

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 435.93  E-value: 2.92e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5214 AGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQV-------VVEEKIQWTESKRLEEYLREDKA 5286
Cdd:PRK12316    69 SGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVpldrpleVEFEDCSGLPEAEQEARLRDEAQ 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5287 VSMGLGDRLA-----RYALIKepYDGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGAVPERQPSFNAF-IQY----LG 5356
Cdd:PRK12316   149 RESLQPFDLCegpllRVRLLR--LGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALpIQYadyaLW 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5357 QQD-LEAAT-----LYWQTALADCKAAL-FPT-LPPTVTQPVADTTVEYQCPPP-----SQSAT--DITTSTLVRAAWAI 5421
Cdd:PRK12316   227 QRSwLEAGEqerqlEYWRAQLGEEHPVLeLPTdHPRPAVPSYRGSRYEFSIDPAlaealRGTARrqGLTLFMLLLGAFNV 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5422 VTSRYTSSDDVVFGATVTGRNApiAGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAHEQTGLQRIA---K 5498
Cdd:PRK12316   307 LLHRYSGQTDIRVGVPIANRNR--AEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVealK 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5499 MSPGARHACGFQTLLVVQP-TDDVLGSDDMLG------EWRSYSEMQDFT--TY----ALMVQCTLAKDRvevtasFDAR 5565
Cdd:PRK12316   385 VERSLSHSPLFQVMYNHQPlVADIEALDTVAGlefgqlEWKSRTTQFDLTldTYekggRLHAALTYATDL------FEAR 458
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5566 VIEqwvveKMLRQFGFVMQQLAEAGaEKTVSDIETTTLEDRQQL-WAWNQ-NVPPAIERCVHDLFTEQAKARPHAPAICA 5643
Cdd:PRK12316   459 TVE-----RMARHWQNLLRGMVENP-QARVDELPMLDAEERGQLvEGWNAtAAEYPLQRGVHRLFEEQVERTPEAPALAF 532
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5644 WDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVV 5723
Cdd:PRK12316   533 GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLL 612
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5724 VTSaQHSARWIGTNH--QVVTVSAGSLGQLSTLVNPVGLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTS-CWGRgRA 5800
Cdd:PRK12316   613 LSQ-SHLGRKLPLAAgvQVLDLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRlCWMQ-QA 690
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5801 FGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRN--DLVKAISTMDVSCALLTPSVARLL----EPSSVP 5874
Cdd:PRK12316   691 YGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDpaKLVELINREGVDTLHFVPSMLQAFlqdeDVASCT 770
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5875 TLQMLVLQGEQVSFADWNRWPASVQT---INGYGPTECSI--CCNTYSgKQGFKSGIIGTSVASV-SWVVDPENHDrlAP 5948
Cdd:PRK12316   771 SLRRIVCSGEALPADAQEQVFAKLPQaglYNLYGPTEAAIdvTHWTCV-EEGGDSVPIGRPIANLaCYILDANLEP--VP 847
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5949 LGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypghpGRQGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQ 6028
Cdd:PRK12316   848 VGVLGELYLAGRGLARGYHGRPGLTAERFVPSPF----------VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 917
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6029 RVELGEVEHHVREcLPEARQLAVEVIlpSGQKdhamLAAFVQLEegtqnallDKEASGEDSMAQvvflasveeELAKRLP 6108
Cdd:PRK12316   918 RIELGEIEARLLE-HPWVREAAVLAV--DGKQ----LVGYVVLE--------SEGGDWREALKA---------HLAASLP 973
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6109 EHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQIAnmqtssqdpkrQPSTEAEQTMQKLWAQVLGIElnGIGLDD 6188
Cdd:PRK12316   974 EYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYV-----------APRNALERTLAAIWQDVLGVE--RVGLDD 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6189 SFFRLGGDSIAAMKLVGEARRIGLQLSVADIFRYARLVDLasldtsqcnsaigevpafsllggraadtAQVSQDAAAMcS 6268
Cdd:PRK12316  1041 NFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSL----------------------------ALVAKAGQAT-A 1091
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6269 VDASSVEDMYPCSPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSE--LGLLQVVV 6346
Cdd:PRK12316  1092 ADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGgwQQAYAAPQ 1171
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6347 EEKIQWTESKRLEEYLR---EDKAVSMGLGD-PLARYAIIKEAWGGKRwFVWTIHHALYDGWSLPRVLQAVKQAYNGAVL 6422
Cdd:PRK12316  1172 AGEVLWQRQAASEEELLalcEEAQRSLDLEQgPLLRALLVDMADGSQR-LLLVIHHLVVDGVSWRILLEDLQRAYADLDA 1250
                         1290      1300      1310      1320
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 6423 ETQPSFNAFIQYLSQQDLEATA-----AYWQTALADCEATL 6458
Cdd:PRK12316  1251 DLPARTSSYQAWARRLHEHAGAraeelDYWQAQLEDAPHEL 1291
PRK12316 PRK12316
peptide synthase; Provisional
442-1682 7.58e-120

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 431.30  E-value: 7.58e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  442 AGDYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQV-------VVEEKMQWTESESLEEYLNEDKA 514
Cdd:PRK12316    69 SGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVpldrpleVEFEDCSGLPEAEQEARLRDEAQ 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  515 ASMGLGDRLA-----RYALIKEScGGKRWFVWTIHHALYDGWSLPLVLDAVKQVYSGAALERQPSFNTF-IQYVS----Q 584
Cdd:PRK12316   149 RESLQPFDLCegpllRVRLLRLG-EEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALpIQYADyalwQ 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  585 QDVKAAA------AYWQTALADCEAVLFPPL--PSTVTQPVADTTVKYQCPP--SPEVTSS----NITTSTLIRAAWAII 650
Cdd:PRK12316   228 RSWLEAGeqerqlEYWRAQLGEEHPVLELPTdhPRPAVPSYRGSRYEFSIDPalAEALRGTarrqGLTLFMLLLGAFNVL 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  651 ASRYTSSEDIVFGTTVTGRNApiTGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTGLQRI---MKM 727
Cdd:PRK12316   308 LHRYSGQTDIRVGVPIANRNR--AEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLveaLKV 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  728 GPGPQHACGFQTLLVVHPTDDVLSSDDTLG-------EWHSRS---DSELQ-YFTTYALTIQCTLAvegvqiTASFDARV 796
Cdd:PRK12316   386 ERSLSHSPLFQVMYNHQPLVADIEALDTVAglefgqlEWKSRTtqfDLTLDtYEKGGRLHAALTYA------TDLFEART 459
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  797 VEhwvveKMLGQFSFVMQQLAEAGvEKKVADIETTTLEDRQQL-WVWNADmpPAV---DRCIHDLFAEQARARPDASAVC 872
Cdd:PRK12316   460 VE-----RMARHWQNLLRGMVENP-QARVDELPMLDAEERGQLvEGWNAT--AAEyplQRGVHRLFEEQVERTPEAPALA 531
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  873 AWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQV 952
Cdd:PRK12316   532 FGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQL 611
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  953 VLTSSQHAMLFASSERHQVTVSKVSTSQLPTVVNFA-KSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAF 1031
Cdd:PRK12316   612 LLSQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEENpGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAY 691
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1032 GYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRN--NLAKAISTMDVNCALLTPSVARLL----EPSAVPS 1105
Cdd:PRK12316   692 GLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDpaKLVELINREGVDTLHFVPSMLQAFlqdeDVASCTS 771
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1106 LKRLVLQGEQVSFADWNRWPGSVQT---INGYGPTECS--VCCNTYSgKQGFKSGIIGTSVASL-SWVVDAgnHNRLAPL 1179
Cdd:PRK12316   772 LRRIVCSGEALPADAQEQVFAKLPQaglYNLYGPTEAAidVTHWTCV-EEGGDSVPIGRPIANLaCYILDA--NLEPVPV 848
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1180 GSIGELLVEGPILARGYLNDIDKTEAAFIDDPawllegyeghAGRRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQR 1259
Cdd:PRK12316   849 GVLGELYLAGRGLARGYHGRPGLTAERFVPSP----------FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 918
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1260 VELGEIEHHVREcLPEARQLAVEVIlpSGQKehalLAAFIQLDkgnhnalfEEKASGEDSMAQvvfltgveeELAKRLPE 1339
Cdd:PRK12316   919 IELGEIEARLLE-HPWVREAAVLAV--DGKQ----LVGYVVLE--------SEGGDWREALKA---------HLAASLPE 974
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1340 HMVPTILFTVKAMPITTSGKIDRKRLQDIGASFTVQQLAemrtssqgpkrQPSTEVEQTMQQLWAQVLSIEPnsIGLDDS 1419
Cdd:PRK12316   975 YMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYV-----------APRNALERTLAAIWQDVLGVER--VGLDDN 1041
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1420 FFRLGGDSIVAMKLVGEARRTGLQLSVADIFRHPRLVDLARVQNSQFSSAAEEVPafsllgedvnavqlsqdaaamcsvA 1499
Cdd:PRK12316  1042 FFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGP------------------------A 1097
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1500 AGIVediyPCSPLQEGLMSLTAKRAGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSE--LGLLQVVIEE 1577
Cdd:PRK12316  1098 SGEV----ALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGgwQQAYAAPQAG 1173
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1578 NIQWTEPKSLEEYLS---EDKAVSVGLGD-PLARYAFVKEACGGKRwFVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQW 1653
Cdd:PRK12316  1174 EVLWQRQAASEEELLalcEEAQRSLDLEQgPLLRALLVDMADGSQR-LLLVIHHLVVDGVSWRILLEDLQRAYADLDADL 1252
                         1290      1300      1310
                   ....*....|....*....|....*....|....
gi 1820002560 1654 QP---SFNAFIQYLGQQ--DLEATVAYWQTALAD 1682
Cdd:PRK12316  1253 PArtsSYQAWARRLHEHagARAEELDYWQAQLED 1286
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
3465-3974 3.95e-118

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 385.79  E-value: 3.95e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 3544
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3545 HPASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTvskaLSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVL 3624
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVI----DEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3625 EHRAVATSCLGHGRAfGITNLSRVLQFASYTFDACIAEIITTLLCGGCiCVPSDSD---RRNSLAKAISTMDVNWAFLTP 3701
Cdd:cd12117    157 THRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGAR-LVLAPKGtllDPDALGALIAEEGVTVLWLTA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3702 SVARLL---DPGLIPSLKILAIGGEQSSSADWNRW----PGsVQKIHVYGPTECCIFCTGYTTKQGFEPST---IGTSVA 3771
Cdd:cd12117    235 ALFNQLadeDPECFAGLRELLTGGEVVSPPHVRRVlaacPG-LRLVNGYGPTENTTFTTSHVVTELDEVAGsipIGRPIA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3772 SVS-WVVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPawllegypghPGRQGRLYKTGDLVQYNADG 3850
Cdd:cd12117    314 NTRvYVLDE--DGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADP----------FGPGERLYRTGDLARWLPDG 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3851 NLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVEVILPSGQKDHamLAAFVQLEEGTQnalldkeaggedsma 3930
Cdd:cd12117    382 RLEFLGRIDDQVKIRGFRIELGEIEAALRAH-PGVREAVVVVREDAGGDKR--LVAYVVAEGALD--------------- 443
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 3931 qvvfLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd12117    444 ----AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
4547-5054 1.11e-116

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 381.55  E-value: 1.11e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHP 4626
Cdd:cd12117      3 FEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4627 ASRHEHIFRQTGAQVVLASAQYATLWTSLGRSVVIVSEASTSQLPVvtktADPSVNPGNAAYAIFTSGSTGIPKGVVLEH 4706
Cdd:cd12117     83 AERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGN----PAVPVSPDDLAYVMYTSGSTGRPKGVAVTH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4707 KAVVTSCLGHGQAfGITDHTRVLQFASYTFDACIAEIITTLLCCGCiCVPSDSDRRNN---LAKAINAMDVNWALLTPSV 4783
Cdd:cd12117    159 RGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGAR-LVLAPKGTLLDpdaLGALIAEEGVTVLWLTAAL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4784 ARML---DPCVVQSLKILVLGGEQVnSADW-----DRWPKsIQTINAYGPTECSICCTTYSGKQGFKSGT---IGTSIVS 4852
Cdd:cd12117    237 FNQLadeDPECFAGLRELLTGGEVV-SPPHvrrvlAACPG-LRLVNGYGPTENTTFTTSHVVTELDEVAGsipIGRPIAN 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4853 VS-WVVDPenHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygghsGRQGRLYKTGDLVRYDADGN 4931
Cdd:cd12117    315 TRvYVLDE--DGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF----------GPGERLYRTGDLARWLPDGR 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4932 LVYLGRKDSQVKLRGQRVELGEVEHHVRECltEAKQLAVeVIVPEGEGGYAMLAAFVqlgddtyntlVKEKAGGDsltvq 5011
Cdd:cd12117    383 LEFLGRIDDQVKIRGFRIELGEIEAALRAH--PGVREAV-VVVREDAGGDKRLVAYV----------VAEGALDA----- 444
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 5012 vvflDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd12117    445 ----AELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
7611-8120 2.91e-116

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 380.39  E-value: 2.91e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 7690
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7691 HPASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTvskaLSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVL 7770
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVI----DEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7771 EHRAVATSCLGHGRAfGITNLSRVLQFASYTFDACIAEIITTLLCGGCiCVPSDSD---RRNSLAKAISTMDVNWAFLTP 7847
Cdd:cd12117    157 THRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGAR-LVLAPKGtllDPDALGALIAEEGVTVLWLTA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7848 SVARLL---DPGLIPSLKILAIGGEQSSSADWNRW----PGsVQKIHVYGPTECCIFCTGYTTKQGFEPST---IGTSVA 7917
Cdd:cd12117    235 ALFNQLadeDPECFAGLRELLTGGEVVSPPHVRRVlaacPG-LRLVNGYGPTENTTFTTSHVVTELDEVAGsipIGRPIA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7918 SVS-WVVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPawllegypghPGRQGRLYKTGDLVQYNADG 7996
Cdd:cd12117    314 NTRvYVLDE--DGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADP----------FGPGERLYRTGDLARWLPDG 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7997 NLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVEVILPSGQKNHamLAVFVQlgkgthiahleekAGGEDSMA 8076
Cdd:cd12117    382 RLEFLGRIDDQVKIRGFRIELGEIEAALRAH-PGVREAVVVVREDAGGDKR--LVAYVV-------------AEGALDAA 445
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 8077 QVvfltgtEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd12117    446 EL------RAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
856-1365 5.78e-115

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 376.54  E-value: 5.78e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  856 DLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPG 935
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  936 HPASRHEEIFKQIGAQVVLTssQHAMLFASSERHQVTVSKVSTSQLPTVVnfAKSPVDPGNTAYIIFTSGTTGIPKGVVL 1015
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLT--DRSLAGRAGGLEVAVVIDEALDAGPAGN--PAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1016 QHRAVTTSCLGHGEAfGYTDHARVLQFASYTFDACIAEIITTLLYGGCiCVPSESDRRNN---LAKAISTMDVNCALLTP 1092
Cdd:cd12117    157 THRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGAR-LVLAPKGTLLDpdaLGALIAEEGVTVLWLTA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1093 SVARLL---EPSAVPSLKRLVLQGEQVSFADWNRW----PGsVQTINGYGPTECSVCCNTYSGKQGFKSGI---IGTSVA 1162
Cdd:cd12117    235 ALFNQLadeDPECFAGLRELLTGGEVVSPPHVRRVlaacPG-LRLVNGYGPTENTTFTTSHVVTELDEVAGsipIGRPIA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1163 SLS-WVVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawllegyeghAGRRGRLYKTGDLVRCDADG 1241
Cdd:cd12117    314 NTRvYVLDE--DGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADP----------FGPGERLYRTGDLARWLPDG 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1242 NLVCLGRKDSQVKVRGQRVELGEIEHHVREClPEARQLAVEVILPSGQKehALLAAFIqldkgnhnaLFEEKASGEDsma 1321
Cdd:cd12117    382 RLEFLGRIDDQVKIRGFRIELGEIEAALRAH-PGVREAVVVVREDAGGD--KRLVAYV---------VAEGALDAAE--- 446
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 1322 qvvfltgVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd12117    447 -------LRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
1933-2442 1.98e-114

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 375.00  E-value: 1.98e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 2012
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2013 HPASRHEDIFRQTGAQVVVTSAQHSARWIGTnhQVVTVSAGSLEQFSTLVNPVdlPAKPENAAYVMFTSGSTGTPKGVVL 2092
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGL--EVAVVIDEALDAGPAGNPAV--PVSPDDLAYVMYTSGSTGRPKGVAV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2093 EHRAVVTSCLGHGQAfGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCiCVPSDSE---RRDNLAKAITDMQVNWGYLTS 2169
Cdd:cd12117    157 THRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGAR-LVLAPKGtllDPDALGALIAEEGVTVLWLTA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2170 SVARLL---DPCLVPSLKVLVLGGEQVNstdwgkwPSSVQT----------INGYGPTECCVFCTGYTGIQGFQSGN--- 2233
Cdd:cd12117    235 ALFNQLadeDPECFAGLRELLTGGEVVS-------PPHVRRvlaacpglrlVNGYGPTENTTFTTSHVVTELDEVAGsip 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2234 IGTSIASVS-WVVDPenHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegypgheGRQGRLYKTGDLV 2312
Cdd:cd12117    308 IGRPIANTRvYVLDE--DGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF----------GPGERLYRTGDLA 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2313 RYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKClPEANQLAVEVVPPSGerDHAMLAAFIRLDDETrnspliikya 2392
Cdd:cd12117    376 RWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAH-PGVREAVVVVREDAG--GDKRLVAYVVAEGAL---------- 442
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2393 ednSTAQivfltgIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd12117    443 ---DAAE------LRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
PRK12316 PRK12316
peptide synthase; Provisional
7200-8442 1.19e-113

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 410.89  E-value: 1.19e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7200 AGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQV-------VVEEKIQWTESEALEEYLkEDKA 7272
Cdd:PRK12316    69 SGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVpldrpleVEFEDCSGLPEAEQEARL-RDEA 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7273 VSMGL------GDPLAHYALVKEAwGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAF-IQY----LG 7341
Cdd:PRK12316   148 QRESLqpfdlcEGPLLRVRLLRLG-EEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALpIQYadyaLW 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7342 QQD-LEA-----TAAYWQTALSDCEAVLFPPL--PSTVTQPVADTTVEYQCPPLSKATLDTTTS-------TLIRAAWAI 7406
Cdd:PRK12316   227 QRSwLEAgeqerQLEYWRAQLGEEHPVLELPTdhPRPAVPSYRGSRYEFSIDPALAEALRGTARrqgltlfMLLLGAFNV 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7407 VTSCYTSSDDVVYGTTVTGRNApiAGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIA---K 7483
Cdd:PRK12316   307 LLHRYSGQTDIRVGVPIANRNR--AEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVealK 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7484 LGSGPRHACGFQTLLVVQP-VDDVLGSDDMLG------EWRSYSKMQDFT--TY----ALMVQFTLAaegvqiTASFDAR 7550
Cdd:PRK12316   385 VERSLSHSPLFQVMYNHQPlVADIEALDTVAGlefgqlEWKSRTTQFDLTldTYekggRLHAALTYA------TDLFEAR 458
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7551 VIE----HW--VLEKMLRQfsfimqqlAEASedskVADIDTTTPEDRQQL-WAWNADVPP-AIERCVHDLFAEQARARPG 7622
Cdd:PRK12316   459 TVErmarHWqnLLRGMVEN--------PQAR----VDELPMLDAEERGQLvEGWNATAAEyPLQRGVHRLFEEQVERTPE 526
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7623 APAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQ 7702
Cdd:PRK12316   527 APALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLED 606
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7703 TGAQVVVaSAQYSARWTSSSCHV-VTVSKALSSQLPAVVDST-NTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 7780
Cdd:PRK12316   607 SGVQLLL-SQSHLGRKLPLAAGVqVLDLDRPAAWLEGYSEENpGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLC 685
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7781 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSV--ARLLDPG 7856
Cdd:PRK12316   686 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDpaKLVELINREGVDTLHFVPSMlqAFLQDED 765
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7857 L--IPSLKILAIGGEQSSSADWNRWPGSVQKIHV---YGPTECCIFCTGYT-TKQGFEPSTIGTSVASV-SWVVDPENHn 7929
Cdd:PRK12316   766 VasCTSLRRIVCSGEALPADAQEQVFAKLPQAGLynlYGPTEAAIDVTHWTcVEEGGDSVPIGRPIANLaCYILDANLE- 844
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7930 rLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypghpGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVK 8009
Cdd:PRK12316   845 -PVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPF----------VAGERMYRTGDLARYRADGVIEYAGRIDHQVK 913
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8010 VRGQRVELGEVEHHVREcLPEARQLAVEVIlpSGQKnhaMLAVFVqlgkgthiahLEEKAGGEDSMAQvvfltgteEELA 8089
Cdd:PRK12316   914 LRGLRIELGEIEARLLE-HPWVREAAVLAV--DGKQ---LVGYVV----------LESEGGDWREALK--------AHLA 969
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8090 KRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGASFTAQQLAetqtssqgpkrQPLTEAEQTMQQLWARVLGIDAdiI 8169
Cdd:PRK12316   970 ASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYV-----------APRNALERTLAAIWQDVLGVER--V 1036
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8170 GLDDSFFRLGGDSIAAMKLVGEARRTGLQLSVADIFRHPRLIDLASLKStfcnsvveevpafsllspvmkdamfsvtepF 8249
Cdd:PRK12316  1037 GLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAK------------------------------A 1086
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8250 GPSLRIDD--ITDVVPASYIQQFYIATGVrAPREAFNYP-FIDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQ 8326
Cdd:PRK12316  1087 GQATAADQgpASGEVALAPVQRWFFEQAI-PQRQHWNQSlLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQ 1165
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8327 ---------VIPRHQDLPFSIFEvngALAEESQAihIRDLDQtSPLglpTSFTLVRNASGMNRLIIRLSHAQYDGVCMPV 8397
Cdd:PRK12316  1166 ayaapqageVLWQRQAASEEELL---ALCEEAQR--SLDLEQ-GPL---LRALLVDMADGSQRLLLVIHHLVVDGVSWRI 1236
                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 8398 IWASLASIYQQ-EPLL--STTGFHSYLAYVHNQ---RSASINYWSRLLKGS 8442
Cdd:PRK12316  1237 LLEDLQRAYADlDADLpaRTSSYQAWARRLHEHagaRAEELDYWQAQLEDA 1287
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
3467-3975 1.94e-113

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 372.45  E-value: 1.94e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3467 FTEQAKARPHAPAIcAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 3545
Cdd:cd17651      1 FERQAARTPDAPAL-VAEGRrLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3546 PASRHEEIFEQTGAQVVVASAQYSARwtsSSCHVVTVSKALSSQLPA-VVDSTNTSVRPENAAYIIFTSGSTGVPKGVVL 3624
Cdd:cd17651     80 PAERLAFMLADAGPVLVLTHPALAGE---LAVELVAVTLLDQPGAAAgADAEPDPALDADDLAYVIYTSGSTGRPKGVVM 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3625 EHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNS--LAKAISTMDVNWAFLTPS 3702
Cdd:cd17651    157 PHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPpaLAAWLDEQRISRVFLPTV 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3703 VARLLD------PGLIPSLKILAIGGEQSSS----ADWNRWPGSVQKIHVYGPTECCiFCTGYTTKQGF----EPSTIGT 3768
Cdd:cd17651    237 ALRALAehgrplGVRLAALRYLLTGGEQLVLtedlREFCAGLPGLRLHNHYGPTETH-VVTALSLPGDPaawpAPPPIGR 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3769 SVASVS-WVVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypghpGRQGRLYKTGDLVQYN 3847
Cdd:cd17651    316 PIDNTRvYVLDA--ALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF----------VPGARMYRTGDLARWL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3848 ADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKDhAMLAAFVQLEEGtqnalldkeagged 3927
Cdd:cd17651    384 PDGELEFLGRADDQVKIRGFRIELGEIEAALARH-PGVREAVV-LAREDRPGE-KRLVAYVVGDPE-------------- 446
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 3928 smaQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd17651    447 ---APVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
858-1365 1.96e-109

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 360.89  E-value: 1.96e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  858 FAEQARARPDASAVcAWDGE-LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGH 936
Cdd:cd17651      1 FERQAARTPDAPAL-VAEGRrLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  937 PASRHEEIFKQIGAQVVLTSSQHAMLFASSERHQVTVSKVSTSQLPTVVNFAksPVDPGNTAYIIFTSGTTGIPKGVVLQ 1016
Cdd:cd17651     80 PAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDP--ALDADDLAYVIYTSGSTGRPKGVVMP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1017 HRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRN--NLAKAISTMDVNCALLTPSV 1094
Cdd:cd17651    158 HRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDppALAAWLDEQRISRVFLPTVA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1095 ARLLEPSAV------PSLKRLVLQGEQVSF----ADWNRWPGSVQTINGYGPTECSVCcnTYSGKQGFKSG-----IIGT 1159
Cdd:cd17651    238 LRALAEHGRplgvrlAALRYLLTGGEQLVLtedlREFCAGLPGLRLHNHYGPTETHVV--TALSLPGDPAAwpappPIGR 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1160 SVASLS-WVVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawllegyeghAGRRGRLYKTGDLVRCD 1238
Cdd:cd17651    316 PIDNTRvYVLDA--ALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDP----------FVPGARMYRTGDLARWL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1239 ADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREClPEARQLAVeVILPSGQKEHAlLAAFIQLDKGnhnalfeekasged 1318
Cdd:cd17651    384 PDGELEFLGRADDQVKIRGFRIELGEIEAALARH-PGVREAVV-LAREDRPGEKR-LVAYVVGDPE-------------- 446
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 1319 smaQVVFLTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17651    447 ---APVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
5626-6135 4.23e-109

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 359.59  E-value: 4.23e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 5705
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5706 HPASRHEDTFRHTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLGQLStlvnPVGLPAIPENAVYIMFTSGSTGIPKGVVL 5785
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAG----NPAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5786 EHRAVVTSCWGRGRAfGITNLSRVLQFASYTFDACMDEIITTLMYGGCiCVPSDSDRRND---LVKAISTMDVSCALLTP 5862
Cdd:cd12117    157 THRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGAR-LVLAPKGTLLDpdaLGALIAEEGVTVLWLTA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5863 SVARLL---EPSSVPTLQMLVLQGEQVSFADWNRWPA---SVQTINGYGPTECSICCNTYSGKQGFKSGI---IGTSVAS 5933
Cdd:cd12117    235 ALFNQLadeDPECFAGLRELLTGGEVVSPPHVRRVLAacpGLRLVNGYGPTENTTFTTSHVVTELDEVAGsipIGRPIAN 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5934 VS-WVVDPenHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPawllegypghPGRQGRLYKTGDLVRYDANGN 6012
Cdd:cd12117    315 TRvYVLDE--DGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADP----------FGPGERLYRTGDLARWLPDGR 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6013 LVCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQLAVEVILPSGQKDHamLAAFVQLEEGTQnalldkeasgedsmaq 6092
Cdd:cd12117    383 LEFLGRIDDQVKIRGFRIELGEIEAALRAH-PGVREAVVVVREDAGGDKR--LVAYVVAEGALD---------------- 443
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 6093 vvfLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd12117    444 ---AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
7613-8121 5.49e-109

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 359.74  E-value: 5.49e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7613 FAEQARARPGAPAIcAWDGE-LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 7691
Cdd:cd17651      1 FERQAARTPDAPAL-VAEGRrLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7692 PASRHEEIFEQTGAQVVVASAQYSARwtsSSCHVVTVSKALSSQLPA-VVDSTNTSVRPENAAYIIFTSGSTGVPKGVVL 7770
Cdd:cd17651     80 PAERLAFMLADAGPVLVLTHPALAGE---LAVELVAVTLLDQPGAAAgADAEPDPALDADDLAYVIYTSGSTGRPKGVVM 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7771 EHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNS--LAKAISTMDVNWAFLTPS 7848
Cdd:cd17651    157 PHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPpaLAAWLDEQRISRVFLPTV 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7849 VARLLD------PGLIPSLKILAIGGEQSSS----ADWNRWPGSVQKIHVYGPTECCiFCTGYTTKQGF----EPSTIGT 7914
Cdd:cd17651    237 ALRALAehgrplGVRLAALRYLLTGGEQLVLtedlREFCAGLPGLRLHNHYGPTETH-VVTALSLPGDPaawpAPPPIGR 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7915 SVASVS-WVVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypghpGRQGRLYKTGDLVQYN 7993
Cdd:cd17651    316 PIDNTRvYVLDA--ALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF----------VPGARMYRTGDLARWL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7994 ADGNLVYLGRKDSQVKVRGQRVELGEVEHHVreclpeARQLAVevilpsgqKNHAMLAVFVQLGKGTHIAHLEEKAGGED 8073
Cdd:cd17651    384 PDGELEFLGRADDQVKIRGFRIELGEIEAAL------ARHPGV--------REAVVLAREDRPGEKRLVAYVVGDPEAPV 449
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 8074 SMAQVvfltgtEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLR 8121
Cdd:cd17651    450 DAAEL------RAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
1935-2443 2.12e-108

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 357.81  E-value: 2.12e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1935 FTEQAKARPHAPAIcAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 2013
Cdd:cd17651      1 FERQAARTPDAPAL-VAEGRrLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2014 PASRHEDIFRQTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLEQFSTlvNPVDLPAKPENAAYVMFTSGSTGTPKGVVLE 2093
Cdd:cd17651     80 PAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGAD--AEPDPALDADDLAYVIYTSGSTGRPKGVVMP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2094 HRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSSV 2171
Cdd:cd17651    158 HRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDppALAAWLDEQRISRVFLPTVA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2172 ARLLDPCLV------PSLKVLVLGGEQVNST----DWGKWPSSVQTINGYGPTECCVfCTGYTgIQGFQSG-----NIGT 2236
Cdd:cd17651    238 LRALAEHGRplgvrlAALRYLLTGGEQLVLTedlrEFCAGLPGLRLHNHYGPTETHV-VTALS-LPGDPAAwpappPIGR 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2237 SIASVS-WVVDPenHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegypgheGRQGRLYKTGDLVRYS 2315
Cdd:cd17651    316 PIDNTRvYVLDA--ALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF----------VPGARMYRTGDLARWL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2316 SDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKClPEANQLAVEVVP-PSGERdhaMLAAFIRLDDETRNSPliikyaed 2394
Cdd:cd17651    384 PDGELEFLGRADDQVKIRGFRIELGEIEAALARH-PGVREAVVLAREdRPGEK---RLVAYVVGDPEAPVDA-------- 451
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 2395 nstaqivflTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLR 2443
Cdd:cd17651    452 ---------AELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
4547-5055 3.15e-108

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 357.42  E-value: 3.15e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQARARPDTPAIcAWDGE-LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 4625
Cdd:cd17651      1 FERQAARTPDAPAL-VAEGRrLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4626 PASRHEHIFRQTGAQVVLASAQYATLWTSLGRSVVIVSEASTSQLPVVTKtaDPSVNPGNAAYAIFTSGSTGIPKGVVLE 4705
Cdd:cd17651     80 PAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEP--DPALDADDLAYVIYTSGSTGRPKGVVMP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4706 HKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRN--NLAKAINAMDVNWALLTPSV 4783
Cdd:cd17651    158 HRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDppALAAWLDEQRISRVFLPTVA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4784 ARMLDPCVV------QSLKILVLGGEQVNS----ADWDRWPKSIQTINAYGPTECSIccTTYSGKQGFKSG-----TIGT 4848
Cdd:cd17651    238 LRALAEHGRplgvrlAALRYLLTGGEQLVLtedlREFCAGLPGLRLHNHYGPTETHV--VTALSLPGDPAAwpappPIGR 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4849 SIVSVS-WVVDPenHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygghsGRQGRLYKTGDLVRYD 4927
Cdd:cd17651    316 PIDNTRvYVLDA--ALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF----------VPGARMYRTGDLARWL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4928 ADGNLVYLGRKDSQVKLRGQRVELGEVEHHVreclteAKQLAVE---VIVPEGEGGYAMLAAFVQLGDDtyntlvkekag 5004
Cdd:cd17651    384 PDGELEFLGRADDQVKIRGFRIELGEIEAAL------ARHPGVReavVLAREDRPGEKRLVAYVVGDPE----------- 446
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 5005 gdsltvQVVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLR 5055
Cdd:cd17651    447 ------APVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
4555-5054 4.74e-108

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 354.64  E-value: 4.74e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4555 PDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIF 4634
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4635 RQTGAQVVLASaqyatlwtslgrsvvivseastsqlpvvtktadpsvnPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCL 4714
Cdd:cd17652     81 ADARPALLLTT-------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4715 GHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRR--NNLAKAINAMDVNWALLTPSVARMLDPCVV 4792
Cdd:cd17652    124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLpgEPLADLLREHRITHVTLPPAALAALPPDDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4793 QSLKILVLGGEQVNSADWDRWPKSIQTINAYGPTECSICCTTYSGKQGFKSGTIGTSIVSVS-WVVDPenHNRLAPLGSI 4871
Cdd:cd17652    204 PDLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRvYVLDA--RLRPVPPGVP 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4872 GELLVEGPILARGYLNDMEKTEAAFIDDPawllegyggHSGRQGRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVEL 4951
Cdd:cd17652    282 GELYIAGAGLARGYLNRPGLTAERFVADP---------FGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4952 GEVEHHVRECltEAKQLAVeVIVPEGEGGYAMLAAFVQlgddtyntlvkeKAGGDSLTVQvvfldRVEEELAKRVPEHMM 5031
Cdd:cd17652    353 GEVEAALTEH--PGVAEAV-VVVRDDRPGDKRLVAYVV------------PAPGAAPTAA-----ELRAHLAERLPGYMV 412
                          490       500
                   ....*....|....*....|...
gi 1820002560 5032 LTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd17652    413 PAAFVVLDALPLTPNGKLDRRAL 435
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2561-2975 1.91e-107

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 352.71  E-value: 1.91e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2561 LTPIQHLYLTLDPSGRSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFQrQTGGRWQQYISEHDSSSL---IVN 2637
Cdd:cd19534      4 LTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFR-REDGGWQQRIRGDVEELFrleVVD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2638 HIHTRDTTEIVEALRQSRGSLDIERGPVLAAVLCD-AGERQSLFVAIHHLVVDLVSWRIL----LEELEDLLLGQTLPPA 2712
Cdd:cd19534     83 LSSLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILledlEAAYEQALAGEPIPLP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2713 LSTPFQAWHAAQAKYIEEHvPPSAVAQVELDPDQLSYWGVSPDDV-LSSYAISEEFVLDRKTTSTLLGSCNDAFSTRPLE 2791
Cdd:cd19534    163 SKTSFQTWAELLAEYAQSP-ALLEELAYWRELPAADYWGLPKDPEqTYGDARTVSFTLDEEETEALLQEANAAYRTEIND 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2792 LMVAALSYSFATiFSDRKPAAIFNEIHGREAWDSSIDLTRTVGWFTSMCPVQAANGAG--LLDAIRETKDCIRSFQDNGW 2869
Cdd:cd19534    242 LLLAALALAFQD-WTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEASedLGDTLKRVKEQLRRIPNKGI 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2870 SYFASQFASASAADAFASLFPMEVLFNYQGLYQQLERKDSLFKnlPMPDSCEPALAALCPRFALFDVSFVVEQGCAKVSF 2949
Cdd:cd19534    321 GYGILRYLTPEGTKRLAFHPQPEISFNYLGQFDQGERDDALFV--SAVGGGGSDIGPDTPRFALLDINAVVEGGQLVITV 398
                          410       420
                   ....*....|....*....|....*.
gi 1820002560 2950 VSDKRARHQYRIRQWIQKYKVTLIDM 2975
Cdd:cd19534    399 SYSRNMYHEETIQQLADSYKEALEAL 424
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
3475-3975 2.18e-107

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 353.21  E-value: 2.18e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVASaqysarwtssschvvtvskalssqlpavvdstntsvRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 3634
Cdd:cd17649     81 EDSGAGLLLTH------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3635 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDS--DRRNSLAKAISTMDVNWAFLTPS-------VAR 3705
Cdd:cd17649    125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPAylqqlaeEAD 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3706 LLDPGLIPSLKILAIGGEQSSSADWNRW-PGSVQKIHVYGPTECCIFCTGYTTKQGFEP----STIGTSVASVSWVVDpE 3780
Cdd:cd17649    205 RTGDGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARagasMPIGRPLGGRSAYIL-D 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3781 NHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDS 3860
Cdd:cd17649    284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPF-------GAPG--SRLYRTGDLARWRDDGVIEYLGRVDH 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3861 QVKVRGQRVELGEVEHHVREcLPEARQLAveVILPSGQKDHAmLAAFVQLEEGtqnalldkEAGGEDsmaqvvfLASVEE 3940
Cdd:cd17649    355 QVKIRGFRIELGEIEAALLE-HPGVREAA--VVALDGAGGKQ-LVAYVVLRAA--------AAQPEL-------RAQLRT 415
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1820002560 3941 ELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd17649    416 ALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
3475-3974 1.37e-106

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 350.40  E-value: 1.37e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVASaqysarwtssschvvtvskalssqlpavvdstntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 3634
Cdd:cd17652     81 ADARPALLLTT-------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3635 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRR--NSLAKAISTMDVNWAFLTPSVARLLDPGLI 3712
Cdd:cd17652    124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLpgEPLADLLREHRITHVTLPPAALAALPPDDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3713 PSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPSTIGTSVASVS-WVVDPenHNRLAPLGSM 3791
Cdd:cd17652    204 PDLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRvYVLDA--RLRPVPPGVP 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3792 GELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVEL 3871
Cdd:cd17652    282 GELYIAGAGLARGYLNRPGLTAERFVADPF-------GAPG--SRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3872 GEVEHHVREClPEARQlAVeVILPSGQKDHAMLAAFVQLEEGTQnalldkeaggedsmaqvVFLASVEEELAKRLPEHMV 3951
Cdd:cd17652    353 GEVEAALTEH-PGVAE-AV-VVVRDDRPGDKRLVAYVVPAPGAA-----------------PTAAELRAHLAERLPGYMV 412
                          490       500
                   ....*....|....*....|...
gi 1820002560 3952 PTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd17652    413 PAAFVVLDALPLTPNGKLDRRAL 435
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
5636-6136 5.09e-105

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 346.66  E-value: 5.09e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5636 PHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTF 5715
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5716 RHTGAQVVVTsaQHsarwigtnhqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCW 5795
Cdd:cd17649     81 EDSGAGLLLT--HH----------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5796 GRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDS--DRRNDLVKAISTMDVSCALLTPS-------VAR 5866
Cdd:cd17649    125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPAylqqlaeEAD 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5867 LLEPSSVPTLQMLVLQGEQVSFADWNRW-PASVQTINGYGPTECSICCNTYSGKQGFKSGI----IGTSVASVSWVVDpE 5941
Cdd:cd17649    205 RTGDGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGasmpIGRPLGGRSAYIL-D 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5942 NHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypGHPGrqGRLYKTGDLVRYDANGNLVCLGRKDS 6021
Cdd:cd17649    284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPF-------GAPG--SRLYRTGDLARWRDDGVIEYLGRVDH 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6022 QVKLRGQRVELGEVEHHVREcLPEARQLAveVILPSGQKDHAmLAAFVQLEEGTQNALLDkeasgedsmaqvvflASVEE 6101
Cdd:cd17649    355 QVKIRGFRIELGEIEAALLE-HPGVREAA--VVALDGAGGKQ-LVAYVVLRAAAAQPELR---------------AQLRT 415
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1820002560 6102 ELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:cd17649    416 ALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
7209-8216 7.51e-105

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 370.91  E-value: 7.51e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7209 LELRADVDEDVFCAAWEHVVQSTAALRTRIVQhSELGLLQVV-------VEEKIQWTES----EALEEYLKED--KAVSM 7275
Cdd:PRK10252    36 VELTGELDAPLLARAVVAGLAEADTLRMRFTE-DNGEVWQWVdpaltfpLPEIIDLRTQpdphAAAQALMQADlqQDLRV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7276 GLGDPLAHYALVKeaWGGKRWFvW--TIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAFI----------QYLGQQ 7343
Cdd:PRK10252   115 DSGKPLVFHQLIQ--LGDNRWY-WyqRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPASPFTpfadvveeyqRYRASE 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7344 DLEATAAYWQTALSDceavlfppLPSTVTQPVADTTVEYQCPPLSKATLDTTTSTLIRAAwAIVTSCYTSsdDVV----- 7418
Cdd:PRK10252   192 AWQRDAAFWAEQRRQ--------LPPPASLSPAPLPGRSASADILRLKLEFTDGAFRQLA-AQASGVQRP--DLAlalva 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7419 -YGTTVTGRNAPIAGVEAM----------VGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAH-----EQtgLQHIA 7482
Cdd:PRK10252   261 lWLGRLCGRMDYAAGFIFMrrlgsaaltaTGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHqrydaEQ--IVRDS 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7483 KLGSGPRHACGfqTLLVVQPVDDVLGSDDMLG--EWRSYSKMQDFT-TYALMVQFTLAAEGVQITASFD-ARVIEHwvle 7558
Cdd:PRK10252   339 GRAAGDEPLFG--PVLNIKVFDYQLDFPGVQAqtHTLATGPVNDLElALFPDEHGGLSIEILANPQRYDeATLIAH---- 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7559 kMLRQFSFIMQqlAEASEDSKVADIDTTTPEDRQQLWAWNADVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGEL 7638
Cdd:PRK10252   413 -AERLKALIAQ--FAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREM 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7639 DVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARW 7718
Cdd:PRK10252   490 REQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRF 569
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7719 TssscHVVTVSKALSSQLPAVVDSTNTSV-RPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQF 7797
Cdd:PRK10252   570 A----DVPDLTSLCYNAPLAPQGAAPLQLsQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQK 645
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7798 ASYTFDACIAEIITTLLCGGCICV-PSDSDRR-NSLAKAISTMDVNWAFLTPS-----VARLLDPGLIPSLKILA---IG 7867
Cdd:PRK10252   646 TPCSFDVSVWEFFWPFIAGAKLVMaEPEAHRDpLAMQQFFAEYGVTTTHFVPSmlaafVASLTPEGARQSCASLRqvfCS 725
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7868 GEQSSSADWNRWPGSVQ-KIH-VYGPTECCIFCTGYTTKQGFEPSTIGTSVaSVSW--------VVDpeNHNRLAPLGSM 7937
Cdd:PRK10252   726 GEALPADLCREWQQLTGaPLHnLYGPTEAAVDVSWYPAFGEELAAVRGSSV-PIGYpvwntglrILD--ARMRPVPPGVA 802
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7938 GELLMEGPILARGYLNDVDKTEAAFIDDPAwllegYPGhpgrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVEL 8017
Cdd:PRK10252   803 GDLYLTGIQLAQGYLGRPDLTASRFIADPF-----APG-----ERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIEL 872
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8018 GEVEHHVREcLPEARQ-LAVEVILPSGQKNHA---MLAVFVQLGKGTHIAhleekaggedsmaqvvfLTGTEEELAKRLP 8093
Cdd:PRK10252   873 GEIDRAMQA-LPDVEQaVTHACVINQAAATGGdarQLVGYLVSQSGLPLD-----------------TSALQAQLRERLP 934
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8094 KHMVPTVFFALLHFPMTTSGKADRKrlreigasftaqQLAETQTSSQGPKRQPLTEAEQTMQQLWARVLGIDADiiGLDD 8173
Cdd:PRK10252   935 PHMVPVVLLQLDQLPLSANGKLDRK------------ALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVV--DADA 1000
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 8174 SFFRLGGDSIAAMKLVGEARRT-GLQLSVADIFRHPRLIDLASL 8216
Cdd:PRK10252  1001 DFFALGGHSLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLATL 1044
PRK05691 PRK05691
peptide synthase; Validated
6842-8511 7.53e-105

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 381.44  E-value: 7.53e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNdpawlveghgkHPGRRgrLYKTGDLVYYnKDGNLVYIGR 6921
Cdd:PRK05691   384 VDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE-----------HDGRT--WLRTGDLGFL-RDGELFVTGR 449
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 KDGQVKVRGQRVELGEIENRLRECmpratqmaVEVISpagaaeqaKTMVVAFlQLNDEARDALlggNVPNDDNLSAQVVF 7001
Cdd:PRK05691   450 LKDMLIVRGHNLYPQDIEKTVERE--------VEVVR--------KGRVAAF-AVNHQGEEGI---GIAAEISRSVQKIL 509
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7002 PAkvdEKLSNLLpSYMMPEVYFAVPQ---------LPMMISGKTDRK--RLR-EIG-----ASFTAQQLAEMRTSSQGPk 7064
Cdd:PRK05691   510 PP---QALIKSI-RQAVAEACQEAPSvvlllnpgaLPKTSSGKLQRSacRLRlADGsldsyALFPALQAVEAAQTAASG- 584
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7065 rqpsTEAERTMQQLWARMLKVKadSIGLDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADVFRHPRLVDLayvqnsqcs 7143
Cdd:PRK05691   585 ----DELQARIAAIWCEQLKVE--QVAADDHFFLLGGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAAF--------- 649
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7144 SAAEEVpafsllgedvnpvQLSQDAAAMCSVAASIVKDIYPCSPLQEGLISL--TAKRAGDYIMQSVLELRADVDEDVFC 7221
Cdd:PRK05691   650 SAAVAR-------------QLAGGGAAQAAIARLPRGQALPQSLAQNRLWLLwqLDPQSAAYNIPGGLHLRGELDEAALR 716
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7222 AAWEHVVQSTAALRTRIVQHSELGLLQVVVEEKIQW----------TESEALEEYLKEDKA---VSMGLGdPLAHYALVK 7288
Cdd:PRK05691   717 ASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALqridlsdlpeAEREARAAQIREEEArqpFDLEKG-PLLRVTLVR 795
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7289 EAWGGKRWFVwTIHHALYDGGSLPLILHAVKQVYSGAV----LERQP---SFNAFI----QYLGQQDLEATAAYWQTALS 7357
Cdd:PRK05691   796 LDDEEHQLLV-TLHHIVADGWSLNILLDEFSRLYAAACqgqtAELAPlplGYADYGawqrQWLAQGEAARQLAYWKAQLG 874
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7358 DCEAVLFPPLPSTVTQPVADTTVEYQC---PPLSKA------TLDTTTSTLIRAAWAIVTSCYTSSDDVVYGttVTGRNA 7428
Cdd:PRK05691   875 DEQPVLELATDHPRSARQAHSAARYSLrvdASLSEAlrglaqAHQATLFMVLLAAFQALLHRYSGQGDIRIG--VPNANR 952
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7429 PIAGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIAKLGSGPRHACGFQTLLVVQPVDdvLG 7508
Cdd:PRK05691   953 PRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQGLFQVMFNHQQRD--LS 1030
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7509 S----DDMLGE---WRSYSKMQDfttyaLMVQFTLAAEGvQITASFD--ARVIEHWVLEKMLRQFSFIMQQLAEASEDSk 7579
Cdd:PRK05691  1031 AlrrlPGLLAEelpWHSREAKFD-----LQLHSEEDRNG-RLTLSFDyaAELFDAATIERLAEHFLALLEQVCEDPQRA- 1103
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7580 VADIDTTTPEDRQQLWAWNADVPPAIERCVHDLFAEQARARPGAPAIcAWDGE-LTYGELDVLSSNLAGHLVQLGVNPED 7658
Cdd:PRK05691  1104 LGDVQLLDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIAL-VWDGGsLDYAELHAQANRLAHYLRDKGVGPDV 1182
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7659 VVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSKALS----- 7733
Cdd:PRK05691  1183 CVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHldswp 1262
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7734 SQLPAVvdstntSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTL 7813
Cdd:PRK05691  1263 SQAPGL------HLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPL 1336
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7814 LCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL----DPGLIPSLKILAIGGEQSSSADWNR----WPGsV 7883
Cdd:PRK05691  1337 ITGCRLVLAGPGEHRDpqRIAELVQQYGVTTLHFVPPLLQLFidepLAAACTSLRRLFSGGEALPAELRNRvlqrLPQ-V 1415
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7884 QKIHVYGPTECCIFCTGY-TTKQGFEPSTIGTSVASV-SWVVDPENHnrLAPLGSMGELLMEGPILARGYLNDVDKTEAA 7961
Cdd:PRK05691  1416 QLHNRYGPTETAINVTHWqCQAEDGERSPIGRPLGNVlCRVLDAELN--LLPPGVAGELCIGGAGLARGYLGRPALTAER 1493
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7962 FIDDPAwllegypGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVEVilp 8041
Cdd:PRK05691  1494 FVPDPL-------GEDG--ARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA-QPGVAQAAVLV--- 1560
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8042 sgqknhAMLAVFVQLgkgthIAHLEEKAGGEDSMAQVvfltgtEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLR 8121
Cdd:PRK05691  1561 ------REGAAGAQL-----VGYYTGEAGQEAEAERL------KAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALP 1623
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8122 EIGAsftaqqlaetqtsSQGPKRQPLTEAEQTMQQLWARVLGIDAdiIGLDDSFFRLGGDSIAAMKLVGEAR-RTGLQLS 8200
Cdd:PRK05691  1624 EPVW-------------QQREHVEPRTELQQQIAAIWREVLGLPR--VGLRDDFFALGGHSLLATQIVSRTRqACDVELP 1688
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8201 VADIFRHPRLidlaslkSTFCNSV--VEEVPAFSLLSPVMKdamfsvtepfgpslriDDITDVVPASYIQQ---FYIATG 8275
Cdd:PRK05691  1689 LRALFEASEL-------GAFAEQVarIQAAGERNSQGAIAR----------------VDRSQPVPLSYSQQrmwFLWQME 1745
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8276 VRAPreAFNY-PFIDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIPRHQDL-----PFSIFEVNG------ 8343
Cdd:PRK05691  1746 PDSP--AYNVgGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLrmdwqDFSALPADArqqrlq 1823
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8344 ALAeESQAIHIRDLdQTSPLglpTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQ---------EPLLSt 8414
Cdd:PRK05691  1824 QLA-DSEAHQPFDL-ERGPL---LRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAflddresplEPLPV- 1897
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8415 tgfhSYLAYVHNQR--------SASINYWSRLLKGSHITNITSKLRPKlgkdTTIRSVKVE--RVIRTPQLPT------- 8477
Cdd:PRK05691  1898 ----QYLDYSVWQRqwlesgerQRQLDYWKAQLGNEHPLLELPADRPR----PPVQSHRGElyRFDLSPELAArvrafna 1969
                         1770      1780      1790
                   ....*....|....*....|....*....|....*.
gi 1820002560 8478 --GLTMASLVSSAWAVVLSHISGEEDVVYGLVVAGR 8511
Cdd:PRK05691  1970 qrGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANR 2005
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
5628-6136 8.20e-105

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 347.41  E-value: 8.20e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5628 FTEQAKARPHAPAIcAWDGE-LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 5706
Cdd:cd17651      1 FERQAARTPDAPAL-VAEGRrLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5707 PASRHEDTFRHTGAQVVVTSAQHSARWIGTNHQVVTVSAgsLGQLSTLVNPVGLPAIPENAVYIMFTSGSTGIPKGVVLE 5786
Cdd:cd17651     80 PAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQ--PGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5787 HRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRND--LVKAISTMDVSCALLTPSV 5864
Cdd:cd17651    158 HRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPpaLAAWLDEQRISRVFLPTVA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5865 ARLLEPSSV------PTLQMLVLQGEQVSF----ADWNRWPASVQTINGYGPTECSICcnTYSGKQGFKSG-----IIGT 5929
Cdd:cd17651    238 LRALAEHGRplgvrlAALRYLLTGGEQLVLtedlREFCAGLPGLRLHNHYGPTETHVV--TALSLPGDPAAwpappPIGR 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5930 SVASVS-WVVDPenHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypghpGRQGRLYKTGDLVRYD 6008
Cdd:cd17651    316 PIDNTRvYVLDA--ALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF----------VPGARMYRTGDLARWL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6009 ANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKDhAMLAAFVQLEEGtqnalldkeasged 6088
Cdd:cd17651    384 PDGELEFLGRADDQVKIRGFRIELGEIEAALARH-PGVREAVV-LAREDRPGE-KRLVAYVVGDPE-------------- 446
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 6089 smaQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:cd17651    447 ---APVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
3464-3974 1.07e-104

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 346.96  E-value: 1.07e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3464 HDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 3543
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3544 DHPASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSKALSSQ---LPAVVdstntsVRPENAAYIIFTSGSTGVPK 3620
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPpatPPLVP------PRPDNLAYVIYTSGSTGRPK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3621 GVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNS--LAKAISTMDVNWAF 3698
Cdd:cd17646    155 GVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPayLAALIREHGVTTCH 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3699 LTPSVARLL----DPGLIPSLKILAIGGEQ---SSSADWNRWPGsVQKIHVYGPTECCIFCTGYTTKQGFEPST--IGTS 3769
Cdd:cd17646    235 FVPSMLRVFlaepAAGSCASLRRVFCSGEAlppELAARFLALPG-AELHNLYGPTEAAIDVTHWPVRGPAETPSvpIGRP 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3770 VASVS-WVVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllegyPGHPGrqGRLYKTGDLVQYNA 3848
Cdd:cd17646    314 VPNTRlYVLDD--ALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPD--------PFGPG--SRMYRTGDLARWRP 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3849 DGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAveVILPSGQKDHAMLAAFVQLEEGtqnalldkEAGGEDs 3928
Cdd:cd17646    382 DGALEFLGRSDDQVKIRGFRVEPGEIEAALAAH-PAVTHAV--VVARAAPAGAARLVGYVVPAAG--------AAGPDT- 449
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 3929 maqvvflASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd17646    450 -------AALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
6282-7405 3.90e-104

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 369.57  E-value: 3.90e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6282 PLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEEKIQWTE------- 6354
Cdd:COG1020     28 WLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLvdleala 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6355 ----SKRLEEYLREDKAVSMGLGDPLARYAIIKEAWGGKRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSFNA 6430
Cdd:COG1020    108 eaaaEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPIQ 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6431 FIQY-------LSQQDLEATAAYWQTALADCEATLFPP-------------------LPSSVKQLVADTTVEHQCPLPSr 6484
Cdd:COG1020    188 YADYalwqrewLQGEELARQLAYWRQQLAGLPPLLELPtdrprpavqsyrgarvsfrLPAELTAALRALARRHGVTLFM- 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6485 stsdtttstLIRAAWAIVASRYTSSDDVVFGTTITGRNAPvtSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATE 6564
Cdd:COG1020    267 ---------VLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLA 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6565 MIAYEQTGLQQI-AKMGP--DPQHACGFQTLLVVQ--PAGDVLGSDDTLGKWRGYSGLQDFmtyALGVRCTLSAEGVKIT 6639
Cdd:COG1020    336 AYAHQDLPFERLvEELQPerDLSRNPLFQVMFVLQnaPADELELPGLTLEPLELDSGTAKF---DLTLTVVETGDGLRLT 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6640 ASFDARVIEHWVVEKMLGQFSFAMQQLAeASADRKVADIDITTTTDRQQLWA-WNA-ELPLAVDRCVHDLFTEQALARPN 6717
Cdd:COG1020    413 LEYNTDLFDAATIERMAGHLVTLLEALA-ADPDQPLGDLPLLTAAERQQLLAeWNAtAAPYPADATLHELFEAQAARTPD 491
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6718 APAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDILRQ 6797
Cdd:COG1020    492 AVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLED 571
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6798 TGAQVILASAQNTTLFQSSNQTVVTVNRSSYILFPDEN----------------------------------------RE 6837
Cdd:COG1020    572 AGARLVLTQSALAARLPELGVPVLALDALALAAEPATNppvpvtpddlayviytsgstgrpkgvmvehralvnllawmQR 651
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6838 AYPF-------------------------------------VRPSNAALA------------------------------ 6850
Cdd:COG1020    652 RYGLgpgdrvlqfaslsfdasvweifgallsgatlvlappeARRDPAALAellarhrvtvlnltpsllralldaapealp 731
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 ------------------------------------------------------------------------------PL 6852
Cdd:COG1020    732 slrlvlvggealppelvrrwrarlpgarlvnlygptettvdstyyevtppdadggsvpigrpiantrvyvldahlqpvPV 811
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6853 GSIGELLVEGPILARGYLNDADKTAAAFVNDPAwlveghgKHPGrrGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQR 6932
Cdd:COG1020    812 GVPGELYIGGAGLARGYLNRPELTAERFVADPF-------GFPG--ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFR 882
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6933 VELGEIENRLRECmPRATQMAVEVISPAGAAEQaktmVVAFLQLNDEARDAllggnvpnddnlsaqvvfPAKVDEKLSNL 7012
Cdd:COG1020    883 IELGEIEAALLQH-PGVREAVVVAREDAPGDKR----LVAYVVPEAGAAAA------------------AALLRLALALL 939
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7013 LPSYMMPEVYFAVPQLPMMISGKTDRKRlreigasftaqqLAEMRTSSQGPKRQPSTEAERTMQQLWARMLKVkaDSIGL 7092
Cdd:COG1020    940 LPPYMVPAAVVLLLPLPLTGNGKLDRLA------------LPAPAAAAAAAAAAPPAEEEEEEAALALLLLLV--VVVGD 1005
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7093 DDSFFRLGGDSIVAMKLVGEARRTGLQLSVADVFRHPRLVDLAYVQNSQCSSAAEEVPAFSLLGEDVNPVQLSQDAAAmc 7172
Cdd:COG1020   1006 DDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALL-- 1083
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7173 SVAASIVKDIYPCSPLQEGLISLTAKRAGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVVVE 7252
Cdd:COG1020   1084 LALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAA 1163
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7253 EKIQWTESEALEEYLKEDKAVSMGLGDPLAHYALVKEAWggkRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPS 7332
Cdd:COG1020   1164 AAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLL---LLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLAL 1240
                         1290      1300      1310      1320      1330      1340      1350
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 7333 FNAFIQYLGQQDLEATAAYWQTALSDCEAVLFPPLPSTVTQPVADTTVEYQCPPLSKATLDTTTSTLIRAAWA 7405
Cdd:COG1020   1241 LALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALAL 1313
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
3475-3974 7.93e-104

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 343.89  E-value: 7.93e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVASAQYSARWTssscHVVTVSKALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 3634
Cdd:cd12116     81 EDAEPALVLTDDALPDRLP----AGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3635 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL---DP 3709
Cdd:cd12116    157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDpeALARLIEAHSITVMQATPATWRMLldaGW 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3710 GLIPSLKILAiGGE------------QSSSAdWNrwpgsvqkihVYGPTECCIFCTGYTTKQGFEPSTIGTSVASVS-WV 3776
Cdd:cd12116    237 QGRAGLTALC-GGEalppdlaarllsRVGSL-WN----------LYGPTETTIWSTAARVTAAAGPIPIGRPLANTQvYV 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3777 VDPEnhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNADGNLVYLG 3856
Cdd:cd12116    305 LDAA--LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPF-------AGPG--SRLYRTGDLVRRRADGRLEYLG 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3857 RKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHamLAAFVQLEEGtqnALLDKEAggedsmaqvvfla 3936
Cdd:cd12116    374 RADGQVKIRGHRIELGEIEAALAA-HPGVAQAAV-VVREDGGDRR--LVAYVVLKAG---AAPDAAA------------- 433
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 3937 sVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd12116    434 -LRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
7621-8120 1.35e-103

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 341.93  E-value: 1.35e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7621 PGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 7700
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7701 EQTGAQVVVASaqysarwtssschvvtvskalssqlpavvdstntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 7780
Cdd:cd17652     81 ADARPALLLTT-------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7781 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRR--NSLAKAISTMDVNWAFLTPSVARLLDPGLI 7858
Cdd:cd17652    124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLpgEPLADLLREHRITHVTLPPAALAALPPDDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7859 PSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPSTIGTSVASVS-WVVDPenHNRLAPLGSM 7937
Cdd:cd17652    204 PDLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRvYVLDA--RLRPVPPGVP 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7938 GELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVEL 8017
Cdd:cd17652    282 GELYIAGAGLARGYLNRPGLTAERFVADPF-------GAPG--SRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8018 GEVEHHVREClPEARQlAVeVILPSGQKNHAMLAVFVQLGKGTHIAHLEEKaggedsmaqvvfltgteEELAKRLPKHMV 8097
Cdd:cd17652    353 GEVEAALTEH-PGVAE-AV-VVVRDDRPGDKRLVAYVVPAPGAAPTAAELR-----------------AHLAERLPGYMV 412
                          490       500
                   ....*....|....*....|...
gi 1820002560 8098 PTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd17652    413 PAAFVVLDALPLTPNGKLDRRAL 435
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
1932-2442 2.39e-103

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 343.10  E-value: 2.39e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1932 HDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 2011
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2012 DHPASRHEDIFRQTGAQVVVTSAQhSARWIGTNHQVVTVSAGSLEQFSTLVNPVdlPAKPENAAYVMFTSGSTGTPKGVV 2091
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTAD-LAARLPAGGDVALLGDEALAAPPATPPLV--PPRPDNLAYVIYTSGSTGRPKGVM 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2092 LEHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTS 2169
Cdd:cd17646    158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDpaYLAALIREHGVTTCHFVP 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2170 SVARLL----DPCLVPSLKVLVLGGEQVNS---TDWGKWPsSVQTINGYGPTECCVFCTG--YTGIQGFQSGNIGTSIAS 2240
Cdd:cd17646    238 SMLRVFlaepAAGSCASLRRVFCSGEALPPelaARFLALP-GAELHNLYGPTEAAIDVTHwpVRGPAETPSVPIGRPVPN 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2241 VS-WVVDPenHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPawlleGYPGhegrqGRLYKTGDLVRYSSDGN 2319
Cdd:cd17646    317 TRlYVLDD--ALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDP-----FGPG-----SRMYRTGDLARWRPDGA 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2320 LVCLGRKDSQVKVRGQRVELGEVEHHMRKClPEANQLAveVVPPSGERDHAMLAAFIRLDDEtrnspliikyAEDNSTAQ 2399
Cdd:cd17646    385 LEFLGRSDDQVKIRGFRVEPGEIEAALAAH-PAVTHAV--VVARAAPAGAARLVGYVVPAAG----------AAGPDTAA 451
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 2400 ivfltgIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd17646    452 ------LRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
PRK12467 PRK12467
peptide synthase; Provisional
6257-7145 3.96e-103

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 375.65  E-value: 3.96e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6257 AQVSQDAAAMCSVDASSVEDMYPCSPLQEGLM--SLTAKRAGDYIMQsvleLRVDV---DEDAFRAAWEHVVQLTAALRT 6331
Cdd:PRK12467  2626 AGLSQEQLDRLPVAVGDIEDIYPLSPMQQGMLfhTLYEGGAGDYINQ----MRVDVeglDVERFRTAWQAVIDRHEILRS 2701
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6332 RIVQHSELGL-LQVVVEE------KIQWTESKRLEEYLRE----DKAVSMGLGD-PLARYAIIKEawGGKRW-FVWTIHH 6398
Cdd:PRK12467  2702 GFLWDGELEEpLQVVYKQarlpfsRLDWRDRADLEQALDAlaaaDRQQGFDLLSaPLLRLTLVRT--GEDRHhLIYTNHH 2779
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6399 ALYDGWSLPRVLQAVKQAYNGAVLETQPS-FNAFIQYLSQQDLEATAAYWQTALADCE-----ATLFPPLPS------SV 6466
Cdd:PRK12467  2780 ILMDGWSGSQLLGEVLQRYFGQPPPAREGrYRDYIAWLQAQDAEASEAFWKEQLAALEeptrlARALYPAPAeavaghGA 2859
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6467 KQLVADTTVEHQCpLPSRSTSDTTTSTLIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTSIDAIVGPTIATVPLRVRLQ 6546
Cdd:PRK12467  2860 HYLHLDATQTRQL-IEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPR 2938
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6547 KDQTVSSFLGYLQQQATEMIAYEQTGLQQIAKMGPDPQHACgFQTLLVVQ--PAGDVLG----SDDTLGKWRGYSGLQDF 6620
Cdd:PRK12467  2939 AEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEAL-FDSILVFEnyPISEALKqgapSGLRFGAVSSREQTNYP 3017
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6621 MTYALGVRCTLSAEGVKITASFDARVIEhwvveKMLGQFSFAMQQLAEASADRkVADIDITTTTDRQQLW-AWNA-ELPL 6698
Cdd:PRK12467  3018 LTLAVGLGDTLELEFSYDRQHFDAAAIE-----RLAESFDRLLQAMLNNPAAR-LGELPTLAAHERRQVLhAWNAtAAAY 3091
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6699 AVDRCVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGA 6778
Cdd:PRK12467  3092 PSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGA 3171
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6779 FVPLDPDHPASRHEDILRQTGAQVILASAQ-NTTLFQSSNQTVVTVNRSSYILFPDEN---------------------- 6835
Cdd:PRK12467  3172 YVPLDPEYPRERLAYMIEDSGVKLLLTQAHlLEQLPAPAGDTALTLDRLDLNGYSENNpstrvmgenlayviytsgstgk 3251
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6836 ------------------REAY---------------------------------------------------------- 6839
Cdd:PRK12467  3252 pkgvgvrhgalanhlcwiAEAYeldandrvllfmsfsfdgaqerflwtlicggclvvrdndlwdpeelwqaihahrisia 3331
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6840 ------------------------------------------------------------------------------PF 6841
Cdd:PRK12467  3332 cfppaylqqfaedaggadcasldiyvfggeavppaafeqvkrklkprgltngygpteavvtvtlwkcggdavceapyaPI 3411
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRP----------SNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPawlVEGHGkhpgrrGRLYKTGDLVYYN 6911
Cdd:PRK12467  3412 GRPvagrsiyvldGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP---FSGSG------GRLYRTGDLARYR 3482
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6912 KDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAGAaeqakTMVVAFLQLNDEARDALlggnvpn 6991
Cdd:PRK12467  3483 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQ-HPSVREAVVLARDGAGG-----KQLVAYVVPADPQGDWR------- 3549
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6992 ddnlsaqvvfpAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREIGASFTAQQLAemrtssqgpkrqPSTEA 7071
Cdd:PRK12467  3550 -----------ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA------------PRSEV 3606
                         1050      1060      1070      1080      1090      1100      1110
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 7072 ERTMQQLWARMLKVkaDSIGLDDSFFRLGGDSIVAMKLVGEARR-TGLQLSVADVFRHPRLVDLA-YVQNSQCSSA 7145
Cdd:PRK12467  3607 EQQLAAIWADVLGV--EQVGVTDNFFELGGDSLLALQVLSRIRQsLGLKLSLRDLMSAPTIAELAgYSPLGDVPVN 3680
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
4555-5055 5.34e-103

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 340.88  E-value: 5.34e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4555 PDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIF 4634
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4635 RQTGAQVVLASAqyatlwtslgrsvvivseastsqlpvvtktadpsvnPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCL 4714
Cdd:cd17649     81 EDSGAGLLLTHH------------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4715 GHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDS--DRRNNLAKAINAMDVNWALLTPS-------VAR 4785
Cdd:cd17649    125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPAylqqlaeEAD 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4786 MLDPCVVQSLKILVLGGEQVNSADWDRW-PKSIQTINAYGPTECSICCTTYSGKQGFKSG----TIGTSIVSVSWVVDpE 4860
Cdd:cd17649    205 RTGDGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARAgasmPIGRPLGGRSAYIL-D 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4861 NHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawllegyggHSGRQGRLYKTGDLVRYDADGNLVYLGRKDS 4940
Cdd:cd17649    284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDP---------FGAPGSRLYRTGDLARWRDDGVIEYLGRVDH 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4941 QVKLRGQRVELGEVEhhvrECLTEAKQLAVEVIVPEGEGGYAMLAAFVQLGDDTYNTLVKEkaggdsltvqvvfldRVEE 5020
Cdd:cd17649    355 QVKIRGFRIELGEIE----AALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRA---------------QLRT 415
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1820002560 5021 ELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLR 5055
Cdd:cd17649    416 ALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
5636-6135 5.49e-103

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 340.00  E-value: 5.49e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5636 PHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTF 5715
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5716 RHTGAQVVVTSaqhsarwigtnhqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCW 5795
Cdd:cd17652     81 ADARPALLLTT-------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5796 GRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRR--NDLVKAISTMDVSCALLTPSVARLLEPSSV 5873
Cdd:cd17652    124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLpgEPLADLLREHRITHVTLPPAALAALPPDDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5874 PTLQMLVLQGEQVSFADWNRWPASVQTINGYGPTECSICCnTYSGKQGFKSGI-IGTSVASVS-WVVDPenHDRLAPLGS 5951
Cdd:cd17652    204 PDLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCA-TMAGPLPGGGVPpIGRPVPGTRvYVLDA--RLRPVPPGV 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5952 IGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypGHPGrqGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVE 6031
Cdd:cd17652    281 PGELYIAGAGLARGYLNRPGLTAERFVADPF-------GAPG--SRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIE 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6032 LGEVEHHVREClPEARQlAVeVILPSGQKDHAMLAAFVQLEEGTQnalldkeasgedsmaqvVFLASVEEELAKRLPEHM 6111
Cdd:cd17652    352 LGEVEAALTEH-PGVAE-AV-VVVRDDRPGDKRLVAYVVPAPGAA-----------------PTAAELRAHLAERLPGYM 411
                          490       500
                   ....*....|....*....|....
gi 1820002560 6112 VPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd17652    412 VPAAFVVLDALPLTPNGKLDRRAL 435
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
7621-8121 5.55e-103

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 340.50  E-value: 5.55e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7621 PGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 7700
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7701 EQTGAQVVVASaqysarwtssschvvtvskalssqlpavvdstntsvRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 7780
Cdd:cd17649     81 EDSGAGLLLTH------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7781 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDS--DRRNSLAKAISTMDVNWAFLTPS-------VAR 7851
Cdd:cd17649    125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPAylqqlaeEAD 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7852 LLDPGLIPSLKILAIGGEQSSSADWNRW-PGSVQKIHVYGPTECCIFCTGYTTKQGFEP----STIGTSVASVSWVVDpE 7926
Cdd:cd17649    205 RTGDGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARagasMPIGRPLGGRSAYIL-D 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7927 NHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNADGNLVYLGRKDS 8006
Cdd:cd17649    284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPF-------GAPG--SRLYRTGDLARWRDDGVIEYLGRVDH 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8007 QVKVRGQRVELGEVEHHVREcLPEARQLAveVILPSGQKNHAMLAVFVqlgkgthiahleekagGEDSMAQVVFLTGTEE 8086
Cdd:cd17649    355 QVKIRGFRIELGEIEAALLE-HPGVREAA--VVALDGAGGKQLVAYVV----------------LRAAAAQPELRAQLRT 415
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1820002560 8087 ELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLR 8121
Cdd:cd17649    416 ALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
866-1365 7.83e-103

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 339.61  E-value: 7.83e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  866 PDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIF 945
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  946 KQIGAQVVLTSsqhamlfasserhqvtvskvstsqlptvvnfakspvdPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCL 1025
Cdd:cd17652     81 ADARPALLLTT-------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1026 GHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRR--NNLAKAISTMDVNCALLTPSVARLLEPSAV 1103
Cdd:cd17652    124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLpgEPLADLLREHRITHVTLPPAALAALPPDDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1104 PSLKRLVLQGEQVSFADWNRWPGSVQTINGYGPTECSVCCnTYSGKQGFKSGI-IGTSVASLS-WVVDAgnHNRLAPLGS 1181
Cdd:cd17652    204 PDLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCA-TMAGPLPGGGVPpIGRPVPGTRvYVLDA--RLRPVPPGV 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1182 IGELLVEGPILARGYLNDIDKTEAAFIDDPawllegyegHAGRRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVE 1261
Cdd:cd17652    281 PGELYIAGAGLARGYLNRPGLTAERFVADP---------FGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIE 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1262 LGEIEHHVREClPEARQlAVeVILPSGQKEHALLAAFiqldkgnhnalfeekASGEDSMAQVVflTGVEEELAKRLPEHM 1341
Cdd:cd17652    352 LGEVEAALTEH-PGVAE-AV-VVVRDDRPGDKRLVAY---------------VVPAPGAAPTA--AELRAHLAERLPGYM 411
                          490       500
                   ....*....|....*....|....
gi 1820002560 1342 VPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17652    412 VPAAFVVLDALPLTPNGKLDRRAL 435
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
7610-8120 4.13e-102

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 339.64  E-value: 4.13e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7610 HDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 7689
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7690 DHPASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSKALSSQ---LPAVVdstntsVRPENAAYIIFTSGSTGVPK 7766
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPpatPPLVP------PRPDNLAYVIYTSGSTGRPK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7767 GVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNS--LAKAISTMDVNWAF 7844
Cdd:cd17646    155 GVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPayLAALIREHGVTTCH 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7845 LTPSVARLL----DPGLIPSLKILAIGGEQ---SSSADWNRWPGsVQKIHVYGPTECCIFCTGYTTKQGFEPST--IGTS 7915
Cdd:cd17646    235 FVPSMLRVFlaepAAGSCASLRRVFCSGEAlppELAARFLALPG-AELHNLYGPTEAAIDVTHWPVRGPAETPSvpIGRP 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7916 VASVS-WVVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllegyPGHPGrqGRLYKTGDLVQYNA 7994
Cdd:cd17646    314 VPNTRlYVLDD--ALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPD--------PFGPG--SRMYRTGDLARWRP 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7995 DGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVEVilpsgQKNHAMLAVFVqlgkgthiAHLEEKAGGEDS 8074
Cdd:cd17646    382 DGALEFLGRSDDQVKIRGFRVEPGEIEAALAAH-PAVTHAVVVA-----RAAPAGAARLV--------GYVVPAAGAAGP 447
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 8075 MAQVVfltgtEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd17646    448 DTAAL-----RAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
7621-8120 5.48e-102

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 338.50  E-value: 5.48e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7621 PGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 7700
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7701 EQTGAQVVVASAQYSARWTssscHVVTVSKALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 7780
Cdd:cd12116     81 EDAEPALVLTDDALPDRLP----AGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7781 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL---DP 7855
Cdd:cd12116    157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDpeALARLIEAHSITVMQATPATWRMLldaGW 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7856 GLIPSLKILAiGGE------------QSSSAdWNrwpgsvqkihVYGPTECCIFCTGYTTKQGFEPSTIGTSVASVS-WV 7922
Cdd:cd12116    237 QGRAGLTALC-GGEalppdlaarllsRVGSL-WN----------LYGPTETTIWSTAARVTAAAGPIPIGRPLANTQvYV 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7923 VDPEnhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGrqGRLYKTGDLVQYNADGNLVYLG 8002
Cdd:cd12116    305 LDAA--LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPF-------AGPG--SRLYRTGDLVRRRADGRLEYLG 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8003 RKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVEVilpSGQKNHAMLAVFVQLGKGTHIAHLEEKAGgedsmaqvvflt 8082
Cdd:cd12116    374 RADGQVKIRGHRIELGEIEAALAA-HPGVAQAAVVV---REDGGDRRLVAYVVLKAGAAPDAAALRAH------------ 437
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 8083 gteeeLAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd12116    438 -----LRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
4555-5054 1.04e-101

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 337.73  E-value: 1.04e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4555 PDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIF 4634
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4635 RQTGAQVVLASAQYATLWTSLGRSVVIVSEASTSQLPVvtktADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCL 4714
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAA----PRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4715 GHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRN--NLAKAINAMDVNWALLTPSVARML---DP 4789
Cdd:cd12116    157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDpeALARLIEAHSITVMQATPATWRMLldaGW 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4790 CVVQSLKILVlGGEQVNSADWDRW-PKSIQTINAYGPTECSICCTTYSGKQGFKSGTIGTSIVSVS-WVVDPEnhNRLAP 4867
Cdd:cd12116    237 QGRAGLTALC-GGEALPPDLAARLlSRVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQvYVLDAA--LRPVP 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4868 LGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygGHSGrqGRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQ 4947
Cdd:cd12116    314 PGVPGELYIGGDGVAQGYLGRPALTAERFVPDPF-------AGPG--SRLYRTGDLVRRRADGRLEYLGRADGQVKIRGH 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4948 RVELGEVEhhvrECLTEAKQLAVEVIVPEGEGGYAMLAAFVQLGDDtyntlvkekAGGDsltvqvvfLDRVEEELAKRVP 5027
Cdd:cd12116    385 RIELGEIE----AALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAG---------AAPD--------AAALRAHLRATLP 443
                          490       500
                   ....*....|....*....|....*..
gi 1820002560 5028 EHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd12116    444 AYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
4547-5056 1.77e-101

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 337.76  E-value: 1.77e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHP 4626
Cdd:cd17655      3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4627 ASRHEHIFRQTGAQVVLASAQYATLWTSLGRSVVI----VSEASTSQLPVVtktadpsVNPGNAAYAIFTSGSTGIPKGV 4702
Cdd:cd17655     83 EERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLdedtIYHEESENLEPV-------SKSDDLAYVIYTSGSTGKPKGV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4703 VLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNN--LAKAINAMDVNWALLT 4780
Cdd:cd17655    156 MIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGqaLTQYIRQNRITIIDLT 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4781 PSVARMLDP---CVVQSLKILVLGGEQVNSADWDRWPK----SIQTINAYGPTECSICCTTY---SGKQGFKSGTIGTSI 4850
Cdd:cd17655    236 PAHLKLLDAaddSEGLSLKHLIVGGEALSTELAKKIIElfgtNPTITNAYGPTETTVDASIYqyePETDQQVSVPIGKPL 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4851 VSVS-WVVDPEnhNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawLLEGygghsgrqGRLYKTGDLVRYDAD 4929
Cdd:cd17655    316 GNTRiYILDQY--GRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDP--FVPG--------ERMYRTGDLARWLPD 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4930 GNLVYLGRKDSQVKLRGQRVELGEVEHhvRECLTEAKQLAVeVIVPEGEGGYAMLAAFVqlgddtyntlVKEKaggdSLT 5009
Cdd:cd17655    384 GNIEFLGRIDHQVKIRGYRIELGEIEA--RLLQHPDIKEAV-VIARKDEQGQNYLCAYI----------VSEK----ELP 446
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 5010 VQvvfldRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:cd17655    447 VA-----QLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
5223-6235 3.07e-101

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 360.13  E-value: 3.07e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5223 LELRVDVDEDAFRAAWEHVVQLTAALRTRIVQhSELGLLQVV-------VEEKIQWTESKRLEEYLRE------DKAVSM 5289
Cdd:PRK10252    36 VELTGELDAPLLARAVVAGLAEADTLRMRFTE-DNGEVWQWVdpaltfpLPEIIDLRTQPDPHAAAQAlmqadlQQDLRV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5290 GLGDRLARYALIKEpydGGKRWFvW--TIHHALYDGWSLPRILQAVKQIYSGAV---PERQPSFNAFIQYLGQQDLEAAT 5364
Cdd:PRK10252   115 DSGKPLVFHQLIQL---GDNRWY-WyqRYHHLLVDGFSFPAITRRIAAIYCAWLrgePTPASPFTPFADVVEEYQRYRAS 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5365 LYWQTAlADCKAALFPTLPPTVTqpVADTtveyqcPPPSQSATD-----------------------ITTSTLVRAAWAI 5421
Cdd:PRK10252   191 EAWQRD-AAFWAEQRRQLPPPAS--LSPA------PLPGRSASAdilrlkleftdgafrqlaaqasgVQRPDLALALVAL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5422 VTSRYTSSDDVVFGATVTGR-NAPIAGVEAMVgptIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAH-----EQtgLQR 5495
Cdd:PRK10252   262 WLGRLCGRMDYAAGFIFMRRlGSAALTATGPV---LNVLPLRVHIAAQETLPELATRLAAQLKKMRRHqrydaEQ--IVR 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5496 IAKMSPGARHACGfqTLLVVQPTDDVLGSDDMLGewrsysemqdfTTYALmvqCTLAKDRVEVTASFD------------ 5563
Cdd:PRK10252   337 DSGRAAGDEPLFG--PVLNIKVFDYQLDFPGVQA-----------QTHTL---ATGPVNDLELALFPDehgglsieilan 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5564 -ARVIEQWVVEKMLRQFGFvMQQLAEAGAEKtVSDIETTTLEDRQQLWAWNQNVPPAIERCVHDLFTEQAKARPHAPAIC 5642
Cdd:PRK10252   401 pQRYDEATLIAHAERLKAL-IAQFAADPALL-CGDVDILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALA 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5643 AWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQV 5722
Cdd:PRK10252   479 DARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSL 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5723 VVTSAQHSARWIGTnhQVVTVSAGSLGQLSTLVNPVGLPAiPENAVYIMFTSGSTGIPKGVVLEHRAVVTSC-WGRGRaF 5801
Cdd:PRK10252   559 LITTADQLPRFADV--PDLTSLCYNAPLAPQGAAPLQLSQ-PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLlWMQNH-Y 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5802 GITNLSRVLQFASYTFDACMDEIITTLMYGGCICV-PSDSDRrnD---LVKAISTMDVSCALLTPS-----VARL---LE 5869
Cdd:PRK10252   635 PLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMaEPEAHR--DplaMQQFFAEYGVTTTHFVPSmlaafVASLtpeGA 712
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5870 PSSVPTLQMLVLQGEQVSFADWNRWPASVQTI--NGYGPTECSICCNTYSGKQGFKSGIIGTSVaSVSW--------VVD 5939
Cdd:PRK10252   713 RQSCASLRQVFCSGEALPADLCREWQQLTGAPlhNLYGPTEAAVDVSWYPAFGEELAAVRGSSV-PIGYpvwntglrILD 791
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5940 penhDRLAPL--GSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegYPGhpgrqGRLYKTGDLVRYDANGNLVCLG 6017
Cdd:PRK10252   792 ----ARMRPVppGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-----APG-----ERMYRTGDVARWLDDGAVEYLG 857
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6018 RKDSQVKLRGQRVELGEVEHHVREcLPEARQ-LAVEVILPSGQK---DHAMLAAFVQLEEGtqnALLDKEAsgedsmaqv 6093
Cdd:PRK10252   858 RSDDQLKIRGQRIELGEIDRAMQA-LPDVEQaVTHACVINQAAAtggDARQLVGYLVSQSG---LPLDTSA--------- 924
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6094 vflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLreigasftaqqiANMQTSSQDPKRQPSTEAEQTMQKLW 6173
Cdd:PRK10252   925 -----LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL------------PLPELKAQVPGRAPKTGTETIIAAAF 987
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 6174 AQVLGIELNGIglDDSFFRLGGDSIAAMKLVGEARRI-GLQLSVADIF------RYARLVDLASLDTSQ 6235
Cdd:PRK10252   988 SSLLGCDVVDA--DADFFALGGHSLLAMKLAAQLSRQfARQVTPGQVMvastvaKLATLLDAEEDESRR 1054
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
451-1465 4.14e-101

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 359.74  E-value: 4.14e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  451 LELRADVDEHAFRAAWEYVVQSIAVLRTRIVQhSELGLLQVVvEEKMQWTESESLEEYLNED-KAASMGL---------- 519
Cdd:PRK10252    36 VELTGELDAPLLARAVVAGLAEADTLRMRFTE-DNGEVWQWV-DPALTFPLPEIIDLRTQPDpHAAAQALmqadlqqdlr 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  520 ---GDRLARYALIKesCGGKRWFvW--TIHHALYDGWSLPLVLDAVKQVYSGAALERQPSFNTFiqyVSQQDV------- 587
Cdd:PRK10252   114 vdsGKPLVFHQLIQ--LGDNRWY-WyqRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPASPF---TPFADVveeyqry 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  588 ------KAAAAYWQTALADceavlFPPLPSTVTQPVADTT-------VKYQCPPSP----EVTSSNITTSTLIRAAWAII 650
Cdd:PRK10252   188 raseawQRDAAFWAEQRRQ-----LPPPASLSPAPLPGRSasadilrLKLEFTDGAfrqlAAQASGVQRPDLALALVALW 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  651 ASRYTSSEDIVFGTTVTGR--NAPITgveaMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEM-----IAYEQtgLQR 723
Cdd:PRK10252   263 LGRLCGRMDYAAGFIFMRRlgSAALT----ATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMrrhqrYDAEQ--IVR 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  724 IMKMGPGPQHACGfqTLLVVHPTDDVLSSDDTLGEWHSRS-----DSELQYFttyaLTIQCTLAVEgvqITASFDARVVE 798
Cdd:PRK10252   337 DSGRAAGDEPLFG--PVLNIKVFDYQLDFPGVQAQTHTLAtgpvnDLELALF----PDEHGGLSIE---ILANPQRYDEA 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  799 HwvVEKMLGQFSFVMQQLAEAGvEKKVADIETTTLEDRQQLWVWNADMPPAVDRCIHDLFAEQARARPDASAVCAWDGEL 878
Cdd:PRK10252   408 T--LIAHAERLKALIAQFAADP-ALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQF 484
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  879 TYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSQ 958
Cdd:PRK10252   485 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTAD 564
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  959 HAMLFASSerhQVTVSKVSTSQLPTVVNFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHAR 1038
Cdd:PRK10252   565 QLPRFADV---PDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDV 641
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1039 VLQFASYTFDACIAEIITTLLYGGCICV-PSESDRR-NNLAKAISTMDVNCALLTPS-----VARL---LEPSAVPSLKR 1108
Cdd:PRK10252   642 VLQKTPCSFDVSVWEFFWPFIAGAKLVMaEPEAHRDpLAMQQFFAEYGVTTTHFVPSmlaafVASLtpeGARQSCASLRQ 721
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1109 LVLQGEQVSFADWNRWPGSVQTI--NGYGPTECSVCCNTYSGKQGFKSGIIGTSVaSLSW--------VVDAgnHNRLAP 1178
Cdd:PRK10252   722 VFCSGEALPADLCREWQQLTGAPlhNLYGPTEAAVDVSWYPAFGEELAAVRGSSV-PIGYpvwntglrILDA--RMRPVP 798
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1179 LGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawllegyeghAGRRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQ 1258
Cdd:PRK10252   799 PGVAGDLYLTGIQLAQGYLGRPDLTASRFIADP----------FAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQ 868
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1259 RVELGEIEHHVREcLPEARQLAVevilpsgqkeHALLAafiqldkgNHNAlfeekASGEDSMAQVVFLT----------G 1328
Cdd:PRK10252   869 RIELGEIDRAMQA-LPDVEQAVT----------HACVI--------NQAA-----ATGGDARQLVGYLVsqsglpldtsA 924
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1329 VEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLqdigasftvqQLAEmrTSSQGPKRQPSTEVEQTMQQLWAQVLS 1408
Cdd:PRK10252   925 LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL----------PLPE--LKAQVPGRAPKTGTETIIAAAFSSLLG 992
                         1050      1060      1070      1080      1090
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 1409 IEPNSIglDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADIFRHPRLVDLARVQNSQ 1465
Cdd:PRK10252   993 CDVVDA--DADFFALGGHSLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLATLLDAE 1048
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
3465-3976 5.76e-101

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 334.28  E-value: 5.76e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 3544
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3545 HPASRHEEIFEQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdsTNTSvrPENAAYIIFTSGSTGVPKGVVL 3624
Cdd:cd17653     81 LPSARIQAILRTSGATLLL---------------------------------TTDS--PDDLAYIIFTSGSTGIPKGVMV 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3625 EHRAVaTSCLGHGRA-FGITNLSRVLQFASYTFDACIAEIITTLlCGGCICVPSDSDrrNSLAKAISTMDVnwAFLTPSV 3703
Cdd:cd17653    126 PHRGV-LNYVSQPPArLDVGPGSRVAQVLSIAFDACIGEIFSTL-CNGGTLVLADPS--DPFAHVARTVDA--LMSTPSI 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3704 ARLLDPGLIPSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTgYTTKQGFEPSTIGTSVASVS-WVVDPENh 3782
Cdd:cd17653    200 LSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISST-MTELLPGQPVTIGKPIPNSTcYILDADL- 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3783 nRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAWllegypghPGRqgRLYKTGDLVQYNADGNLVYLGRKDSQV 3862
Cdd:cd17653    278 -QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW--------PGS--RMYRTGDYGRWTEDGGLEFLGREDNQV 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3863 KVRGQRVELGEVEHHVRECLPEARQLAVEVIlpSGQkdhamLAAFVqleegtqnalldkeaggedsMAQVVFLASVEEEL 3942
Cdd:cd17653    347 KVRGFRINLEEIEEVVLQSQPEVTQAAAIVV--NGR-----LVAFV--------------------TPETVDVDGLRSEL 399
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 3943 AKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:cd17653    400 AKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
4545-5056 1.07e-100

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 333.51  E-value: 1.07e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4545 DQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 4624
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4625 HPASRHEHIFRQTGAQVVLasaqyatlwtslgrsvvivseastsqlpvvtkTADpsvNPGNAAYAIFTSGSTGIPKGVVL 4704
Cdd:cd17653     81 LPSARIQAILRTSGATLLL--------------------------------TTD---SPDDLAYIIFTSGSTGIPKGVMV 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4705 EHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLlCCGCICVPSDSDrrNNLAKAINAMDVnwALLTPSVA 4784
Cdd:cd17653    126 PHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTL-CNGGTLVLADPS--DPFAHVARTVDA--LMSTPSIL 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4785 RMLDPCVVQSLKILVLGGEQVNSADWDRWPKSIQTINAYGPTECSICCTTYSGKQGFKSgTIGTSIVSVS-WVVDPENhn 4863
Cdd:cd17653    201 STLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQPV-TIGKPIPNSTcYILDADL-- 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4864 RLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAWllegygghSGRqgRLYKTGDLVRYDADGNLVYLGRKDSQVK 4943
Cdd:cd17653    278 QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW--------PGS--RMYRTGDYGRWTEDGGLEFLGREDNQVK 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4944 LRGQRVELGEVEHHVRECLTEAKQLAveVIVPEGeggyaMLAAFVqlgddtyntlvkekaggdslTVQVVFLDRVEEELA 5023
Cdd:cd17653    348 VRGFRINLEEIEEVVLQSQPEVTQAA--AIVVNG-----RLVAFV--------------------TPETVDVDGLRSELA 400
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 5024 KRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:cd17653    401 KHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
4142-5148 1.89e-100

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 357.82  E-value: 1.89e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4142 LELRADVNEDAFRAAWELVVQLTAVLRTRIVQhSELGLLQVV-------VEERIQWTESESLEEYPRE------DKAVSM 4208
Cdd:PRK10252    36 VELTGELDAPLLARAVVAGLAEADTLRMRFTE-DNGEVWQWVdpaltfpLPEIIDLRTQPDPHAAAQAlmqadlQQDLRV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4209 GVGDRLARYALIKEpydGGKRWFvW--TMHHALYDGWSLPRILHAVKQAYSGVVLERQPS---FNAFIQYLS-----QQD 4278
Cdd:PRK10252   115 DSGKPLVFHQLIQL---GDNRWY-WyqRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPaspFTPFADVVEeyqryRAS 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4279 P--EAAAAYWQTALVDCK--AALFPTlpPTVTQPVADTTVEYQCPPPSQS-------ATDITTSTLARAAWAIVTSRYTS 4347
Cdd:PRK10252   191 EawQRDAAFWAEQRRQLPppASLSPA--PLPGRSASADILRLKLEFTDGAfrqlaaqASGVQRPDLALALVALWLGRLCG 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4348 SDDVVFGATVTGRnapiAGGEAIV--GPTIATVPVRLRVQRDQTVFAFLQGVQQQATDMIAH-----EQtgLQRIAKMSP 4420
Cdd:PRK10252   269 RMDYAAGFIFMRR----LGSAALTatGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHqrydaEQ--IVRDSGRAA 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4421 GARHACGfqTLLVVQPTDDVLGSDDMLG--EWRSYSEMQDFTTYalmvqcVLVKDRVGVTASFDA---RVIEQWVVEKML 4495
Cdd:PRK10252   343 GDEPLFG--PVLNIKVFDYQLDFPGVQAqtHTLATGPVNDLELA------LFPDEHGGLSIEILAnpqRYDEATLIAHAE 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4496 RQFGFVMQQLADagEEKKVAGIETTTTGDRQQLWAWNQDVPPAIERCVHDQFAEQARARPDTPAICAWDGELTYGELDTL 4575
Cdd:PRK10252   415 RLKALIAQFAAD--PALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQ 492
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4576 SSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLASAQYATLWTSL 4655
Cdd:PRK10252   493 VVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADV 572
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4656 GRSVVIVSEAstsQLPVVTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYT 4735
Cdd:PRK10252   573 PDLTSLCYNA---PLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCS 649
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4736 FDACIAEIITTLLCCGCICV-PSDSDRR-NNLAKAINAMDVNWALLTPSvarMLD-----------PCVVQSLKILVLGG 4802
Cdd:PRK10252   650 FDVSVWEFFWPFIAGAKLVMaEPEAHRDpLAMQQFFAEYGVTTTHFVPS---MLAafvasltpegaRQSCASLRQVFCSG 726
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4803 EQVNSADWDRWPKSIQTI--NAYGPTECSICCTTYSGKQGFKSGTIGTSiVSVSW--------VVDpeNHNRLAPLGSIG 4872
Cdd:PRK10252   727 EALPADLCREWQQLTGAPlhNLYGPTEAAVDVSWYPAFGEELAAVRGSS-VPIGYpvwntglrILD--ARMRPVPPGVAG 803
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4873 ELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygghsGRQGRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELG 4952
Cdd:PRK10252   804 DLYLTGIQLAQGYLGRPDLTASRFIADPF----------APGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELG 873
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4953 EVEHHVRECLTEAKQLAVEVIV---PEGEGGYAMLAAFVQLGDDtyntlvkekAGGDSLTVQvvfldrveEELAKRVPEH 5029
Cdd:PRK10252   874 EIDRAMQALPDVEQAVTHACVInqaAATGGDARQLVGYLVSQSG---------LPLDTSALQ--------AQLRERLPPH 936
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5030 MMLTTFFTLEAMPTTTSGKIDRKRLreigasfTAQQLAemrtsSQGPKRQPSTEAERTMQQLWTRVLGIELNGIglDDSF 5109
Cdd:PRK10252   937 MVPVVLLQLDQLPLSANGKLDRKAL-------PLPELK-----AQVPGRAPKTGTETIIAAAFSSLLGCDVVDA--DADF 1002
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|
gi 1820002560 5110 FRLGGDSIAAMKLVGEARRT-GLQLSVADVFRHPRLVDLA 5148
Cdd:PRK10252  1003 FALGGHSLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLA 1042
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
3022-3430 2.48e-100

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 331.19  E-value: 2.48e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3022 VFPCTPMQEGILTSQGKDPDAYWVCFIYEVIPnqetSISLARLQQAWKGVVHQHSLLRTLLVDNVPGSTgTTNVVLKDPQ 3101
Cdd:cd19542      1 IYPCTPMQEGMLLSQLRSPGLYFNHFVFDLDS----SVDVERLRNAWRQLVQRHDILRTVFVESSAEGT-FLQVVLKSLD 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3102 PSISVFSSEGTATIELFRSRYNpaAQRSIGQLQHHLSICQLNNGKVYLCLDINHAIIDAHSRGILMHDLQEAYDANLNPQ 3181
Cdd:cd19542     76 PPIEEVETDEDSLDALTRDLLD--DPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3182 STSFRDFASYIKQQSQEEAGRYWAEYLDGVEPCFFPSLGdsgGANTIPRTVEVPSIDSSAVHMFCKIWEVTPATIIQTAW 3261
Cdd:cd19542    154 APPFSDYISYLQSQSQEESLQYWRKYLQGASPCAFPSLS---PKRPAERSLSSTRRSLAKLEAFCASLGVTLASLFQAAW 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3262 ALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPLISILPCRIHLHKQLTVLEALKTVQENYASSLSFQTFPLASMHSF 3341
Cdd:cd19542    231 ALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRA 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3342 LGLGTSA-LFNTALSLQRIDDIgPCSASEIT--LKMKEGLDPTEYNITLSAGYSKDAIDISMTFRAGCMDLVQAKRLASN 3418
Cdd:cd19542    311 LGLWPSGtLFNTLVSYQNFEAS-PESELSGSsvFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQ 389
                          410
                   ....*....|..
gi 1820002560 3419 FSQAIKAVTTEP 3430
Cdd:cd19542    390 FDDILEALLANP 401
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
5625-6135 2.93e-100

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 334.24  E-value: 2.93e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5625 HDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 5704
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5705 DHPASRHEDTFRHTGAQVVVTSAQhSARWIGTNHQVVTVSAGSLGQLSTLVNPVglPAIPENAVYIMFTSGSTGIPKGVV 5784
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTAD-LAARLPAGGDVALLGDEALAAPPATPPLV--PPRPDNLAYVIYTSGSTGRPKGVM 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5785 LEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPsDSDRRND---LVKAISTMDVSCALLT 5861
Cdd:cd17646    158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVA-RPGGHRDpayLAALIREHGVTTCHFV 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5862 PSVARLL----EPSSVPTLQMLVLQGEQVSFADWNRWPA--SVQTINGYGPTECSICCN--TYSGKQGFKSGIIGTSVAS 5933
Cdd:cd17646    237 PSMLRVFlaepAAGSCASLRRVFCSGEALPPELAARFLAlpGAELHNLYGPTEAAIDVThwPVRGPAETPSVPIGRPVPN 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5934 VS-WVVDPENhdRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpawllegyPGHPGrqGRLYKTGDLVRYDANGN 6012
Cdd:cd17646    317 TRlYVLDDAL--RPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPD--------PFGPG--SRMYRTGDLARWRPDGA 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6013 LVCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQLAveVILPSGQKDHAMLAAFVQLEEGtqnalldkeASGEDSmaq 6092
Cdd:cd17646    385 LEFLGRSDDQVKIRGFRVEPGEIEAALAAH-PAVTHAV--VVARAAPAGAARLVGYVVPAAG---------AAGPDT--- 449
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 6093 vvflASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd17646    450 ----AALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1533-2539 5.12e-100

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 356.28  E-value: 5.12e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1533 LELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQhSELGLLQVVIEENIQ--------WTEPKSLEEYLSEDKA-----VSV 1599
Cdd:PRK10252    36 VELTGELDAPLLARAVVAGLAEADTLRMRFTE-DNGEVWQWVDPALTFplpeiidlRTQPDPHAAAQALMQAdlqqdLRV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1600 GLGDPLARYAFVKeaCGGKRWFvW--TIHHAVYDGWSLPLILHAVKQVYSGGVLQWQPSFNAFI----------QYLGQQ 1667
Cdd:PRK10252   115 DSGKPLVFHQLIQ--LGDNRWY-WyqRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPASPFTpfadvveeyqRYRASE 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1668 DLEATVAYWQTALADceavlfptLPPTVT---QPVADAT-------VEYQCP-----PLSKATSDTTTSTLIRAAWAIVT 1732
Cdd:PRK10252   192 AWQRDAAFWAEQRRQ--------LPPPASlspAPLPGRSasadilrLKLEFTdgafrQLAAQASGVQRPDLALALVALWL 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1733 SRYTTSDDVVFGTTVTGRntpvTGVEAMV--GPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAH-----EQtgLQRI 1805
Cdd:PRK10252   264 GRLCGRMDYAAGFIFMRR----LGSAALTatGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHqrydaEQ--IVRD 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1806 AKMGQGPQHAcsFQTLLVVQPVDDVLDNTLGEWRDHsELQEFTTYTLMLQCMLAAEG---VQITASFDtRVIEKWVVEKM 1882
Cdd:PRK10252   338 SGRAAGDEPL--FGPVLNIKVFDYQLDFPGVQAQTH-TLATGPVNDLELALFPDEHGglsIEILANPQ-RYDEATLIAHA 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1883 LRQFSFiMQQLAEAGAEKtVSDIETTTPEDRQQLWAWNQEVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDA 1962
Cdd:PRK10252   414 ERLKAL-IAQFAADPALL-CGDVDILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMRE 491
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1963 LSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSAQHSARWIG 2042
Cdd:PRK10252   492 QVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFAD 571
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2043 tnhqvvtVSAGSLEQFSTLVNPVD----LPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLRALQ 2118
Cdd:PRK10252   572 -------VPDLTSLCYNAPLAPQGaaplQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQ 644
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2119 FTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSS----------VARLLDPCLvpSLKVL 2186
Cdd:PRK10252   645 KTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDplAMQQFFAEYGVTTTHFVPSmlaafvasltPEGARQSCA--SLRQV 722
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2187 VLGGEQVNST---DWGKWpSSVQTINGYGPTECCVFCTGYTGIQGFQSGNIGTS--IASVSW-----VVDpeNHGRLAPL 2256
Cdd:PRK10252   723 FCSGEALPADlcrEWQQL-TGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSvpIGYPVWntglrILD--ARMRPVPP 799
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2257 GSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegYPGhegrqGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQR 2336
Cdd:PRK10252   800 GVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-----APG-----ERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQR 869
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2337 VELGEVEHHMRKcLPEANQ-LAVEVVppsgERDHAMLAafirlDDETRnsplIIKY--AEDNSTAQIVFLtgiEEELSER 2413
Cdd:PRK10252   870 IELGEIDRAMQA-LPDVEQaVTHACV----INQAAATG-----GDARQ----LVGYlvSQSGLPLDTSAL---QAQLRER 932
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2414 LPQHMVPTVFFALVHFPTTTSGKTDRKRLreigasfTAQQLAemrtsSEGPKRQPSTEAERTMQQLWAQVLGieLESIGL 2493
Cdd:PRK10252   933 LPPHMVPVVLLQLDQLPLSANGKLDRKAL-------PLPELK-----AQVPGRAPKTGTETIIAAAFSSLLG--CDVVDA 998
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 2494 DDSFFRLGGDSITAMQISSS-ARALHLSVSTGDILKKKTIALIAREI 2539
Cdd:PRK10252   999 DADFFALGGHSLLAMKLAAQlSRQFARQVTPGQVMVASTVAKLATLL 1045
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
1943-2442 7.44e-100

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 331.14  E-value: 7.44e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1943 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIF 2022
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2023 RQTGAQVVVTSaqhsarwigtnhqvvtvsagsleqfstlvnpvdlpakPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCL 2102
Cdd:cd17652     81 ADARPALLLTT-------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2103 GHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERR--DNLAKAITDMQVNWGYLTSSVARLLDPCLV 2180
Cdd:cd17652    124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLpgEPLADLLREHRITHVTLPPAALAALPPDDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2181 PSLKVLVLGGEQVNSTDWGKWPSSVQTINGYGPTECCVFCTGYTGIQGFQSGNIGTSIASVS-WVVDPenHGRLAPLGSI 2259
Cdd:cd17652    204 PDLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRvYVLDA--RLRPVPPGVP 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2260 GELLVEGPILARGYLNDVDKTQAAFIDDPAwlleGYPGhegrqGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVEL 2339
Cdd:cd17652    282 GELYIAGAGLARGYLNRPGLTAERFVADPF----GAPG-----SRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2340 GEVEHHMRKClpEANQLAVEVV---PPSGERdhamLAAFIRLDDETRNSPliikyaednstaqivflTGIEEELSERLPQ 2416
Cdd:cd17652    353 GEVEAALTEH--PGVAEAVVVVrddRPGDKR----LVAYVVPAPGAAPTA-----------------AELRAHLAERLPG 409
                          490       500
                   ....*....|....*....|....*.
gi 1820002560 2417 HMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd17652    410 YMVPAAFVVLDALPLTPNGKLDRRAL 435
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
855-1365 1.92e-99

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 331.93  E-value: 1.92e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  855 HDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 934
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  935 GHPASRHEEIFKQIGAQVVLTSSQHAMLFASSERHQVTVSKVSTSQLPTVvnfAKSPVDPGNTAYIIFTSGTTGIPKGVV 1014
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATP---PLVPPRPDNLAYVIYTSGSTGRPKGVM 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1015 LQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRN--NLAKAISTMDVNCALLTP 1092
Cdd:cd17646    158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDpaYLAALIREHGVTTCHFVP 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1093 SVARLL----EPSAVPSLKRLVLQGEQVS---FADWNRWPGsVQTINGYGPTECS--VCCNTYSGKQGFKSGIIGTSVAS 1163
Cdd:cd17646    238 SMLRVFlaepAAGSCASLRRVFCSGEALPpelAARFLALPG-AELHNLYGPTEAAidVTHWPVRGPAETPSVPIGRPVPN 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1164 LS-WVVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawllegyeghAGRRGRLYKTGDLVRCDADGN 1242
Cdd:cd17646    317 TRlYVLDD--ALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDP----------FGPGSRMYRTGDLARWRPDGA 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1243 LVCLGRKDSQVKVRGQRVELGEIEHHVREClPEARQLAveVILPSGQKEHALLAAFIQLDKGnhnalfeekASGEDSMAq 1322
Cdd:cd17646    385 LEFLGRSDDQVKIRGFRVEPGEIEAALAAH-PAVTHAV--VVARAAPAGAARLVGYVVPAAG---------AAGPDTAA- 451
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 1323 vvfltgVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17646    452 ------LRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
5626-6137 2.00e-99

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 329.66  E-value: 2.00e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 5705
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5706 HPASRHEDTFRHTGAQVVVTsaqhsarwigtnhqvvtvsagslgqlstlvnpvglPAIPENAVYIMFTSGSTGIPKGVVL 5785
Cdd:cd17653     81 LPSARIQAILRTSGATLLLT-----------------------------------TDSPDDLAYIIFTSGSTGIPKGVMV 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5786 EHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGcICVPSDSDrrNDLVKAISTMDVScaLLTPSVA 5865
Cdd:cd17653    126 PHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGG-TLVLADPS--DPFAHVARTVDAL--MSTPSIL 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5866 RLLEPSSVPTLQMLVLQGEQVSFADWNRWPASVQTINGYGPTECSICCNTYSGKQGFKSgIIGTSVASVS-WVVDPEnhD 5944
Cdd:cd17653    201 STLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQPV-TIGKPIPNSTcYILDAD--L 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5945 RLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAWllegypghPGRqgRLYKTGDLVRYDANGNLVCLGRKDSQVK 6024
Cdd:cd17653    278 QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW--------PGS--RMYRTGDYGRWTEDGGLEFLGREDNQVK 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6025 LRGQRVELGEVEHHVRECLPEARQLAVEVIlpSGQkdhamLAAFVqleegtqnalldkeasgedsMAQVVFLASVEEELA 6104
Cdd:cd17653    348 VRGFRINLEEIEEVVLQSQPEVTQAAAIVV--NGR-----LVAFV--------------------TPETVDVDGLRSELA 400
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 6105 KRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:cd17653    401 KHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
3466-3976 4.41e-99

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 330.83  E-value: 4.41e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3466 LFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 3545
Cdd:cd17655      2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3546 PASRHEEIFEQTGAQVVVASAQYSARwTSSSCHVV-----TVSKALSSQLPAVvdstntsVRPENAAYIIFTSGSTGVPK 3620
Cdd:cd17655     82 PEERIQYILEDSGADILLTQSHLQPP-IAFIGLIDlldedTIYHEESENLEPV-------SKSDDLAYVIYTSGSTGKPK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3621 GVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAF 3698
Cdd:cd17655    154 GVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDgqALTQYIRQNRITIID 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3699 LTPSVARLLDP---GLIPSLKILAIGGEQSSSADWNRW----PGSVQKIHVYGPTECCIFCTGY-----TTKQGFEPstI 3766
Cdd:cd17655    234 LTPAHLKLLDAaddSEGLSLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDASIYqyepeTDQQVSVP--I 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3767 GTSVASVS-WVVDPEnhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegYPGhpgrqGRLYKTGDLVQ 3845
Cdd:cd17655    312 GKPLGNTRiYILDQY--GRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-----VPG-----ERMYRTGDLAR 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3846 YNADGNLVYLGRKDSQVKVRGQRVELGEVEHhvRECLPEARQLAVEVILPSGQKDHAMLAAFVQLEEGTQnalldkeagg 3925
Cdd:cd17655    380 WLPDGNIEFLGRIDHQVKIRGYRIELGEIEA--RLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPV---------- 447
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 3926 edsmaqvvflASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:cd17655    448 ----------AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
856-1367 9.97e-99

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 327.73  E-value: 9.97e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  856 DLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPG 935
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  936 HPASRHEEIFKQIGAQVVLtssqhamlfasserhqvtvskvstsqlptvvnFAKSPVDPgntAYIIFTSGTTGIPKGVVL 1015
Cdd:cd17653     81 LPSARIQAILRTSGATLLL--------------------------------TTDSPDDL---AYIIFTSGSTGIPKGVMV 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1016 QHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVpseSDRRNNLAKAISTMDVncALLTPSVA 1095
Cdd:cd17653    126 PHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL---ADPSDPFAHVARTVDA--LMSTPSIL 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1096 RLLEPSAVPSLKRLVLQGEQVSFADWNRWPGSVQTINGYGPTECSVCCNTYSGKQGFKSgIIGTSVASLS-WVVDAGNhn 1174
Cdd:cd17653    201 STLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQPV-TIGKPIPNSTcYILDADL-- 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1175 RLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAWLLEgyeghagrrgRLYKTGDLVRCDADGNLVCLGRKDSQVK 1254
Cdd:cd17653    278 QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGS----------RMYRTGDYGRWTEDGGLEFLGREDNQVK 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1255 VRGQRVELGEIEHHVRECLPEARQLAVEVIlpSGQkehalLAAFIqldkgnhnalfeekasgedsMAQVVFLTGVEEELA 1334
Cdd:cd17653    348 VRGFRINLEEIEEVVLQSQPEVTQAAAIVV--NGR-----LVAFV--------------------TPETVDVDGLRSELA 400
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 1335 KRLPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:cd17653    401 KHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
866-1365 1.11e-98

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 328.17  E-value: 1.11e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  866 PDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIF 945
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  946 KQIGAQVVLTssQHamlfasserhqvtvskvstsqlptvvnfakspvdPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCL 1025
Cdd:cd17649     81 EDSGAGLLLT--HH----------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1026 GHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSES--DRRNNLAKAISTMDVNCALLTPS-------VAR 1096
Cdd:cd17649    125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPAylqqlaeEAD 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1097 LLEPSAVPSLKRLVLQGEQVSFADWNRW-PGSVQTINGYGPTECSVCCNTYSGKQGFKSGI----IGTSVASLSWVVDaG 1171
Cdd:cd17649    205 RTGDGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGasmpIGRPLGGRSAYIL-D 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1172 NHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAwlleGYEGhagrrGRLYKTGDLVRCDADGNLVCLGRKDS 1251
Cdd:cd17649    284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPF----GAPG-----SRLYRTGDLARWRDDGVIEYLGRVDH 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1252 QVKVRGQRVELGEIEHHVREcLPEARQLAveVILPSGQKEHALLAAFIqldkgnhnalfeekasGEDSMAQVVFLTGVEE 1331
Cdd:cd17649    355 QVKIRGFRIELGEIEAALLE-HPGVREAA--VVALDGAGGKQLVAYVV----------------LRAAAAQPELRAQLRT 415
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 1332 ELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17649    416 ALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
857-1365 1.12e-98

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 329.67  E-value: 1.12e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  857 LFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGH 936
Cdd:cd17655      2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  937 PASRHEEIFKQIGAQVVLTSSQhamlFASSERHQ--VTVSKVSTSQLPTVVNFAkSPVDPGNTAYIIFTSGTTGIPKGVV 1014
Cdd:cd17655     82 PEERIQYILEDSGADILLTQSH----LQPPIAFIglIDLLDEDTIYHEESENLE-PVSKSDDLAYVIYTSGSTGKPKGVM 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1015 LQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNN--LAKAISTMDVNCALLTP 1092
Cdd:cd17655    157 IEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGqaLTQYIRQNRITIIDLTP 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1093 SVARLLEP---SAVPSLKRLVLQGEQVSFADWNRW----PGSVQTINGYGPTECSVCCNTY---SGKQGFKSGIIGTSVA 1162
Cdd:cd17655    237 AHLKLLDAaddSEGLSLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDASIYqyePETDQQVSVPIGKPLG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1163 SLS-WVVDAGnhNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawLLEGyeghagrrGRLYKTGDLVRCDADG 1241
Cdd:cd17655    317 NTRiYILDQY--GRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDP--FVPG--------ERMYRTGDLARWLPDG 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1242 NLVCLGRKDSQVKVRGQRVELGEIEHhvreclpeaRQLAVEVIlpsgqKEHALLAafiqldkgnhnalfEEKASGEDSM- 1320
Cdd:cd17655    385 NIEFLGRIDHQVKIRGYRIELGEIEA---------RLLQHPDI-----KEAVVIA--------------RKDEQGQNYLc 436
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1321 AQVVF-----LTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17655    437 AYIVSekelpVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
4544-5054 2.96e-98

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 328.47  E-value: 2.96e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4544 HDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 4623
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4624 DHPASRHEHIFRQTGAQVVLASAQYATLWTSLGRSVVIVSEASTSQLPVVTktaDPSVNPGNAAYAIFTSGSTGIPKGVV 4703
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPP---LVPPRPDNLAYVIYTSGSTGRPKGVM 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4704 LEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRN--NLAKAINAMDVNWALLTP 4781
Cdd:cd17646    158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDpaYLAALIREHGVTTCHFVP 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4782 SV----ARMLDPCVVQSLKILVLGGEQVNSADWDRWPK--SIQTINAYGPTECSICCT--TYSGKQGFKSGTIGTSIVSV 4853
Cdd:cd17646    238 SMlrvfLAEPAAGSCASLRRVFCSGEALPPELAARFLAlpGAELHNLYGPTEAAIDVThwPVRGPAETPSVPIGRPVPNT 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4854 S-WVVDPenHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygghsGRQGRLYKTGDLVRYDADGNL 4932
Cdd:cd17646    318 RlYVLDD--ALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF----------GPGSRMYRTGDLARWRPDGAL 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4933 VYLGRKDSQVKLRGQRVELGEVEHHVRECLTEAkqlAVEVIVPEGEGGYAMLAAFVQLGDDtyntlvkeKAGGDSltvqv 5012
Cdd:cd17646    386 EFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVT---HAVVVARAAPAGAARLVGYVVPAAG--------AAGPDT----- 449
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 5013 vflDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd17646    450 ---AALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
PRK12316 PRK12316
peptide synthase; Provisional
6257-7157 3.61e-98

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 359.66  E-value: 3.61e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6257 AQVSQDAAAMCSVDASSVEDMYPCSPLQEGLM--SLTAKRAGDYIMQsvleLRVDV---DEDAFRAAWEHVVQLTAALRT 6331
Cdd:PRK12316  4082 AGLDQARLDALPLPLGEIEDIYPLSPMQQGMLfhSLYEQEAGDYINQ----MRVDVqglDVERFRAAWQAALDRHDVLRS 4157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6332 RIVQHSELGLLQVVVEEKIQ-------WTESKRLEEYLREDKAVSMGLG-----DPLARYAIIKEAWGGKRwFVWTIHHA 6399
Cdd:PRK12316  4158 GFVWQGELGRPLQVVHKQVSlpfaeldWRGRADLQAALDALAAAERERGfdlqrAPLLRLVLVRTAEGRHH-LIYTNHHI 4236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6400 LYDGWSLPRVLQAVKQAYNGAVLETQPS-FNAFIQYLSQQDLEATAAYWQTALADCEA-TLFPPLPSSVKQLVADTTVEH 6477
Cdd:PRK12316  4237 LMDGWSNSQLLGEVLERYSGRPPAQPGGrYRDYIAWLQRQDAAASEAFWREQLAALDEpTRLAQAIARADLRSANGYGEH 4316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6478 QCPLPSRSTSDTTT---------STLIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTSIDAIVGPTIATVPLRVRLQKD 6548
Cdd:PRK12316  4317 VRELDATATARLREfartqrvtlNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQ 4396
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6549 QTVSSFLGYLQQQATEMIAYEQTGLQQI---AKMGPDPQhacgFQTLLVVQ--PAGDVLGSDDTLGKWRGYSGLQDFMTY 6623
Cdd:PRK12316  4397 QSVVEWLQQVQRQNLALREHEHTPLYEIqrwAGQGGEAL----FDSLLVFEnyPVSEALQQGAPGGLRFGEVTNHEQTNY 4472
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6624 ----ALGVRCTLSAEGVKITASFDARVIEhwvveKMLGQFSFAMQQLAEASAdRKVADIDITTTTDRQQLWA-WN---AE 6695
Cdd:PRK12316  4473 pltlAVGLGETLSLQFSYDRGHFDAATIE-----RLARHLTNLLEAMAEDPQ-RRLGELQLLEKAEQQRIVAlWNrtdAG 4546
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6696 LPLAvdRCVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKA 6775
Cdd:PRK12316  4547 YPAT--RCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKA 4624
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6776 GGAFVPLDPDHP-------------------------------------------------------------------- 6787
Cdd:PRK12316  4625 GGAYVPLDPEYPrerlaymmedsgaallltqshllqrlpipdglaslaldrdedwegfpahdpavrlhpdnlayviytsg 4704
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6788 --------ASRHEDILRQ------------------------------------TGAQVILASAQ----NTTLFQSSNQT 6819
Cdd:PRK12316  4705 stgrpkgvAVSHGSLVNHlhatgeryeltpddrvlqfmsfsfdgsheglyhpliNGASVVIRDDSlwdpERLYAEIHEHR 4784
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6820 VVTVNRSSYILFP----DENREAYPFVR-------------------------------PSNAA---------------- 6848
Cdd:PRK12316  4785 VTVLVFPPVYLQQlaehAERDGEPPSLRvycfggeavaqasydlawralkpvylfngygPTETTvtvllwkardgdacga 4864
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6849 ----------------------LAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPawlVEGHGkhpgrrGRLYKTGD 6906
Cdd:PRK12316  4865 aympigtplgnrsgyvldgqlnPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDP---FGAPG------GRLYRTGD 4935
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6907 LVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcmPRATQMAVeVISPAGAAEQaktMVVAFLqlndeardallg 6986
Cdd:PRK12316  4936 LARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLRE--HPAVREAV-VIAQEGAVGK---QLVGYV------------ 4997
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6987 gnVPND----DNLSAQVVFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREIGASFTAQQLAemrtssqg 7062
Cdd:PRK12316  4998 --VPQDpalaDADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYV-------- 5067
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7063 pkrQPSTEAERTMQQLWARMLKVKadSIGLDDSFFRLGGDSIVAMKLVGEAR-RTGLQLSVADVFRHPRLVDLAYVQNSQ 7141
Cdd:PRK12316  5068 ---APRSELEQQVAAIWAEVLQLE--RVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTLAAFVELAAAA 5142
                         1130
                   ....*....|....*..
gi 1820002560 7142 CSSAAEEVPAF-SLLGE 7157
Cdd:PRK12316  5143 GSGDDEKFDDLeELLSE 5159
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
1943-2443 6.47e-98

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 325.86  E-value: 6.47e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1943 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIF 2022
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2023 RQTGAQVVVTsaQHsarwigtnhqvvtvsagsleqfstlvnpvdlpakPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCL 2102
Cdd:cd17649     81 EDSGAGLLLT--HH----------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2103 GHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDS--ERRDNLAKAITDMQVNWGYLTSS-------VAR 2173
Cdd:cd17649    125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPAylqqlaeEAD 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2174 LLDPCLVPSLKVLVLGGEQVNSTDWGKW-PSSVQTINGYGPTECCVFCTGYTGIQGFQSGN----IGTSIASVSWVVDpE 2248
Cdd:cd17649    205 RTGDGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGasmpIGRPLGGRSAYIL-D 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2249 NHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwlleGYPGhegrqGRLYKTGDLVRYSSDGNLVCLGRKDS 2328
Cdd:cd17649    284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPF----GAPG-----SRLYRTGDLARWRDDGVIEYLGRVDH 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2329 QVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVPPSGERdhaMLAAFIRLDDETRNspliikyAEDnstaqivfLTGIEE 2408
Cdd:cd17649    355 QVKIRGFRIELGEIEAALLE-HPGVREAAVVALDGAGGK---QLVAYVVLRAAAAQ-------PEL--------RAQLRT 415
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1820002560 2409 ELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLR 2443
Cdd:cd17649    416 ALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
1930-2442 1.01e-97

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 325.93  E-value: 1.01e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1930 CVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL 2009
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2010 DPDHPASRHEDIFRQTGAQVVVTsaqhsarwigtnhqvvtvsagsleqfstlvnpvdlpaKPENAAYVMFTSGSTGTPKG 2089
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLT-------------------------------------QPENLAYVIYTSGSTGKPKG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2090 VVLEHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYL 2167
Cdd:cd17644    124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSleDFVQYIQQWQLTVLSL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2168 TSSVARLL------DPCLVP-SLKVLVLGGEQVNSTDWGKWPSSV----QTINGYGPTECCVFCTGY--TGIQGFQSGN- 2233
Cdd:cd17644    204 PPAYWHLLvlelllSTIDLPsSLRLVIVGGEAVQPELVRQWQKNVgnfiQLINVYGPTEATIAATVCrlTQLTERNITSv 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2234 -IGTSIASVSWVVDPENHgRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPawllegYPGHEGRqgRLYKTGDLV 2312
Cdd:cd17644    284 pIGRPIANTQVYILDENL-QPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHP------FNSSESE--RLYKTGDLA 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2313 RYSSDGNLVCLGRKDSQVKVRGQRVELGEVEhhmrKCLPEANQLAVEVVppsgerdhamlaafIRLDDETRNSPLII--- 2389
Cdd:cd17644    355 RYLPDGNIEYLGRIDNQVKIRGFRIELGEIE----AVLSQHNDVKTAVV--------------IVREDQPGNKRLVAyiv 416
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 2390 -KYAEDNSTAQivfltgIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd17644    417 pHYEESPSTVE------LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
7612-8122 1.03e-97

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 326.98  E-value: 1.03e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7612 LFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 7691
Cdd:cd17655      2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7692 PASRHEEIFEQTGAQVVVASAQYSARwTSSSCHVV-----TVSKALSSQLPAVvdstntsVRPENAAYIIFTSGSTGVPK 7766
Cdd:cd17655     82 PEERIQYILEDSGADILLTQSHLQPP-IAFIGLIDlldedTIYHEESENLEPV-------SKSDDLAYVIYTSGSTGKPK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7767 GVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAF 7844
Cdd:cd17655    154 GVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDgqALTQYIRQNRITIID 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7845 LTPSVARLLDP---GLIPSLKILAIGGEQSSSADWNRW----PGSVQKIHVYGPTECCIFCTGY-----TTKQGFEPstI 7912
Cdd:cd17655    234 LTPAHLKLLDAaddSEGLSLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDASIYqyepeTDQQVSVP--I 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7913 GTSVASVS-WVVDPEnhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegYPGhpgrqGRLYKTGDLVQ 7991
Cdd:cd17655    312 GKPLGNTRiYILDQY--GRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-----VPG-----ERMYRTGDLAR 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7992 YNADGNLVYLGRKDSQVKVRGQRVELGEVEHhvRECLPEARQLAVEVILPSGQKNHAMLAVFVQlgkgthiahleekagg 8071
Cdd:cd17655    380 WLPDGNIEFLGRIDHQVKIRGYRIELGEIEA--RLLQHPDIKEAVVIARKDEQGQNYLCAYIVS---------------- 441
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 8072 EDSMAQvvflTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:cd17655    442 EKELPV----AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
1943-2442 2.52e-97

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 325.01  E-value: 2.52e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1943 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIF 2022
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2023 RQTGAQVVVTSAQHSARWIGTnhqvVTVSAGSLEQFSTLVNPVDLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCL 2102
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAG----LPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2103 GHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSSVARLL---DP 2177
Cdd:cd12116    157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDpeALARLIEAHSITVMQATPATWRMLldaGW 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2178 CLVPSLKVLVlGGEQVNSTDWGKWPSSV-QTINGYGPTE------CCVFCTGYTGIQgfqsgnIGTSIASVS-WVVDPEn 2249
Cdd:cd12116    237 QGRAGLTALC-GGEALPPDLAARLLSRVgSLWNLYGPTEttiwstAARVTAAAGPIP------IGRPLANTQvYVLDAA- 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2250 hGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwlleGYPGHegrqgRLYKTGDLVRYSSDGNLVCLGRKDSQ 2329
Cdd:cd12116    309 -LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPF----AGPGS-----RLYRTGDLVRRRADGRLEYLGRADGQ 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2330 VKVRGQRVELGEVEHHMRKcLPEANQLAVEVVPPSGERdhaMLAAFIRLDDETRNSPliikyaednstaqivflTGIEEE 2409
Cdd:cd12116    379 VKIRGHRIELGEIEAALAA-HPGVAQAAVVVREDGGDR---RLVAYVVLKAGAAPDA-----------------AALRAH 437
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 2410 LSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd12116    438 LRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
7611-8122 3.74e-97

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 323.11  E-value: 3.74e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 7690
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7691 HPASRHEEIFEQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdsTNTSvrPENAAYIIFTSGSTGVPKGVVL 7770
Cdd:cd17653     81 LPSARIQAILRTSGATLLL---------------------------------TTDS--PDDLAYIIFTSGSTGIPKGVMV 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7771 EHRAVaTSCLGHGRA-FGITNLSRVLQFASYTFDACIAEIITTLlCGGCICVPSDSDrrNSLAKAISTMDVnwAFLTPSV 7849
Cdd:cd17653    126 PHRGV-LNYVSQPPArLDVGPGSRVAQVLSIAFDACIGEIFSTL-CNGGTLVLADPS--DPFAHVARTVDA--LMSTPSI 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7850 ARLLDPGLIPSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECCIFCTgYTTKQGFEPSTIGTSVASVS-WVVDPENh 7928
Cdd:cd17653    200 LSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISST-MTELLPGQPVTIGKPIPNSTcYILDADL- 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7929 nRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAWllegypghPGRqgRLYKTGDLVQYNADGNLVYLGRKDSQV 8008
Cdd:cd17653    278 -QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW--------PGS--RMYRTGDYGRWTEDGGLEFLGREDNQV 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8009 KVRGQRVELGEVEHHVRECLPEARQLAVEVIlpsgqkNHAMLAvFVqlgkgthiahleekaggedsMAQVVFLTGTEEEL 8088
Cdd:cd17653    347 KVRGFRINLEEIEEVVLQSQPEVTQAAAIVV------NGRLVA-FV--------------------TPETVDVDGLRSEL 399
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 8089 AKRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:cd17653    400 AKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
4542-5054 3.78e-97

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 324.39  E-value: 3.78e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4542 CVHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL 4621
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4622 DPDHPASRHEHIFRQTGAQVVLAsaqyatlwtslgrsvvivseastsqlpvvtktadpsvNPGNAAYAIFTSGSTGIPKG 4701
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLT-------------------------------------QPENLAYVIYTSGSTGKPKG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4702 VVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICV------PSDSD-----RRNNLaKAIN 4770
Cdd:cd17644    124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLrpeemrSSLEDfvqyiQQWQL-TVLS 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4771 AMDVNWALLTPSVARMLDPcVVQSLKILVLGGEQVNSADWDRWPKS----IQTINAYGPTECSICCTTYS----GKQGFK 4842
Cdd:cd17644    203 LPPAYWHLLVLELLLSTID-LPSSLRLVIVGGEAVQPELVRQWQKNvgnfIQLINVYGPTEATIAATVCRltqlTERNIT 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4843 SGTIGTSIVSVSWVVDPENHnRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegyggHSGRQGRLYKTGD 4922
Cdd:cd17644    282 SVPIGRPIANTQVYILDENL-QPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPF--------NSSESERLYKTGD 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4923 LVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhhvrECLTEAKQL-AVEVIVPEGEGGYAMLAAFVqLGDDTYNTLVKE 5001
Cdd:cd17644    353 LARYLPDGNIEYLGRIDNQVKIRGFRIELGEIE----AVLSQHNDVkTAVVIVREDQPGNKRLVAYI-VPHYEESPSTVE 427
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 5002 kaggdsltvqvvfldrVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd17644    428 ----------------LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
1934-2444 1.46e-96

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 323.51  E-value: 1.46e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1934 LFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 2013
Cdd:cd17655      2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2014 PASRHEDIFRQTGAQVVVTSA--QHSARWIGTNHQVV--TVSAGSLEQFSTLVNPVDLpakpenaAYVMFTSGSTGTPKG 2089
Cdd:cd17655     82 PEERIQYILEDSGADILLTQShlQPPIAFIGLIDLLDedTIYHEESENLEPVSKSDDL-------AYVIYTSGSTGKPKG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2090 VVLEHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRDN--LAKAITDMQVNWGYL 2167
Cdd:cd17655    155 VMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGqaLTQYIRQNRITIIDL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2168 TSSVARLLDP---CLVPSLKVLVLGGEQVNSTDWGKW----PSSVQTINGYGPTECCVFCTGYTGIQGFQSGN---IGTS 2237
Cdd:cd17655    235 TPAHLKLLDAaddSEGLSLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDASIYQYEPETDQQVsvpIGKP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2238 IASVS-WVVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegYPGhegrqGRLYKTGDLVRYSS 2316
Cdd:cd17655    315 LGNTRiYILDQY--GRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-----VPG-----ERMYRTGDLARWLP 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2317 DGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVPpsgerdhamlaafirldDETRNSPLIIKYAEDNS 2396
Cdd:cd17655    383 DGNIEFLGRIDHQVKIRGYRIELGEIEARLLQ-HPDIKEAVVIARK-----------------DEQGQNYLCAYIVSEKE 444
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 2397 TAQivflTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:cd17655    445 LPV----AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
1933-2444 6.50e-96

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 319.64  E-value: 6.50e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 2012
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2013 HPASRHEDIFRQTGAQVVVTsaqhsarwigtnhqvvtvsagsleqfstlvnpvdlPAKPENAAYVMFTSGSTGTPKGVVL 2092
Cdd:cd17653     81 LPSARIQAILRTSGATLLLT-----------------------------------TDSPDDLAYIIFTSGSTGIPKGVMV 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2093 EHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGcICVPSDSErrDNLAKAITdmQVNWGYLTSSVA 2172
Cdd:cd17653    126 PHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGG-TLVLADPS--DPFAHVAR--TVDALMSTPSIL 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2173 RLLDPCLVPSLKVLVLGGEQVNSTDWGKWPSSVQTINGYGPTECCVFCTgYTGIQGFQSGNIGTSIASVS-WVVDPEnhG 2251
Cdd:cd17653    201 STLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISST-MTELLPGQPVTIGKPIPNSTcYILDAD--L 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2252 RLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAWllegyPGHegrqgRLYKTGDLVRYSSDGNLVCLGRKDSQVK 2331
Cdd:cd17653    278 QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW-----PGS-----RMYRTGDYGRWTEDGGLEFLGREDNQVK 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2332 VRGQRVELGEVEHHMRKCLPEANQLAVEVVppsGERdhamLAAFIrlddetrnspliikyaednsTAQIVFLTGIEEELS 2411
Cdd:cd17653    348 VRGFRINLEEIEEVVLQSQPEVTQAAAIVV---NGR----LVAFV--------------------TPETVDVDGLRSELA 400
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 2412 ERLPQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:cd17653    401 KHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
3148-4068 8.31e-96

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 343.56  E-value: 8.31e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3148 YLCLDINHAIIDAHSRGILMHDLQEAYDANLN----------PQSTSFRDFASYIKQQSQEEAGRYWAEYLDGVEP---- 3213
Cdd:PRK10252   134 YWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRgeptpaspftPFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPpasl 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3214 CFFPSLGDSGGANTIPRTVEVPSIDssAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTN-----PCFGNLSSgrdlPIH 3288
Cdd:PRK10252   214 SPAPLPGRSASADILRLKLEFTDGA--FRQLAAQASGVQRPDLALALVALWLGRLCGRMDyaagfIFMRRLGS----AAL 287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3289 NVNsifGPLISILPCRIHLHKQLTVLEALKTVQENYASSLSFQTFPLASMHSFLGL--GTSALFNTALSLQRID---DIG 3363
Cdd:PRK10252   288 TAT---GPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRaaGDEPLFGPVLNIKVFDyqlDFP 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3364 pcsaseitlkmkeGLDPTEYniTLSAGYSKDaidISMTFR---AGCMDL---------------VQAKRLASNFSQAIKA 3425
Cdd:PRK10252   365 -------------GVQAQTH--TLATGPVND---LELALFpdeHGGLSIeilanpqrydeatliAHAERLKALIAQFAAD 426
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3426 vttePHSRIYSLDILTYNESKKIWGWNADVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQ 3505
Cdd:PRK10252   427 ----PALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRE 502
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3506 LGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARWTssscHVVTVSKA 3585
Cdd:PRK10252   503 RGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFA----DVPDLTSL 578
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3586 LSSQLPAVVDSTNTSV-RPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEII 3664
Cdd:PRK10252   579 CYNAPLAPQGAAPLQLsQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFF 658
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3665 TTLLCGGCICV-PSDSDRR-NSLAKAISTMDVNWAFLTPS-----VARLLDPGLIPSLKILA---IGGEQSSSADWNRWP 3734
Cdd:PRK10252   659 WPFIAGAKLVMaEPEAHRDpLAMQQFFAEYGVTTTHFVPSmlaafVASLTPEGARQSCASLRqvfCSGEALPADLCREWQ 738
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3735 GSVQ-KIH-VYGPTECCIFCTGYTTKQGFEPSTIGTSVaSVSW--------VVDpeNHNRLAPLGSMGELLMEGPILARG 3804
Cdd:PRK10252   739 QLTGaPLHnLYGPTEAAVDVSWYPAFGEELAAVRGSSV-PIGYpvwntglrILD--ARMRPVPPGVAGDLYLTGIQLAQG 815
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3805 YLNDVDKTEAAFIDDPAwllegYPGhpgrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPE 3884
Cdd:PRK10252   816 YLGRPDLTASRFIADPF-----APG-----ERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQA-LPD 884
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3885 ARQ-LAVEVILPSGQK---DHAMLAAFVQLEEGtqnALLDKEAggedsmaqvvflasVEEELAKRLPEHMVPTVFFSLLH 3960
Cdd:PRK10252   885 VEQaVTHACVINQAAAtggDARQLVGYLVSQSG---LPLDTSA--------------LQAQLRERLPPHMVPVVLLQLDQ 947
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3961 FPTTTSGKTDRKRLreigasfTAQQLAemrtsSQGPKRQPSTEAEQTMQQLWAQVlsLGADIIGLDDSFFRLGGDSIAAM 4040
Cdd:PRK10252   948 LPLSANGKLDRKAL-------PLPELK-----AQVPGRAPKTGTETIIAAAFSSL--LGCDVVDADADFFALGGHSLLAM 1013
                          970       980
                   ....*....|....*....|....*....
gi 1820002560 4041 KLVGEARR-MGLHLSVADIFRHPKLADFA 4068
Cdd:PRK10252  1014 KLAAQLSRqFARQVTPGQVMVASTVAKLA 1042
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
854-1365 1.85e-95

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 318.88  E-value: 1.85e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 933
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 PGHPASRHEEIFKQIGAQVVLTssqhamlfasserhqvtvskvstsqlptvvnfakspvDPGNTAYIIFTSGTTGIPKGV 1013
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLT-------------------------------------DPDDLAYVIYTSGSTGRPKGV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1014 VLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCIcVPSES--DRRNNLAKAISTMdVNCallT 1091
Cdd:cd12115    124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKV-VLADNvlALPDLPAAAEVTL-INT---V 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1092 PSVAR-LLEPSAVP-SLKRLVLQGE---QVSFADWNRWPGSVQTINGYGPTECSvccnTYS-----GKQGFKSGIIGTSV 1161
Cdd:cd12115    199 PSAAAeLLRHDALPaSVRVVNLAGEplpRDLVQRLYARLQVERVVNLYGPSEDT----TYStvapvPPGASGEVSIGRPL 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1162 A-SLSWVVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAwllegyegHAGRRgrLYKTGDLVRCDAD 1240
Cdd:cd12115    275 AnTQAYVLDR--ALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF--------GPGAR--LYRTGDLVRWRPD 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1241 GNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQlAVeVILPSGQKEHALLAAFIQLDKGnhnalfeekasgedsm 1320
Cdd:cd12115    343 GLLEFLGRADNQVKVRGFRIELGEIEAALRS-IPGVRE-AV-VVAIGDAAGERRLVAYIVAEPG---------------- 403
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 1321 aQVVFLTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd12115    404 -AAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
3463-3974 5.38e-95

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 317.34  E-value: 5.38e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3463 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 3542
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3543 PDHPASRHEEIFEQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsVRPENAAYIIFTSGSTGVPKGV 3622
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVL-------------------------------------TDPDDLAYVIYTSGSTGRPKGV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3623 VLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNwafLTPS 3702
Cdd:cd12115    124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAAEVTLIN---TVPS 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3703 VAR-LLDPGLIP-SLKILAIGGEQSSS---ADWNRWPGSVQKIHVYGPTECCIFCTGY-TTKQGFEPSTIGTSVA-SVSW 3775
Cdd:cd12115    201 AAAeLLRHDALPaSVRVVNLAGEPLPRdlvQRLYARLQVERVVNLYGPSEDTTYSTVApVPPGASGEVSIGRPLAnTQAY 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3776 VVDpeNHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypgHPGRqgRLYKTGDLVQYNADGNLVYL 3855
Cdd:cd12115    281 VLD--RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF--------GPGA--RLYRTGDLVRWRPDGLLEFL 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3856 GRKDSQVKVRGQRVELGEVEHHVREcLPEARQlAVeVILPSGQKDHAMLAAFVQLEEGTQnalldkeaggedsmaqvVFL 3935
Cdd:cd12115    349 GRADNQVKVRGFRIELGEIEAALRS-IPGVRE-AV-VVAIGDAAGERRLVAYIVAEPGAA-----------------GLV 408
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1820002560 3936 ASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd12115    409 EDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
3462-3974 7.79e-95

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 317.84  E-value: 7.79e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3462 CVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL 3541
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3542 DPDHPASRHEEIFEQTGAQVVVAsaqysarwtssschvvtvskalssqlpavvdstntsvRPENAAYIIFTSGSTGVPKG 3621
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLT-------------------------------------QPENLAYVIYTSGSTGKPKG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3622 VVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGC-ICVPsdsdrrnslAKAISTMDVNWAF-- 3698
Cdd:cd17644    124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATlVLRP---------EEMRSSLEDFVQYiq 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3699 --------LTPSVARLLDPGLIP-------SLKILAIGGEQSSSADWNRWPGSVQK----IHVYGPTECCI---FC--TG 3754
Cdd:cd17644    195 qwqltvlsLPPAYWHLLVLELLLstidlpsSLRLVIVGGEAVQPELVRQWQKNVGNfiqlINVYGPTEATIaatVCrlTQ 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3755 YTTKQGFEPsTIGTSVASVSWVVDPENHnRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPawllegYPGHPGRq 3834
Cdd:cd17644    275 LTERNITSV-PIGRPIANTQVYILDENL-QPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHP------FNSSESE- 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3835 gRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE------HHVRECLPEARQlaveviLPSGQKdhaMLAAFV 3908
Cdd:cd17644    346 -RLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEavlsqhNDVKTAVVIVRE------DQPGNK---RLVAYI 415
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 3909 qleegtqnalldkeaggedsMAQVVFLASVEEE---LAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd17644    416 --------------------VPHYEESPSTVELrqfLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
5623-6135 1.02e-93

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 314.37  E-value: 1.02e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5623 CVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL 5702
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5703 DPDHPASRHEDTFRHTGAQVVVTSaqhsarwigtnhqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKG 5782
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLTQ-------------------------------------PENLAYVIYTSGSTGKPKG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5783 VVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRN--DLVKAISTMDVSCALL 5860
Cdd:cd17644    124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSleDFVQYIQQWQLTVLSL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5861 TPSVARLL------EPSSVP-TLQMLVLQGEQVSFADWNRWPASV----QTINGYGPTECSI---CCN-TYSGKQGFKSG 5925
Cdd:cd17644    204 PPAYWHLLvlelllSTIDLPsSLRLVIVGGEAVQPELVRQWQKNVgnfiQLINVYGPTEATIaatVCRlTQLTERNITSV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5926 IIGTSVASVSWVVDPENHdRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPawllegYPGHPGRqgRLYKTGDLV 6005
Cdd:cd17644    284 PIGRPIANTQVYILDENL-QPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHP------FNSSESE--RLYKTGDLA 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6006 RYDANGNLVCLGRKDSQVKLRGQRVELGEVE------HHVRECLPEARQlaveviLPSGQKdhaMLAAFVqleegtqnal 6079
Cdd:cd17644    355 RYLPDGNIEYLGRIDNQVKIRGFRIELGEIEavlsqhNDVKTAVVIVRE------DQPGNK---RLVAYI---------- 415
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 6080 ldkeasgedsMAQVVFLASVEEE---LAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd17644    416 ----------VPHYEESPSTVELrqfLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
5624-6135 1.22e-93

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 313.48  E-value: 1.22e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5624 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 5703
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5704 PDHPASRHEDTFRHTGAQVVVTSAQHSArwigtnhqvvtvsagslgqlstlvnpvglpaipenavYIMFTSGSTGIPKGV 5783
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLTDPDDLA-------------------------------------YVIYTSGSTGRPKGV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5784 VLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCIcVPSDSDRrnDLVKAISTMDVSCALLTPS 5863
Cdd:cd12115    124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKV-VLADNVL--ALPDLPAAAEVTLINTVPS 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5864 VAR-LLEPSSVPT-LQMLVLQGE---QVSFADWNRWPASVQTINGYGPTECSiccnTYS-----GKQGFKSGIIGTSVA- 5932
Cdd:cd12115    201 AAAeLLRHDALPAsVRVVNLAGEplpRDLVQRLYARLQVERVVNLYGPSEDT----TYStvapvPPGASGEVSIGRPLAn 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5933 SVSWVVDpeNHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypgHPGRqgRLYKTGDLVRYDANGN 6012
Cdd:cd12115    277 TQAYVLD--RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF--------GPGA--RLYRTGDLVRWRPDGL 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6013 LVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQlAVeVILPSGQKDHAMLAAFVQLEEGTQnalldkeasgedsmaq 6092
Cdd:cd12115    345 LEFLGRADNQVKVRGFRIELGEIEAALRS-IPGVRE-AV-VVAIGDAAGERRLVAYIVAEPGAA---------------- 405
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 6093 vVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd12115    406 -GLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
7608-8120 1.40e-93

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 313.99  E-value: 1.40e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7608 CVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL 7687
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7688 DPDHPASRHEEIFEQTGAQVVVAsaqysarwtssschvvtvskalssqlpavvdstntsvRPENAAYIIFTSGSTGVPKG 7767
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLT-------------------------------------QPENLAYVIYTSGSTGKPKG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7768 VVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGC-ICVPsdsdrrnslAKAISTMDVNWAF-- 7844
Cdd:cd17644    124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATlVLRP---------EEMRSSLEDFVQYiq 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7845 --------LTPSVARLLDPGLIP-------SLKILAIGGEQSSSADWNRWPGSVQK----IHVYGPTECCI---FC--TG 7900
Cdd:cd17644    195 qwqltvlsLPPAYWHLLVLELLLstidlpsSLRLVIVGGEAVQPELVRQWQKNVGNfiqlINVYGPTEATIaatVCrlTQ 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7901 YTTKQGFEPsTIGTSVASVSWVVDPENHnRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPawllegYPGHPGRq 7980
Cdd:cd17644    275 LTERNITSV-PIGRPIANTQVYILDENL-QPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHP------FNSSESE- 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7981 gRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE------HHVREclpearqlaVEVILPSGQKNHAMLAVFV 8054
Cdd:cd17644    346 -RLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEavlsqhNDVKT---------AVVIVREDQPGNKRLVAYI 415
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 8055 qlgkgthIAHLEEkaggEDSMAQVvfltgtEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd17644    416 -------VPHYEE----SPSTVEL------RQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
PRK05691 PRK05691
peptide synthase; Validated
4107-5161 1.52e-93

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 344.07  E-value: 1.52e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4107 VDASAITDVYPCSPLQEGLM--SLTAKRAGDYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELGLLQVVV 4184
Cdd:PRK05691  3249 VPAAEIEDVYPLTPMQEGLLlhTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIH 3328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4185 EE---RIQWTESESLEEYPREDKAVSMGVGDRLARYALIKEP--------YDGGKRWFVWTMHHALYDGWSLPRILHAVK 4253
Cdd:PRK05691  3329 KPgrtPIDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPpfhlrlirVDEARYWFMMSNHHILIDAWCRSLLMNDFF 3408
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4254 QAYSGVVLERQ------PSFNAFIQYLSQQDPEAAAAYWQTALVDCKAalfPTLPPTvTQP-------------VADTTV 4314
Cdd:PRK05691  3409 EIYTALGEGREaqlpvpPRYRDYIGWLQRQDLAQARQWWQDNLRGFER---PTPIPS-DRPflrehagdsggmvVGDCYT 3484
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4315 EYQCPPPSQ-----SATDITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQ- 4388
Cdd:PRK05691  3485 RLDAADGARlrelaQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLPAAGq 3564
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4389 --TVFAFLQGVQQQATDMIAHEQTGLQRIAKMSPGARHACGFQTLLVVQ--PTD-DVLGSDDMLGEwrSYSEMQDFTTYA 4463
Cdd:PRK05691  3565 rcSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGQPLFDSLFVFEnaPVEvSVLDRAQSLNA--SSDSGRTHTNFP 3642
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4464 LMVQCvLVKDRVGVTASFDARVIEQWVVEKMLRQFGFVMQQLADaGEEKKVAGIETTTTGDRQQLW-AWNQ---DVPpaI 4539
Cdd:PRK05691  3643 LTAVC-YPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQ-GFHGDLSELPLLGEQERDFLLdGCNRserDYP--L 3718
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4540 ERCVHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFV 4619
Cdd:PRK05691  3719 EQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYL 3798
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4620 PLDPDHPASRHEHIFRQTGAQVVLASAQYATLWTSLgrsVVIVSEASTSQLPV---VTKTADPSVNPG------NAAYAI 4690
Cdd:PRK05691  3799 PLDPGLPAQRLQRIIELSRTPVLVCSAACREQARAL---LDELGCANRPRLLVweeVQAGEVASHNPGiysgpdNLAYVI 3875
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4691 FTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCI-CVPSDSDRR-NNLAKA 4768
Cdd:PRK05691  3876 YTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVeIVPNAIAHDpQGLLAH 3955
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4769 INAMDVNWALLTPS-VARML--DPCVVQSLKILVLGGEQVN---SADW-DRWPKsIQTINAYGPTECSICCTTYSGKQGF 4841
Cdd:PRK05691  3956 VQAQGITVLESVPSlIQGMLaeDRQALDGLRWMLPTGEAMPpelARQWlQRYPQ-IGLVNAYGPAECSDDVAFFRVDLAS 4034
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4842 KSGT---IGTsivsvswvvdPENHNRL---------APLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawllegygg 4909
Cdd:PRK05691  4035 TRGSylpIGS----------PTDNNRLylldealelVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHP--------- 4095
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4910 HSGRQGRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREcLTEAKQLAveVIVPEGEGGYAMLAAFVq 4989
Cdd:PRK05691  4096 FGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE-QAEVREAA--VAVQEGVNGKHLVGYLV- 4171
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4990 lgddtyntlvkekaGGDSLTVQVVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLR--EIGASFTAQQLA 5067
Cdd:PRK05691  4172 --------------PHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPalDIGQLQSQAYLA 4237
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5068 emrtssqgpkrqPSTEAERTMQQLWTRVLGIElnGIGLDDSFFRLGGDSIAAMKLVGEARRTgLQLSVA--DVFRHPRLV 5145
Cdd:PRK05691  4238 ------------PRNELEQTLATIWADVLKVE--RVGVHDNFFELGGHSLLATQIASRVQKA-LQRNVPlrAMFECSTVE 4302
                         1130
                   ....*....|....*..
gi 1820002560 5146 DLA-YVQNSECSSAAEE 5161
Cdd:PRK05691  4303 ELAeYIEGLAGSAIDEQ 4319
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
853-1365 3.45e-93

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 312.83  E-value: 3.45e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  853 CIHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL 932
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  933 DPGHPASRHEEIFKQIGAQVVLTSsqhamlfasserhqvtvskvstsqlptvvnfakspvdPGNTAYIIFTSGTTGIPKG 1012
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLTQ-------------------------------------PENLAYVIYTSGSTGKPKG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1013 VVLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRN--NLAKAISTMDVNCALL 1090
Cdd:cd17644    124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSleDFVQYIQQWQLTVLSL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1091 TPSVARLL------EPSAVPSLKRLVLQG-EQVSFADWNRW----PGSVQTINGYGPTECSV---CCN-TYSGKQGFKSG 1155
Cdd:cd17644    204 PPAYWHLLvlelllSTIDLPSSLRLVIVGgEAVQPELVRQWqknvGNFIQLINVYGPTEATIaatVCRlTQLTERNITSV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1156 IIGTSVASLS-WVVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawlLEGYEGHagrrgRLYKTGDL 1234
Cdd:cd17644    284 PIGRPIANTQvYILDE--NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHP---FNSSESE-----RLYKTGDL 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1235 VRCDADGNLVCLGRKDSQVKVRGQRVELGEIE------HHVRECLPEARQlaveviLPSGQKEhalLAAFIQLDKGNHNA 1308
Cdd:cd17644    354 ARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEavlsqhNDVKTAVVIVRE------DQPGNKR---LVAYIVPHYEESPS 424
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 1309 LFEekasgedsmaqvvfltgVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17644    425 TVE-----------------LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
862-1365 5.13e-93

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 311.87  E-value: 5.13e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  862 ARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRH 941
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  942 EEIFKQIGAQVVLtssqhamlfasserhqvtvskvstsqlptvvnfakspVDPGNTAYIIFTSGTTGIPKGVVLQHRAVT 1021
Cdd:cd05945     81 REILDAAKPALLI-------------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDNLV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1022 TSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGC-ICVPSE-SDRRNNLAKAISTMDVNCALLTPSVARLLE 1099
Cdd:cd05945    124 SFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDaTADPKQLFRFLAEHGITVWVSTPSFAAMCL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1100 ------PSAVPSLKRLVLQGEQVSFADWNRW----PGSVqTINGYGPTECSVCCNTYSGKQ----GFKSGIIGTSVASLS 1165
Cdd:cd05945    204 lsptftPESLPSLRHFLFCGEVLPHKTARALqqrfPDAR-IYNTYGPTEATVAVTYIEVTPevldGYDRLPIGYAKPGAK 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1166 -WVVDAGNhnRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawllegyeghaGRRGrlYKTGDLVRCDADGNLV 1244
Cdd:cd05945    283 lVILDEDG--RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-----------GQRA--YRTGDLVRLEADGLLF 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1245 CLGRKDSQVKVRGQRVELGEIEHHVREClPEARQlAVEVILPSGQKeHALLAAFIQLDKGnhnalfeekasgedsmAQVV 1324
Cdd:cd05945    348 YRGRLDFQVKLNGYRIELEEIEAALRQV-PGVKE-AVVVPKYKGEK-VTELIAFVVPKPG----------------AEAG 408
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 1325 FLTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd05945    409 LTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
866-1365 1.27e-92

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 311.53  E-value: 1.27e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  866 PDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIF 945
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  946 KQIGAQVVLTSSQHAMLFAsserHQVTVSKVSTSQLPTVVNFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCL 1025
Cdd:cd12116     81 EDAEPALVLTDDALPDRLP----AGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1026 GHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRN--NLAKAISTMDVNCALLTPSVARLL---EP 1100
Cdd:cd12116    157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDpeALARLIEAHSITVMQATPATWRMLldaGW 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1101 SAVPSLKRLV--------LQGEQVSFAdwnrwpGSVqtINGYGPTEC---SVCCNTYSGKQGFKSG--IIGTSVaslsWV 1167
Cdd:cd12116    237 QGRAGLTALCggealppdLAARLLSRV------GSL--WNLYGPTETtiwSTAARVTAAAGPIPIGrpLANTQV----YV 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1168 VDAGnhNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawllegyegHAGRRGRLYKTGDLVRCDADGNLVCLG 1247
Cdd:cd12116    305 LDAA--LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDP---------FAGPGSRLYRTGDLVRRRADGRLEYLG 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1248 RKDSQVKVRGQRVELGEIEHHVREcLPEARQLAVeVILPSGQKEHalLAAFIQLDkgnHNALFEEKAsgedsmaqvvflt 1327
Cdd:cd12116    374 RADGQVKIRGHRIELGEIEAALAA-HPGVAQAAV-VVREDGGDRR--LVAYVVLK---AGAAPDAAA------------- 433
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 1328 gVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd12116    434 -LRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
5627-6137 1.70e-92

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 311.95  E-value: 1.70e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5627 LFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 5706
Cdd:cd17655      2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5707 PASRHEDTFRHTGAQVVVTSA--QHSARWIGTNHQVV--TVSAGSLGQLSTLVNPVGLpaipenaVYIMFTSGSTGIPKG 5782
Cdd:cd17655     82 PEERIQYILEDSGADILLTQShlQPPIAFIGLIDLLDedTIYHEESENLEPVSKSDDL-------AYVIYTSGSTGKPKG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5783 VVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRND--LVKAISTMDVSCALL 5860
Cdd:cd17655    155 VMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGqaLTQYIRQNRITIIDL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5861 TPSVARLLEP---SSVPTLQMLVLQGEQVSFADWNRW----PASVQTINGYGPTECSICCNTY---SGKQGFKSGIIGTS 5930
Cdd:cd17655    235 TPAHLKLLDAaddSEGLSLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDASIYqyePETDQQVSVPIGKP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5931 VASVS-WVVDPENhdRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegYPGhpgrqGRLYKTGDLVRYDA 6009
Cdd:cd17655    315 LGNTRiYILDQYG--RPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-----VPG-----ERMYRTGDLARWLP 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6010 NGNLVCLGRKDSQVKLRGQRVELGEVEHhvRECLPEARQLAVEVILPSGQKDHAMLAAFVQLEEGTQnalldkeasgeds 6089
Cdd:cd17655    383 DGNIEFLGRIDHQVKIRGYRIELGEIEA--RLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPV------------- 447
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 6090 maqvvflASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:cd17655    448 -------AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
4543-5054 5.26e-92

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 308.86  E-value: 5.26e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4543 VHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 4622
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4623 PDHPASRHEHIFRQTGAQVVLasaqyatlwtslgrsvvivseastsqlpvvtktadpsVNPGNAAYAIFTSGSTGIPKGV 4702
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVL-------------------------------------TDPDDLAYVIYTSGSTGRPKGV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4703 VLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLAKAINAMDVNwalLTPS 4782
Cdd:cd12115    124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAAEVTLIN---TVPS 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4783 VARML---DPcVVQSLKILVLGGEQVNS---ADWDRWPKSIQTINAYGPTECsiccTTYS-----GKQGFKSGTIGTSIV 4851
Cdd:cd12115    201 AAAELlrhDA-LPASVRVVNLAGEPLPRdlvQRLYARLQVERVVNLYGPSED----TTYStvapvPPGASGEVSIGRPLA 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4852 -SVSWVVDpeNHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegyggHSGRqgRLYKTGDLVRYDADG 4930
Cdd:cd12115    276 nTQAYVLD--RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF--------GPGA--RLYRTGDLVRWRPDG 343
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4931 NLVYLGRKDSQVKLRGQRVELGEVEHhvreCLTEAKQLAVEVIV-PEGEGGYAMLAAFVQLgddtyntlvkeKAGGDSLt 5009
Cdd:cd12115    344 LLEFLGRADNQVKVRGFRIELGEIEA----ALRSIPGVREAVVVaIGDAAGERRLVAYIVA-----------EPGAAGL- 407
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 5010 vqvvfLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd12115    408 -----VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
7609-8120 8.67e-92

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 308.09  E-value: 8.67e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7609 VHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 7688
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7689 PDHPASRHEEIFEQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsVRPENAAYIIFTSGSTGVPKGV 7768
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVL-------------------------------------TDPDDLAYVIYTSGSTGRPKGV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7769 VLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNwafLTPS 7848
Cdd:cd12115    124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAAEVTLIN---TVPS 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7849 VAR-LLDPGLIP-SLKILAIGGEQSSS---ADWNRWPGSVQKIHVYGPTECCIFCTGY-TTKQGFEPSTIGTSVA-SVSW 7921
Cdd:cd12115    201 AAAeLLRHDALPaSVRVVNLAGEPLPRdlvQRLYARLQVERVVNLYGPSEDTTYSTVApVPPGASGEVSIGRPLAnTQAY 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7922 VVDpeNHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypgHPGRqgRLYKTGDLVQYNADGNLVYL 8001
Cdd:cd12115    281 VLD--RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF--------GPGA--RLYRTGDLVRWRPDGLLEFL 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8002 GRKDSQVKVRGQRVELGEVEHHVREcLPEARQlAVeVILPSGQKNHAMLAVFVQLGKGTHIAhleekaggedsmaqvvfL 8081
Cdd:cd12115    349 GRADNQVKVRGFRIELGEIEAALRS-IPGVRE-AV-VVAIGDAAGERRLVAYIVAEPGAAGL-----------------V 408
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1820002560 8082 TGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd12115    409 EDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
5636-6135 5.47e-91

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 306.91  E-value: 5.47e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5636 PHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTF 5715
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5716 RHTGAQVVVTSAQHSARWIGTnhqvVTVSAGSLGQLSTLVNPVGLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCW 5795
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAG----LPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5796 GRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRN--DLVKAISTMDVSCALLTPSVARLL---EP 5870
Cdd:cd12116    157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDpeALARLIEAHSITVMQATPATWRMLldaGW 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5871 SSVPTLQMLVlQGEQVS------FADwnrwpASVQTINGYGPTECSIcCNTYSGKQGFKSGI-IGTSVASVS-WVVDPEN 5942
Cdd:cd12116    237 QGRAGLTALC-GGEALPpdlaarLLS-----RVGSLWNLYGPTETTI-WSTAARVTAAAGPIpIGRPLANTQvYVLDAAL 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5943 hdRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypGHPGrqGRLYKTGDLVRYDANGNLVCLGRKDSQ 6022
Cdd:cd12116    310 --RPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPF-------AGPG--SRLYRTGDLVRRRADGRLEYLGRADGQ 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6023 VKLRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHamLAAFVQLEEGtqnALLDKEAsgedsmaqvvflasVEEE 6102
Cdd:cd12116    379 VKIRGHRIELGEIEAALAA-HPGVAQAAV-VVREDGGDRR--LVAYVVLKAG---AAPDAAA--------------LRAH 437
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 6103 LAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd12116    438 LRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
1931-2442 7.16e-91

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 305.78  E-value: 7.16e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1931 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 2010
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2011 PDHPASRHEDIFRQTGAQVVVTsaqhsarwigtnhqvvtvsagsleqfstlvnpvdlpaKPENAAYVMFTSGSTGTPKGV 2090
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLT-------------------------------------DPDDLAYVIYTSGSTGRPKGV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2091 VLEHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCIcVPSDS--ERRDNLAKAITDMqVNwgYLT 2168
Cdd:cd12115    124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKV-VLADNvlALPDLPAAAEVTL-IN--TVP 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2169 SSVARLLD-PCLVPSLKVLVLGGEQVNST---DWGKWPSSVQTINGYGPTECCVFCTGY-TGIQGFQSGNIGTSIA-SVS 2242
Cdd:cd12115    200 SAAAELLRhDALPASVRVVNLAGEPLPRDlvqRLYARLQVERVVNLYGPSEDTTYSTVApVPPGASGEVSIGRPLAnTQA 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2243 WVVDpeNHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegypgHEGRqgRLYKTGDLVRYSSDGNLVC 2322
Cdd:cd12115    280 YVLD--RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF--------GPGA--RLYRTGDLVRWRPDGLLEF 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2323 LGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQlAVeVVPPSGERDHAMLAAFIRLDDetrnspliikyaednstAQIVF 2402
Cdd:cd12115    348 LGRADNQVKVRGFRIELGEIEAALRS-IPGVRE-AV-VVAIGDAAGERRLVAYIVAEP-----------------GAAGL 407
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 2403 LTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd12115    408 VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
1943-2442 1.56e-89

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 301.92  E-value: 1.56e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1943 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIF 2022
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2023 RQTGAQVVVTsaqhsarwigtnhqvvtvsagsleqfstlvnpvdlpaKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCL 2102
Cdd:cd17643     81 ADSGPSLLLT-------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2103 GHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSSVARLLDPCL- 2179
Cdd:cd17643    124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSpeDFARLLRDEGVTVLNQTPSAFYQLVEAAd 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2180 -----VPSLKVLVLGGEQVNSTDWGKW-----PSSVQTINGYGPTECCVFCTGY----TGIQGFQSGNIGTSIASVSW-V 2244
Cdd:cd17643    204 rdgrdPLALRYVIFGGEALEAAMLRPWagrfgLDRPQLVNMYGITETTVHVTFRpldaADLPAAAASPIGRPLPGLRVyV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2245 VDpeNHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegypGHEGRqgRLYKTGDLVRYSSDGNLVCLG 2324
Cdd:cd17643    284 LD--ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF-------GGPGS--RMYRTGDLARRLPDGELEYLG 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2325 RKDSQVKVRGQRVELGEVEHHMRKClPEANQLAVeVVPPSGERDHAMLAAFIrlddetrnspliikyAEDNSTAQIvflT 2404
Cdd:cd17643    353 RADEQVKIRGFRIELGEIEAALATH-PSVRDAAV-IVREDEPGDTRLVAYVV---------------ADDGAAADI---A 412
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 2405 GIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd17643    413 ELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
3471-3974 1.64e-89

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 301.86  E-value: 1.64e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 3550
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3551 EEIfeqtgaqvvVASAQysarwtssschvvtvskalssqlPAVVDSTNTSVrpenaAYIIFTSGSTGVPKGVVLEHRAVA 3630
Cdd:cd05945     81 REI---------LDAAK-----------------------PALLIADGDDN-----AYIIFTSGSTGRPKGVQISHDNLV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3631 tSCLGHGRA-FGITNLSRVLQFASYTFDACIAEIITTLLCGGC-ICVPSD-SDRRNSLAKAISTMDVNWAFLTPSVARL- 3706
Cdd:cd05945    124 -SFTNWMLSdFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDaTADPKQLFRFLAEHGITVWVSTPSFAAMc 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3707 -----LDPGLIPSLKILAIGGEQ---SSSADW-NRWPGSVqKIHVYGPTECCIFCTGYTTKQ----GFEPSTIGTSVASV 3773
Cdd:cd05945    203 llsptFTPESLPSLRHFLFCGEVlphKTARALqQRFPDAR-IYNTYGPTEATVAVTYIEVTPevldGYDRLPIGYAKPGA 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3774 S-WVVDPENhnRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAWllegypghpgrqgRLYKTGDLVQYNADGNL 3852
Cdd:cd05945    282 KlVILDEDG--RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQ-------------RAYRTGDLVRLEADGLL 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3853 VYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQlAVEVILPSGQKdHAMLAAFVQLEEGTQNALLDkeaggedsmaqv 3932
Cdd:cd05945    347 FYRGRLDFQVKLNGYRIELEEIEAALRQV-PGVKE-AVVVPKYKGEK-VTELIAFVVPKPGAEAGLTK------------ 411
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 3933 vflaSVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd05945    412 ----AIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
PRK05691 PRK05691
peptide synthase; Validated
5176-6216 4.08e-89

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 329.44  E-value: 4.08e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5176 AQVSQDAAAMCSVDASSVEDMYPCSPLQEGLM--SLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIV 5253
Cdd:PRK05691  3237 AQLTQAQLDALPVPAAEIEDVYPLTPMQEGLLlhTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFS 3316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5254 QHSELGLLQVVVEE---KIQWTESKRLEEYLREDKAVSMGLGDRLARYALIKEP--------YDGGKRWFVWTIHHALYD 5322
Cdd:PRK05691  3317 WNAGETMLQVIHKPgrtPIDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPpfhlrlirVDEARYWFMMSNHHILID 3396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5323 GWSLPRILQAVKQIYSGAVPERQ------PSFNAFIQYLGQQDLEAATLYWQTALADCKAalfPTLPPTvTQP------- 5389
Cdd:PRK05691  3397 AWCRSLLMNDFFEIYTALGEGREaqlpvpPRYRDYIGWLQRQDLAQARQWWQDNLRGFER---PTPIPS-DRPflrehag 3472
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5390 ------VADTTVEYQCPPPSQ-----SATDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGVEAMVGPTIAT 5458
Cdd:PRK05691  3473 dsggmvVGDCYTRLDAADGARlrelaQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINS 3552
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5459 VPLRVCLQKDQ---TVSTLLECLQQQSTDMIAHEQTGLQRIAKMSPGARHACGFQTLLVVQ--PTD-DVLGSDDMLGEwr 5532
Cdd:PRK05691  3553 IALRVQLPAAGqrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGQPLFDSLFVFEnaPVEvSVLDRAQSLNA-- 3630
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5533 SYSEMQDFTTYALMVQCTLAKDrVEVTASFDARVIEQWVVEKMLRQFGFVMQQLAEaGAEKTVSDIETTTLEDRQQLW-A 5611
Cdd:PRK05691  3631 SSDSGRTHTNFPLTAVCYPGDD-LGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQ-GFHGDLSELPLLGEQERDFLLdG 3708
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5612 WNQ---NVPpaIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVA 5688
Cdd:PRK05691  3709 CNRserDYP--LEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGM 3786
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5689 MLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSAQHSARwigtNHQVVTVSAGSlGQLSTLV------------N 5756
Cdd:PRK05691  3787 IVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQ----ARALLDELGCA-NRPRLLVweevqagevashN 3861
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5757 PvGLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGcicv 5836
Cdd:PRK05691  3862 P-GIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGA---- 3936
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5837 psdsdrRNDLVKAISTMDVScALLTPSVAR---LLEpsSVPTLQMLVLQGEQVSF------------------ADW-NRW 5894
Cdd:PRK05691  3937 ------RVEIVPNAIAHDPQ-GLLAHVQAQgitVLE--SVPSLIQGMLAEDRQALdglrwmlptgeamppelaRQWlQRY 4007
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5895 PAsVQTINGYGPTECSICCNTYSGKQGFKSGI---IGTsvasvswvvdPENHDR---------LAPLGSIGELLVEGPIL 5962
Cdd:PRK05691  4008 PQ-IGLVNAYGPAECSDDVAFFRVDLASTRGSylpIGS----------PTDNNRlylldealeLVPLGAVGELCVAGTGV 4076
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5963 ARGYLNDIQKTAAVFIDDPAwllegypGHPGRqgRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREc 6042
Cdd:PRK05691  4077 GRGYVGDPLRTALAFVPHPF-------GAPGE--RLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE- 4146
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6043 LPEARQLAVEVIL-PSGQkdhaMLAAFVQLEEGTQN--ALLDKeasgedsmaqvvflasVEEELAKRLPEHMVPTVFFSL 6119
Cdd:PRK05691  4147 QAEVREAAVAVQEgVNGK----HLVGYLVPHQTVLAqgALLER----------------IKQRLRAELPDYMVPLHWLWL 4206
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6120 LHFPTTTSGKTDRKRLREIgasftaqQIANMQtsSQDpKRQPSTEAEQTMQKLWAQVLGIElnGIGLDDSFFRLGGDSIA 6199
Cdd:PRK05691  4207 DRLPLNANGKLDRKALPAL-------DIGQLQ--SQA-YLAPRNELEQTLATIWADVLKVE--RVGVHDNFFELGGHSLL 4274
                         1130
                   ....*....|....*..
gi 1820002560 6200 AMKLVGEARRIgLQLSV 6216
Cdd:PRK05691  4275 ATQIASRVQKA-LQRNV 4290
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
866-1365 4.32e-89

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 300.38  E-value: 4.32e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  866 PDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIF 945
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  946 KQIGAQVVLTssqhamlfasserhqvtvskvstsqlptvvnfakspvDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCL 1025
Cdd:cd17643     81 ADSGPSLLLT-------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1026 GHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNNLAKAISTMDVNCALL--TPSVARLL----- 1098
Cdd:cd17643    124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLnqTPSAFYQLveaad 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1099 -EPSAVPSLKRLVLQGEQVSFADWNRWPG-----SVQTINGYGPTECSVcCNTY-----SGKQGFKSGIIGTSVASLSW- 1166
Cdd:cd17643    204 rDGRDPLALRYVIFGGEALEAAMLRPWAGrfgldRPQLVNMYGITETTV-HVTFrpldaADLPAAAASPIGRPLPGLRVy 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1167 VVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAwllegyeGHAGRrgRLYKTGDLVRCDADGNLVCL 1246
Cdd:cd17643    283 VLDA--DGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF-------GGPGS--RMYRTGDLARRLPDGELEYL 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1247 GRKDSQVKVRGQRVELGEIEHHVREClPEARQLAVeVILPSGQKEHALLAAFIqldkgnhnalfeekasGEDSMAQVVfl 1326
Cdd:cd17643    352 GRADEQVKIRGFRIELGEIEAALATH-PSVRDAAV-IVREDEPGDTRLVAYVV----------------ADDGAAADI-- 411
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1820002560 1327 TGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17643    412 AELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
3475-3974 5.14e-88

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 297.30  E-value: 5.14e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 3634
Cdd:cd17643     81 ADSGPSLLL-------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3635 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLLDPGL- 3711
Cdd:cd17643    124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSpeDFARLLRDEGVTVLNQTPSAFYQLVEAAd 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3712 -----IPSLKILAIGGEQ---SSSADWNRWPG--SVQKIHVYGPTECCIFCTGY----TTKQGFEPSTIGTSVASVSW-V 3776
Cdd:cd17643    204 rdgrdPLALRYVIFGGEAleaAMLRPWAGRFGldRPQLVNMYGITETTVHVTFRpldaADLPAAAASPIGRPLPGLRVyV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3777 VDpeNHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGRqgRLYKTGDLVQYNADGNLVYLG 3856
Cdd:cd17643    284 LD--ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF-------GGPGS--RMYRTGDLARRLPDGELEYLG 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3857 RKDSQVKVRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKDHAMLAAFVQLEEGTQNAlldkeaggedsmaqvvflA 3936
Cdd:cd17643    353 RADEQVKIRGFRIELGEIEAALATH-PSVRDAAV-IVREDEPGDTRLVAYVVADDGAAADI------------------A 412
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 3937 SVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd17643    413 ELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
5632-6135 1.54e-87

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 296.08  E-value: 1.54e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 5711
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5712 EDTFRHTGAQVVVTsaqhsarwigtnhqvvtvsAGSlgqlstlvnpvglpaipENAvYIMFTSGSTGIPKGVVLEHRAVV 5791
Cdd:cd05945     81 REILDAAKPALLIA-------------------DGD-----------------DNA-YIIFTSGSTGRPKGVQISHDNLV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5792 T-SCWGRGRaFGITNLSRVLQFASYTFDACMDEIITTLMYGGC-ICVPSD-SDRRNDLVKAISTMDVSCALLTPSVARLL 5868
Cdd:cd05945    124 SfTNWMLSD-FPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDaTADPKQLFRFLAEHGITVWVSTPSFAAMC 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5869 E------PSSVPTLQMLVLQGEQVSFADWNRW----PASVqTINGYGPTECSICCNTYSGKQ----GFKSGIIGTSVASV 5934
Cdd:cd05945    203 LlsptftPESLPSLRHFLFCGEVLPHKTARALqqrfPDAR-IYNTYGPTEATVAVTYIEVTPevldGYDRLPIGYAKPGA 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5935 S-WVVDPENhdRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAWllegypghpgrqgRLYKTGDLVRYDANGNL 6013
Cdd:cd05945    282 KlVILDEDG--RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQ-------------RAYRTGDLVRLEADGLL 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6014 VCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQlAVEVILPSGQKdHAMLAAFVQLEEGTQNALLDkeasgedsmaqv 6093
Cdd:cd05945    347 FYRGRLDFQVKLNGYRIELEEIEAALRQV-PGVKE-AVVVPKYKGEK-VTELIAFVVPKPGAEAGLTK------------ 411
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 6094 vflaSVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd05945    412 ----AIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
1939-2442 2.79e-87

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 295.31  E-value: 2.79e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 2018
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2019 EDIFRQTGAQVVvtsaqhsarwigtnhqvvtvsagsleqfstLVNPVDLpakpenaAYVMFTSGSTGTPKGVVLEHRAVV 2098
Cdd:cd05945     81 REILDAAKPALL------------------------------IADGDDN-------AYIIFTSGSTGRPKGVQISHDNLV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2099 TSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSSVARL-- 2174
Cdd:cd05945    124 SFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADpkQLFRFLAEHGITVWVSTPSFAAMcl 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2175 ----LDPCLVPSLKVLVLGGEQVNSTDWGKW----PSSVqTINGYGPTECCVFCTGY----TGIQGFQSGNIGTSIASVS 2242
Cdd:cd05945    204 lsptFTPESLPSLRHFLFCGEVLPHKTARALqqrfPDAR-IYNTYGPTEATVAVTYIevtpEVLDGYDRLPIGYAKPGAK 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2243 -WVVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAWllegypghegrqgRLYKTGDLVRYSSDGNLV 2321
Cdd:cd05945    283 lVILDED--GRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQ-------------RAYRTGDLVRLEADGLLF 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2322 CLGRKDSQVKVRGQRVELGEVEHHMRKClPEANQlAVEVVPPSGErDHAMLAAFIRLDDEtrnspliikyaednstAQIV 2401
Cdd:cd05945    348 YRGRLDFQVKLNGYRIELEEIEAALRQV-PGVKE-AVVVPKYKGE-KVTELIAFVVPKPG----------------AEAG 408
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 2402 FLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd05945    409 LTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
4551-5054 2.95e-87

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 295.31  E-value: 2.95e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 4630
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4631 EHIFRQTGAQVVLAsaqyatlwtslgrsvvivseastsqlpvvtktaDPSVNpgnaAYAIFTSGSTGIPKGVVLEHKAVV 4710
Cdd:cd05945     81 REILDAAKPALLIA---------------------------------DGDDN----AYIIFTSGSTGRPKGVQISHDNLV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4711 TSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGC-ICVPSD-SDRRNNLAKAINAMDVNWALLTPSVARM-- 4786
Cdd:cd05945    124 SFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDaTADPKQLFRFLAEHGITVWVSTPSFAAMcl 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4787 ----LDPCVVQSLKILVLGGEQVNSADWDRW----PKSiQTINAYGPTECSICCTTYSGKQ----GFKSGTIGTSIVSVS 4854
Cdd:cd05945    204 lsptFTPESLPSLRHFLFCGEVLPHKTARALqqrfPDA-RIYNTYGPTEATVAVTYIEVTPevldGYDRLPIGYAKPGAK 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4855 -WVVDPENhnRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAWllegygghsgrqgRLYKTGDLVRYDADGNLV 4933
Cdd:cd05945    283 lVILDEDG--RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQ-------------RAYRTGDLVRLEADGLLF 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4934 YLGRKDSQVKLRGQRVELGEVEHHVREClTEAKQlAVEVIVPEGEGGyAMLAAFVQLGDdtyntlvkekaggdslTVQVV 5013
Cdd:cd05945    348 YRGRLDFQVKLNGYRIELEEIEAALRQV-PGVKE-AVVVPKYKGEKV-TELIAFVVPKP----------------GAEAG 408
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 5014 FLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd05945    409 LTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
7617-8120 1.40e-86

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 293.38  E-value: 1.40e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 7696
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7697 EEIfeqtgaqvvVASAQysarwtssschvvtvskalssqlPAVVDSTNTSVrpenaAYIIFTSGSTGVPKGVVLEHRAVA 7776
Cdd:cd05945     81 REI---------LDAAK-----------------------PALLIADGDDN-----AYIIFTSGSTGRPKGVQISHDNLV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7777 tSCLGHGRA-FGITNLSRVLQFASYTFDACIAEIITTLLCGGC-ICVPSD-SDRRNSLAKAISTMDVNWAFLTPSVARL- 7852
Cdd:cd05945    124 -SFTNWMLSdFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDaTADPKQLFRFLAEHGITVWVSTPSFAAMc 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7853 -----LDPGLIPSLKILAIGGEQ---SSSADW-NRWPGSVqKIHVYGPTECCIFCTGYTTKQ----GFEPSTIGTSVASV 7919
Cdd:cd05945    203 llsptFTPESLPSLRHFLFCGEVlphKTARALqQRFPDAR-IYNTYGPTEATVAVTYIEVTPevldGYDRLPIGYAKPGA 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7920 S-WVVDPENhnRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAWllegypghpgrqgRLYKTGDLVQYNADGNL 7998
Cdd:cd05945    282 KlVILDEDG--RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQ-------------RAYRTGDLVRLEADGLL 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7999 VYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQlAVEVILPSGQKnHAMLAVFVQLGKGthiahleekaggedsmAQV 8078
Cdd:cd05945    347 FYRGRLDFQVKLNGYRIELEEIEAALRQV-PGVKE-AVVVPKYKGEK-VTELIAFVVPKPG----------------AEA 407
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 8079 VFLTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd05945    408 GLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
5636-6135 2.36e-86

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 292.67  E-value: 2.36e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5636 PHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTF 5715
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5716 RHTGAQVVVTSaqhsarwigtnhqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCW 5795
Cdd:cd17643     81 ADSGPSLLLTD-------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5796 GRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRN-----DLVKaistmDVSCALL--TPSVARLL 5868
Cdd:cd17643    124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSpedfaRLLR-----DEGVTVLnqTPSAFYQL 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5869 ------EPSSVPTLQMLVLQGEQVSFADWNRW-----PASVQTINGYGPTECSIcCNTY-----SGKQGFKSGIIGTSVA 5932
Cdd:cd17643    199 veaadrDGRDPLALRYVIFGGEALEAAMLRPWagrfgLDRPQLVNMYGITETTV-HVTFrpldaADLPAAAASPIGRPLP 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5933 SVSW-VVDpeNHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypGHPGRqgRLYKTGDLVRYDANG 6011
Cdd:cd17643    278 GLRVyVLD--ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF-------GGPGS--RMYRTGDLARRLPDG 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6012 NLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKDHAMLAAFVQLEEGTQNAlldkeasgedsma 6091
Cdd:cd17643    347 ELEYLGRADEQVKIRGFRIELGEIEAALATH-PSVRDAAV-IVREDEPGDTRLVAYVVADDGAAADI------------- 411
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 6092 qvvflASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd17643    412 -----AELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
7182-7573 2.85e-85

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 287.67  E-value: 2.85e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7182 IYPCSPLQEGLISLTAKRAGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELG-LLQVVVEE-KIQW-- 7257
Cdd:cd19542      1 IYPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtFLQVVLKSlDPPIee 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7258 --TESEALEEYLKEDKAVSMGLGDPLAHYALVKEAwGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNA 7335
Cdd:cd19542     81 veTDEDSLDALTRDLLDDPTLFGQPPHRLTLLETS-SGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFSD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7336 FIQYLGQQDLEATAAYWQTALSDCEAVLFPPLPSTVTQPVADTTVEYQCPPL--SKATLDTTTSTLIRAAWAIVTSCYTS 7413
Cdd:cd19542    160 YISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTRRSLAKLeaFCASLGVTLASLFQAAWALVLARYTG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7414 SDDVVYGTTVTGRNAPIAGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIAKLGSGPRHACG 7493
Cdd:cd19542    240 SRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWPSGTL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7494 FQTLLVVQPVDDVlGSDDMLGEWRSY-SKMQDFTTYALMVQFTLAAEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLA 7572
Cdd:cd19542    320 FNTLVSYQNFEAS-PESELSGSSVFElSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALL 398

                   .
gi 1820002560 7573 E 7573
Cdd:cd19542    399 A 399
AMP-binding pfam00501
AMP-binding enzyme;
4547-4945 3.92e-85

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 288.06  E-value: 3.92e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQARARPDTPAICAWDGE-LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 4625
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4626 PASRHEHIFRQTGAQVVLASAQ----------------YATLWTSLGRSVVIVSEASTSQLPVVTKTADPSVNPGNAAYA 4689
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDAlkleellealgklevvKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4690 IFTSGSTGIPKGVVLEHKAVVTSCLGHGQ----AFGITDHTRVLQFASYTFDA-CIAEIITTLLCCGCICVPSDSDRRN- 4763
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDp 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4764 -NLAKAINAMDVNWALLTPSVARML------DPCVVQSLKILVLGGEQVNSADWDRW----PKSIqtINAYGPTECSICC 4832
Cdd:pfam00501  241 aALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFrelfGGAL--VNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4833 TT--YSGKQGFKSGTIGTSIVSVSW-VVDPEnHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpawllegygg 4909
Cdd:pfam00501  319 TTplPLDEDLRSLGSVGRPLPGTEVkIVDDE-TGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED---------- 387
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1820002560 4910 hsgrqgRLYKTGDLVRYDADGNLVYLGRKDSQVKLR 4945
Cdd:pfam00501  388 ------GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
866-1365 6.58e-85

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 288.21  E-value: 6.58e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  866 PDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIF 945
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  946 KQIGAQVVLTssqhamlfasserhqvtvskvstsqlptvvnfakspvDPGNTAYIIFTSGTTGIPKGVVLQHRAVttscl 1025
Cdd:cd17650     81 EDSGAKLLLT-------------------------------------QPEDLAYVIYTSGTTGKPKGVMVEHRNV----- 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1026 gHGEAFGYTDH-------ARVLQFASYTFDACIAEIITTLLYGGC-ICVPSESD-RRNNLAKAISTMDVNCALLTPSVAR 1096
Cdd:cd17650    119 -AHAAHAWRREyeldsfpVRLLQMASFSFDVFAGDFARSLLNGGTlVICPDEVKlDPAALYDLILKSRITLMESTPALIR 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1097 LL------EPSAVPSLKRLVLqGEQVSFADWNRWP-----GSVQTINGYGPTECSVCCNTYSGKQGFKSGI----IGTSV 1161
Cdd:cd17650    198 PVmayvyrNGLDLSAMRLLIV-GSDGCKAQDFKTLaarfgQGMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPL 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1162 ASLS-WVVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAwllegyeghaGRRGRLYKTGDLVRCDAD 1240
Cdd:cd17650    277 PNTAmYVLDE--RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF----------APGERMYRTGDLARWRAD 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1241 GNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQLAVEVILPSGQkeHALLAAFI-QLDKGNHNALfeekasgeds 1319
Cdd:cd17650    345 GNVELLGRVDHQVKIRGFRIELGEIESQLAR-HPAIDEAVVAVREDKGG--EARLCAYVvAAATLNTAEL---------- 411
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 1320 maqvvfltgvEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17650    412 ----------RAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
4555-5054 7.03e-85

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 288.44  E-value: 7.03e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4555 PDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIF 4634
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4635 RQTGAQVVLasaqyatlwtslgrsvvivseastsqlpvvtktadpsVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCL 4714
Cdd:cd17643     81 ADSGPSLLL-------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4715 GHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRN--NLAKAINAMDVNWALLTPSVARMLDPCVV 4792
Cdd:cd17643    124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSpeDFARLLRDEGVTVLNQTPSAFYQLVEAAD 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4793 Q------SLKILVLGGEQVNSADWDRWPK-----SIQTINAYGPTECSICCT----TYSGKQGFKSGTIGTSIVSVSW-V 4856
Cdd:cd17643    204 RdgrdplALRYVIFGGEALEAAMLRPWAGrfgldRPQLVNMYGITETTVHVTfrplDAADLPAAAASPIGRPLPGLRVyV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4857 VDpeNHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygGHSGRqgRLYKTGDLVRYDADGNLVYLG 4936
Cdd:cd17643    284 LD--ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF-------GGPGS--RMYRTGDLARRLPDGELEYLG 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4937 RKDSQVKLRGQRVELGEVEHHVRECltEAKQLAVeVIVPEGEGGYAMLAAFVqLGDDTYNTLVKEkaggdsltvqvvfld 5016
Cdd:cd17643    353 RADEQVKIRGFRIELGEIEAALATH--PSVRDAA-VIVREDEPGDTRLVAYV-VADDGAAADIAE--------------- 413
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 5017 rVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd17643    414 -LRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
4555-5054 1.25e-84

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 287.44  E-value: 1.25e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4555 PDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIF 4634
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4635 RQTGAQVVLasaqyatlwtslgrsvvivseastsqlpvvtktadpsVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCL 4714
Cdd:cd17650     81 EDSGAKLLL-------------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4715 GHGQAFGITDHT-RVLQFASYTFDACIAEIITTLLCCGCICVPSDSDR--RNNLAKAINAMDVNWALLTPSVAR-MLDPC 4790
Cdd:cd17650    124 AWRREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKldPAALYDLILKSRITLMESTPALIRpVMAYV 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4791 V-----VQSLKILVLGGEQVNSADW----DRWPKSIQTINAYGPTECSICCTTYSGKQGFKSGT----IGTSIVSVS-WV 4856
Cdd:cd17650    204 YrngldLSAMRLLIVGSDGCKAQDFktlaARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAmYV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4857 VDPenHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygghsGRQGRLYKTGDLVRYDADGNLVYLG 4936
Cdd:cd17650    284 LDE--RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF----------APGERMYRTGDLARWRADGNVELLG 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4937 RKDSQVKLRGQRVELGEVEHHVREclTEAKQLAVeVIVPEGEGGYAMLAAFVqLGDDTYNTlvkekaggdsltvqvvflD 5016
Cdd:cd17650    352 RVDHQVKIRGFRIELGEIESQLAR--HPAIDEAV-VAVREDKGGEARLCAYV-VAAATLNT------------------A 409
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 5017 RVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd17650    410 ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
5196-5588 1.45e-84

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 286.41  E-value: 1.45e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5196 MYPCSPLQEGLM--SLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEE-KIQWT 5272
Cdd:cd19543      1 IYPLSPMQEGMLfhSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDrKLPWR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5273 E-----------SKRLEEYLREDKAVSMGLG-DRLARYALIKepYDGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGA 5340
Cdd:cd19543     81 EldlshlseaeqEAELEALAEEDRERGFDLArAPLMRLTLIR--LGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAAL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5341 VPERQPS------FNAFIQYLGQQDLEAATLYWQTALADCKAalfPTLPPTVTQPVADTTVEYQ---CPPPSQsATD--- 5408
Cdd:cd19543    159 GEGQPPSlppvrpYRDYIAWLQRQDKEAAEAYWREYLAGFEE---PTPLPKELPADADGSYEPGevsFELSAE-LTArlq 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5409 -------ITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQ 5481
Cdd:cd19543    235 elarqhgVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQ 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5482 STDMIAHEQTGLQRIAKMSPGARHAcgFQTLLVVQ--PTDDVLGSDDMLGEWR-SYSEMQDFTTYALMVQCTLAkDRVEV 5558
Cdd:cd19543    315 QLELREHEYVPLYEIQAWSEGKQAL--FDHLLVFEnyPVDESLEEEQDEDGLRiTDVSAEEQTNYPLTVVAIPG-EELTI 391
                          410       420       430
                   ....*....|....*....|....*....|
gi 1820002560 5559 TASFDARVIEQWVVEKMLRQFGFVMQQLAE 5588
Cdd:cd19543    392 KLSYDAEVFDEATIERLLGHLRRVLEQVAA 421
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
4544-5054 1.73e-84

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 286.76  E-value: 1.73e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4544 HDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 4623
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4624 DHPASRHEHIFRQTGAQVVLAsaqyatlwtslgrsvvivseastsqlpvvtktadpsvNPGNAAYAIFTSGSTGIPKGVV 4703
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLT-------------------------------------NPDDLAYVIYTSGSTGLPKGVM 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4704 LEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVpSDSDRRNNLAKA---INAMDVNWALLT 4780
Cdd:cd17645    124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHV-VPSERRLDLDALndyFNQEGITISFLP 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4781 PSVARMLDPCVVQSLKILVLGGEQVNSADwdrwPKSIQTINAYGPTECSICCTTYSGKQGFKSGTIGTSIVSVSWVVDPE 4860
Cdd:cd17645    203 TGAAEQFMQLDNQSLRVLLTGGDKLKKIE----RKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4861 NhNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAWLLEgygghsgrqgRLYKTGDLVRYDADGNLVYLGRKDS 4940
Cdd:cd17645    279 A-LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGE----------RMYRTGDLAKFLPDGNIEFLGRLDQ 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4941 QVKLRGQRVELGEVEhhVRECLTEAKQLAVeVIVPEGEGGYAMLAAFVqlgddtyntLVKEKAGGDSLtvqvvfldrvEE 5020
Cdd:cd17645    348 QVKIRGYRIEPGEIE--PFLMNHPLIELAA-VLAKEDADGRKYLVAYV---------TAPEEIPHEEL----------RE 405
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 5021 ELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd17645    406 WLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
7621-8120 2.82e-84

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 286.51  E-value: 2.82e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7621 PGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 7700
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7701 EQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 7780
Cdd:cd17643     81 ADSGPSLLL-------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7781 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLLDPGL- 7857
Cdd:cd17643    124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSpeDFARLLRDEGVTVLNQTPSAFYQLVEAAd 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7858 -----IPSLKILAIGGEQ---SSSADWNRWPG--SVQKIHVYGPTECCIFCTGY----TTKQGFEPSTIGTSVASVSW-V 7922
Cdd:cd17643    204 rdgrdPLALRYVIFGGEAleaAMLRPWAGRFGldRPQLVNMYGITETTVHVTFRpldaADLPAAAASPIGRPLPGLRVyV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7923 VDpeNHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypGHPGRqgRLYKTGDLVQYNADGNLVYLG 8002
Cdd:cd17643    284 LD--ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF-------GGPGS--RMYRTGDLARRLPDGELEYLG 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8003 RKDSQVKVRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKNHAMLAVFV-QLGKGTHIAHLEEKaggedsmaqvvfl 8081
Cdd:cd17643    353 RADEQVKIRGFRIELGEIEAALATH-PSVRDAAV-IVREDEPGDTRLVAYVVaDDGAAADIAELRAL------------- 417
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1820002560 8082 tgteeeLAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd17643    418 ------LKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
1932-2442 3.80e-84

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 285.99  E-value: 3.80e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1932 HDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 2011
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2012 DHPASRHEDIFRQTGAQVVVTsaqhsarwigtnhqvvtvsagsleqfstlvnpvdlpaKPENAAYVMFTSGSTGTPKGVV 2091
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLT-------------------------------------NPDDLAYVIYTSGSTGLPKGVM 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2092 LEHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVpSDSERR---DNLAKAITDMQVNWGYLT 2168
Cdd:cd17645    124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHV-VPSERRldlDALNDYFNQEGITISFLP 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2169 SSVARLLDPCLVPSLKVLVLGGEQVNSTDwgkwPSSVQTINGYGPTECCVFCTGYTGIQGFQSGNIGTSIASVS-WVVDP 2247
Cdd:cd17645    203 TGAAEQFMQLDNQSLRVLLTGGDKLKKIE----RKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRvYILDE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2248 ENhgRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegYPGHegrqgRLYKTGDLVRYSSDGNLVCLGRKD 2327
Cdd:cd17645    279 AL--QLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-----VPGE-----RMYRTGDLAKFLPDGNIEFLGRLD 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2328 SQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVPPSGERDHamLAAFIRLDDEtrnspliikyaednstaqiVFLTGIE 2407
Cdd:cd17645    347 QQVKIRGYRIEPGEIEPFLMN-HPLIELAAVLAKEDADGRKY--LVAYVTAPEE-------------------IPHEELR 404
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1820002560 2408 EELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd17645    405 EWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
1943-2442 5.22e-84

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 285.90  E-value: 5.22e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1943 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIF 2022
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2023 RQTGAQVVVTsaqhsarwigtnhqvvtvsagsleqfstlvnpvdlpaKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCL 2102
Cdd:cd17650     81 EDSGAKLLLT-------------------------------------QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2103 GHGQAFGVTNL-LRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSSVAR-LLDPC 2178
Cdd:cd17650    124 AWRREYELDSFpVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDpaALYDLILKSRITLMESTPALIRpVMAYV 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2179 L-----VPSLKVLVLGGEqVNSTDWGKWP-----SSVQTINGYGPTECCV----FCTGYTGIQGFQSGNIGTSIASVS-W 2243
Cdd:cd17650    204 YrngldLSAMRLLIVGSD-GCKAQDFKTLaarfgQGMRIINSYGVTEATIdstyYEEGRDPLGDSANVPIGRPLPNTAmY 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2244 VVDPenHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegYPGhegrqGRLYKTGDLVRYSSDGNLVCL 2323
Cdd:cd17650    283 VLDE--RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-----APG-----ERMYRTGDLARWRADGNVELL 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2324 GRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVvpPSGERDHAMLAAFIRLDDETRNSPLiikyaednstaqivfl 2403
Cdd:cd17650    351 GRVDHQVKIRGFRIELGEIESQLAR-HPAIDEAVVAV--REDKGGEARLCAYVVAAATLNTAEL---------------- 411
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1820002560 2404 tgiEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd17650    412 ---RAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
AMP-binding pfam00501
AMP-binding enzyme;
1935-2333 5.35e-84

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 284.59  E-value: 5.35e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1935 FTEQAKARPHAPAICAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 2013
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2014 PASRHEDIFRQTGAQVVVTSAQHSARWIGTNHQ-------VVTVSAGSLEQFSTL---------VNPVDLPAKPENAAYV 2077
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEALGklevvklVLVLDRDPVLKEEPLpeeakpadvPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2078 MFTSGSTGTPKGVVLEHRAVVTSCLGHGQ----AFGVTNLLRALQFTAYTFDV-CIAEIITTLVHGGCICVPSDSERRD- 2151
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDp 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2152 -NLAKAITDMQVNWGYLTSSVARLL------DPCLVPSLKVLVLGGEQVNSTDWGKW----PSSVqtINGYGPTECCVFC 2220
Cdd:pfam00501  241 aALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFrelfGGAL--VNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2221 TGYTGIQGFQS--GNIGTSIASVSW-VVDPEnHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpawllegypg 2297
Cdd:pfam00501  319 TTPLPLDEDLRslGSVGRPLPGTEVkIVDDE-TGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED---------- 387
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1820002560 2298 hegrqgRLYKTGDLVRYSSDGNLVCLGRKDSQVKVR 2333
Cdd:pfam00501  388 ------GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
PRK05691 PRK05691
peptide synthase; Validated
7163-8231 6.05e-84

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 312.49  E-value: 6.05e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7163 QLSQDAAAMCSVAASIVKDIYPCSPLQEGLI--SLTAKRAGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQ 7240
Cdd:PRK05691  3238 QLTQAQLDALPVPAAEIEDVYPLTPMQEGLLlhTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSW 3317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7241 HSELGLLQVVVE------EKIQW------TESEALEEYLKEDKAVSMGLGD-PLAHYALVK--EAwggKRWFVWTIHHAL 7305
Cdd:PRK05691  3318 NAGETMLQVIHKpgrtpiDYLDWrglpedGQEQRLQALHKQEREAGFDLLNqPPFHLRLIRvdEA---RYWFMMSNHHIL 3394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7306 YDGGSLPLILHAVKQVYSG------AVLERQPSFNAFIQYLGQQDLEATAAYWQTALSDCEAVlfPPLPS---------- 7369
Cdd:PRK05691  3395 IDAWCRSLLMNDFFEIYTAlgegreAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFERP--TPIPSdrpflrehag 3472
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7370 -TVTQPVAD--TTVE----YQCPPLSKATlDTTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPIAGVEAMVGPTIA 7442
Cdd:PRK05691  3473 dSGGMVVGDcyTRLDaadgARLRELAQAH-QLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFIN 3551
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7443 TVPVRLRVQRDQ---TVFAFLQGLQQQSTDMIAHEQTGLQHIAKLGSGPRHACGFQTLLVVQ--PVDDvlgsdDMLGEWR 7517
Cdd:PRK05691  3552 SIALRVQLPAAGqrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGQPLFDSLFVFEnaPVEV-----SVLDRAQ 3626
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7518 SYSKMQD----FTTYALMVqFTLAAEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLAEASeDSKVADIDTTTPEDRQQ 7593
Cdd:PRK05691  3627 SLNASSDsgrtHTNFPLTA-VCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGF-HGDLSELPLLGEQERDF 3704
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7594 LWAW--NADVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTV 7671
Cdd:PRK05691  3705 LLDGcnRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLL 3784
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7672 VAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASA----QYSARWTSSSCHVV--------TVSKALSSQLPAV 7739
Cdd:PRK05691  3785 GMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAacreQARALLDELGCANRprllvweeVQAGEVASHNPGI 3864
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7740 VDStntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCI 7819
Cdd:PRK05691  3865 YSG------PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARV 3938
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7820 -CVPSD--SDRRNSLAKA----ISTMDVnwaflTPS-VARLL--DPGLIPSLKILAIGGEQSS---SADW-NRWPGsVQK 7885
Cdd:PRK05691  3939 eIVPNAiaHDPQGLLAHVqaqgITVLES-----VPSlIQGMLaeDRQALDGLRWMLPTGEAMPpelARQWlQRYPQ-IGL 4012
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7886 IHVYGPTEC----CIFCTGYTTKQG-FEPstIGTsvasvswvvdPENHNRL---------APLGSMGELLMEGPILARGY 7951
Cdd:PRK05691  4013 VNAYGPAECsddvAFFRVDLASTRGsYLP--IGS----------PTDNNRLylldealelVPLGAVGELCVAGTGVGRGY 4080
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7952 LNDVDKTEAAFIDDPAwllegypGHPGRqgRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEA 8031
Cdd:PRK05691  4081 VGDPLRTALAFVPHPF-------GAPGE--RLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE-QAEV 4150
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8032 RQLAVevilpsgqknhamlavFVQLG-KGTH-IAHLeekAGGEDSMAQVVFLTGTEEELAKRLPKHMVPTVFFALLHFPM 8109
Cdd:PRK05691  4151 REAAV----------------AVQEGvNGKHlVGYL---VPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPL 4211
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8110 TTSGKADRKRLR--EIGASFTAQQLAetqtssqgpkrqPLTEAEQTMQQLWARVLGIDAdiIGLDDSFFRLGGDSIAAMK 8187
Cdd:PRK05691  4212 NANGKLDRKALPalDIGQLQSQAYLA------------PRNELEQTLATIWADVLKVER--VGVHDNFFELGGHSLLATQ 4277
                         1130      1140      1150      1160
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 8188 LVGEARRTgLQLSVadifrhprlidlaSLKSTFCNSVVEEVPAF 8231
Cdd:PRK05691  4278 IASRVQKA-LQRNV-------------PLRAMFECSTVEELAEY 4307
AMP-binding pfam00501
AMP-binding enzyme;
3467-3865 8.64e-84

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 283.82  E-value: 8.64e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3467 FTEQAKARPHAPAICAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 3545
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3546 PASRHEEIFEQTGAQVVVASAQY---------SARWTSSSCHVVTVSKALSSQL-------PAVVDSTNTSVRPENAAYI 3609
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleellealGKLEVVKLVLVLDRDPVLKEEPlpeeakpADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3610 IFTSGSTGVPKGVVLEHRAVATSCLGHG----RAFGITNLSRVLQFASYTFDA-CIAEIITTLLCGGCICVPSDSDRRN- 3683
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDp 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3684 -SLAKAISTMDVNWAFLTPSVARLL------DPGLIPSLKILAIGGEQSSSADWNRW----PGSVqkIHVYGPTECCIFC 3752
Cdd:pfam00501  241 aALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFrelfGGAL--VNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3753 TGYTTKQGFE--PSTIGTSVASVSW-VVDPEnHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllegypg 3829
Cdd:pfam00501  319 TTPLPLDEDLrsLGSVGRPLPGTEVkIVDDE-TGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED---------- 387
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1820002560 3830 hpgrqgRLYKTGDLVQYNADGNLVYLGRKDSQVKVR 3865
Cdd:pfam00501  388 ------GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
3475-3974 2.05e-83

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 285.32  E-value: 2.05e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVASAQYsarwtssSCHVVTVSKAL---SSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVAT 3631
Cdd:cd12114     81 ADAGARLVLTDGPD-------AQLDVAVFDVLildLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3632 SCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVN-WAFLtPSVARLL- 3707
Cdd:cd12114    154 TILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDpaHWAELIERHGVTlWNSV-PALLEMLl 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3708 -----DPGLIPSLKILAIGGeqsssaDW----------NRWPGSvQKIHVYGPTECCIFCTGYT-TKQGFEPSTI--GTS 3769
Cdd:cd12114    233 dvleaAQALLPSLRLVLLSG------DWipldlparlrALAPDA-RLISLGGATEASIWSIYHPiDEVPPDWRSIpyGRP 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3770 VASVSW-VVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypghpgrQGRLYKTGDLVQYNA 3848
Cdd:cd12114    306 LANQRYrVLDP--RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPD------------GERLYRTGDLGRYRP 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3849 DGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVEVIlpsGQKDHAMLAAFVQLEEGtqnalldkeaggeds 3928
Cdd:cd12114    372 DGTLEFLGRRDGQVKVRGYRIELGEIE-AALQAHPGVARAVVVVL---GDPGGKRLAAFVVPDND--------------- 432
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 3929 mAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd12114    433 -GTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
3475-3974 2.90e-83

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 283.59  E-value: 2.90e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 3634
Cdd:cd17650     81 EDSGAKLLL-------------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3635 GHGRAFGITNLS-RVLQFASYTFDACIAEIITTLLCGGCICVPSDSDR--RNSLAKAISTMDVNWAFLTPSVARLLDPGL 3711
Cdd:cd17650    124 AWRREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKldPAALYDLILKSRITLMESTPALIRPVMAYV 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3712 ------IPSLKILAIGGEQSSSADW----NRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPST----IGTSVASVS-WV 3776
Cdd:cd17650    204 yrngldLSAMRLLIVGSDGCKAQDFktlaARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAmYV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3777 VDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypgHPGrqGRLYKTGDLVQYNADGNLVYLG 3856
Cdd:cd17650    284 LDE--RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF--------APG--ERMYRTGDLARWRADGNVELLG 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3857 RKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVEVilpsgQKD---HAMLAAFVQLEEGTQnalldkeaggedsmaqvv 3933
Cdd:cd17650    352 RVDHQVKIRGFRIELGEIESQLAR-HPAIDEAVVAV-----REDkggEARLCAYVVAAATLN------------------ 407
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 3934 fLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd17650    408 -TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
5636-6135 3.52e-83

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 283.20  E-value: 3.52e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5636 PHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTF 5715
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5716 RHTGAQVVVTSaqhsarwigtnhqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCW 5795
Cdd:cd17650     81 EDSGAKLLLTQ-------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5796 GRGRAFGITNLS-RVLQFASYTFDACMDEIITTLMYGGCICVPSDSDR--RNDLVKAISTMDVSCALLTPSVARLL---- 5868
Cdd:cd17650    124 AWRREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKldPAALYDLILKSRITLMESTPALIRPVmayv 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5869 --EPSSVPTLQMLVLqGEQVSFADWNRWP-----ASVQTINGYGPTECSICCNTYSGKQGFKSGI----IGTSVASVS-W 5936
Cdd:cd17650    204 yrNGLDLSAMRLLIV-GSDGCKAQDFKTLaarfgQGMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAmY 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5937 VVDPenHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypgHPGrqGRLYKTGDLVRYDANGNLVCL 6016
Cdd:cd17650    283 VLDE--RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF--------APG--ERMYRTGDLARWRADGNVELL 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6017 GRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAVEVilpsgQKD---HAMLAAFVQLEEGTQnalldkeasgedsmaqv 6093
Cdd:cd17650    351 GRVDHQVKIRGFRIELGEIESQLAR-HPAIDEAVVAV-----REDkggEARLCAYVVAAATLN----------------- 407
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 6094 vfLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd17650    408 --TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
AMP-binding pfam00501
AMP-binding enzyme;
858-1256 8.49e-83

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 281.12  E-value: 8.49e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  858 FAEQARARPDASAVCAWDGE-LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGH 936
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  937 PASRHEEIFKQIGAQVVLTSSQH--AMLFASSERHQVTVSKVSTSQLP--------------TVVNFAKSPVDPGNTAYI 1000
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALklEELLEALGKLEVVKLVLVLDRDPvlkeeplpeeakpaDVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1001 IFTSGTTGIPKGVVLQHRAVTTSCLGHG----EAFGYTDHARVLQFASYTFDA-CIAEIITTLLYGGCICVPSESDRRN- 1074
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDp 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1075 -NLAKAISTMDVNCALLTPSVARLL------EPSAVPSLKRLVLQGEQVSFADWNRW----PGSVqtINGYGPTECSVCC 1143
Cdd:pfam00501  241 aALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFrelfGGAL--VNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1144 NT--YSGKQGFKSGIIGTSVASLSW-VVDAgNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpawllegyeg 1220
Cdd:pfam00501  319 TTplPLDEDLRSLGSVGRPLPGTEVkIVDD-ETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED---------- 387
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1820002560 1221 hagrrgRLYKTGDLVRCDADGNLVCLGRKDSQVKVR 1256
Cdd:pfam00501  388 ------GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
7613-8011 1.17e-82

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 280.74  E-value: 1.17e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7613 FAEQARARPGAPAICAWDGE-LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 7691
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7692 PASRHEEIFEQTGAQVVVASAQY---------SARWTSSSCHVVTVSKALSSQL-------PAVVDSTNTSVRPENAAYI 7755
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleellealGKLEVVKLVLVLDRDPVLKEEPlpeeakpADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7756 IFTSGSTGVPKGVVLEHRAVATSCLGHG----RAFGITNLSRVLQFASYTFDA-CIAEIITTLLCGGCICVPSDSDRRN- 7829
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDp 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7830 -SLAKAISTMDVNWAFLTPSVARLL------DPGLIPSLKILAIGGEQSSSADWNRW----PGSVqkIHVYGPTECCIFC 7898
Cdd:pfam00501  241 aALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFrelfGGAL--VNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7899 TGYTTKQGFE--PSTIGTSVASVSW-VVDPEnHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllegypg 7975
Cdd:pfam00501  319 TTPLPLDEDLrsLGSVGRPLPGTEVkIVDDE-TGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED---------- 387
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1820002560 7976 hpgrqgRLYKTGDLVQYNADGNLVYLGRKDSQVKVR 8011
Cdd:pfam00501  388 ------GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
4543-5056 1.44e-82

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 281.70  E-value: 1.44e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4543 VHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 4622
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4623 PDHPASRHEHIFRQTGAQVVLAsaqyatlwtslgrsvvivseastsqlpvvtktadpsvnpgnaAYAIFTSGSTGIPKGV 4702
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4703 VLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLAKAINAMDVNWALLTPS 4782
Cdd:COG0318    119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPT 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4783 VARML------DPCVVQSLKILVLGGEQVNSADWDRWPK--SIQTINAYGPTECS-ICCTTYSGKQGFKSGTIGTSIVSV 4853
Cdd:COG0318    199 MLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFEErfGVRIVEGYGLTETSpVVTVNPEDPGERRPGSVGRPLPGV 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4854 S-WVVDPEnhNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpaWLlegygghsgrqgrlyKTGDLVRYDADGNL 4932
Cdd:COG0318    279 EvRIVDED--GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG--WL---------------RTGDLGRLDEDGYL 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4933 VYLGRKDSQVKLRGQRVELGEVEHHVREC--LTEAkqlAVeVIVPEGEGGYAmLAAFVQLGDdtyntlvkekagGDSLTV 5010
Cdd:COG0318    340 YIVGRKKDMIISGGENVYPAEVEEVLAAHpgVAEA---AV-VGVPDEKWGER-VVAFVVLRP------------GAELDA 402
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 5011 qvvflDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:COG0318    403 -----EELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
866-1365 1.98e-82

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 281.60  E-value: 1.98e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  866 PDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKR-EDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEI 944
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  945 FKQIGAQVVLTssqhamlfasserhqvtvskvstsqlptvvnfakspvDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSC 1024
Cdd:cd17648     81 LEDTGARVVIT-------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1025 LGHGEAFGYTDHA--RVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNN--LAKAISTMDVNCALLTPSVARLLEP 1100
Cdd:cd17648    124 TSLSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPdrFYAYINREKVTYLSGTPSVLQQYDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1101 SAVPSLKRLVLQGEQVSFADWN----RWPGsvQTINGYGPTECSVCC--NTYSGKQGF-KSgiIGTSVASLSWVVDAGNH 1173
Cdd:cd17648    204 ARLPHLKRVDAAGEEFTAPVFEklrsRFAG--LIINAYGPTETTVTNhkRFFPGDQRFdKS--LGRPVRNTKCYVLNDAM 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1174 NRLaPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawLLEGYEGHAGRRGRLYKTGDLVRCDADGNLVCLGRKDSQV 1253
Cdd:cd17648    280 KRV-PVGAVGELYLGGDGVARGYLNRPELTAERFLPNP--FQTEQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQV 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1254 KVRGQRVELGEIEHHVREClpearqlavevilpSGQKEHALLAafiqldkgnhnalfEEKASGEDSMAQ---VVFLTGVE 1330
Cdd:cd17648    357 KIRGQRIEPGEVEAALASY--------------PGVRECAVVA--------------KEDASQAQSRIQkylVGYYLPEP 408
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 1331 EE---------LAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17648    409 GHvpesdllsfLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
3475-3974 4.07e-82

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 280.44  E-value: 4.07e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLG-VNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEI 3553
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3554 FEQTGAQVVVASaqysarwtssschvvtvskalSSQLpavvdstntsvrpenaAYIIFTSGSTGVPKGVVLEHRAVATSC 3633
Cdd:cd17648     81 LEDTGARVVITN---------------------STDL----------------AYAIYTSGTTGKPKGVLVEHGSVVNLR 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3634 LG-HGRAFGITNLS-RVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLLDP 3709
Cdd:cd17648    124 TSlSERYFGRDNGDeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDpdRFYAYINREKVTYLSGTPSVLQQYDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3710 GLIPSLKILAIGGEQSSSADWN----RWPGSVqkIHVYGPTECCIfctgYTTKQGFEPS-----TIGTSVASVSWVVDPE 3780
Cdd:cd17648    204 ARLPHLKRVDAAGEEFTAPVFEklrsRFAGLI--INAYGPTETTV----TNHKRFFPGDqrfdkSLGRPVRNTKCYVLND 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3781 NHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPawLLEGYPGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDS 3860
Cdd:cd17648    278 AMKRV-PVGAVGELYLGGDGVARGYLNRPELTAERFLPNP--FQTEQERARGRNARLYKTGDLVRWLPSGELEYLGRNDF 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3861 QVKVRGQRVELGEVEHH------VRECLPEARQLAVEVilPSGQKDHamLAAFVQLEEGTQNAlldkeaggedsmaqvvf 3934
Cdd:cd17648    355 QVKIRGQRIEPGEVEAAlasypgVRECAVVAKEDASQA--QSRIQKY--LVGYYLPEPGHVPE----------------- 413
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 3935 lASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd17648    414 -SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
7621-8120 7.26e-82

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 280.70  E-value: 7.26e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7621 PGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 7700
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7701 EQTGAQVVVASAQYsarwtssSCHVVTVSKAL---SSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVAT 7777
Cdd:cd12114     81 ADAGARLVLTDGPD-------AQLDVAVFDVLildLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7778 SCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVN-WAFLtPSVARLL- 7853
Cdd:cd12114    154 TILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDpaHWAELIERHGVTlWNSV-PALLEMLl 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7854 -----DPGLIPSLKILAIGGeqsssaDW----------NRWPGSvQKIHVYGPTECCIFCTGYT-TKQGFEPSTI--GTS 7915
Cdd:cd12114    233 dvleaAQALLPSLRLVLLSG------DWipldlparlrALAPDA-RLISLGGATEASIWSIYHPiDEVPPDWRSIpyGRP 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7916 VASVSW-VVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypghpgrQGRLYKTGDLVQYNA 7994
Cdd:cd12114    306 LANQRYrVLDP--RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPD------------GERLYRTGDLGRYRP 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7995 DGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVEVIlpsGQKNHAMLAVFVqlgkgthIAHLEEKAGGEDS 8074
Cdd:cd12114    372 DGTLEFLGRRDGQVKVRGYRIELGEIE-AALQAHPGVARAVVVVL---GDPGGKRLAAFV-------VPDNDGTPIAPDA 440
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 8075 MAQVvfltgteeeLAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd12114    441 LRAF---------LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
5197-5588 9.04e-82

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 277.65  E-value: 9.04e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5197 YPCSPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELG-LLQVVVEE-KIQW--- 5271
Cdd:cd19542      2 YPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtFLQVVLKSlDPPIeev 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5272 -TESKRLEEYLREDKAVSMGLGDRLARYALIKEPydGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGAVPERQPSFNA 5350
Cdd:cd19542     82 eTDEDSLDALTRDLLDDPTLFGQPPHRLTLLETS--SGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFSD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5351 FIQYLGQQDLEAATLYWQTALADCKAALFPTLPPTVTQPVADTTVEYQ-CPPPSQSAT-DITTSTLVRAAWAIVTSRYTS 5428
Cdd:cd19542    160 YISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTRRSlAKLEAFCASlGVTLASLFQAAWALVLARYTG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5429 SDDVVFGATVTGRNAPIAGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAHEQTGLQRIAKMSPGARHACG 5508
Cdd:cd19542    240 SRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWPSGTL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5509 FQTLLVVQPTDDVlGSDDMLGEWRSY-SEMQDFTTYALMVQCTLAKDRVEVTASFDARVIEQWVVEKMLRQFGFVMQQLA 5587
Cdd:cd19542    320 FNTLVSYQNFEAS-PESELSGSSVFElSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALL 398

                   .
gi 1820002560 5588 E 5588
Cdd:cd19542    399 A 399
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
7621-8120 1.44e-81

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 278.58  E-value: 1.44e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7621 PGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 7700
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7701 EQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 7780
Cdd:cd17650     81 EDSGAKLLL-------------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7781 GHGRAFGITNLS-RVLQFASYTFDACIAEIITTLLCGGCICVPSDSDR--RNSLAKAISTMDVNWAFLTPSVARLLDPGL 7857
Cdd:cd17650    124 AWRREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKldPAALYDLILKSRITLMESTPALIRPVMAYV 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7858 ------IPSLKILAIGGEQSSSADW----NRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPST----IGTSVASVS-WV 7922
Cdd:cd17650    204 yrngldLSAMRLLIVGSDGCKAQDFktlaARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAmYV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7923 VDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegypgHPGrqGRLYKTGDLVQYNADGNLVYLG 8002
Cdd:cd17650    284 LDE--RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF--------APG--ERMYRTGDLARWRADGNVELLG 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8003 RKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVEVILPSGQknHAMLAVFVQLGKGTHIAHLeekaggedsmaqvvflt 8082
Cdd:cd17650    352 RVDHQVKIRGFRIELGEIESQLAR-HPAIDEAVVAVREDKGG--EARLCAYVVAAATLNTAEL----------------- 411
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 8083 gtEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd17650    412 --RAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
866-1365 1.91e-81

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 279.54  E-value: 1.91e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  866 PDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIF 945
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  946 KQIGAQVVLTssQHAMLFASSERHQVTVskVSTSQLPTVVNFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCL 1025
Cdd:cd12114     81 ADAGARLVLT--DGPDAQLDVAVFDVLI--LDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1026 GHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNN--LAKAISTMDV---NC--ALLTPSVARLL 1098
Cdd:cd12114    157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPahWAELIERHGVtlwNSvpALLEMLLDVLE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1099 EPSAVPSLKRLVLQGeqvsfADW----------NRWPGSVQTINGyGPTECSVCCNTYS-GKQ--GFKSGIIGTSVASLS 1165
Cdd:cd12114    237 AAQALLPSLRLVLLS-----GDWipldlparlrALAPDARLISLG-GATEASIWSIYHPiDEVppDWRSIPYGRPLANQR 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1166 W-VVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAwllegyeghagrRGRLYKTGDLVRCDADGNLV 1244
Cdd:cd12114    311 YrVLDP--RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPD------------GERLYRTGDLGRYRPDGTLE 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1245 CLGRKDSQVKVRGQRVELGEIEhHVRECLPEARQLAVEVIlpsGQKEHALLAAFIQLDKGnhnalfeekasgedsmAQVV 1324
Cdd:cd12114    377 FLGRRDGQVKVRGYRIELGEIE-AALQAHPGVARAVVVVL---GDPGGKRLAAFVVPDND----------------GTPI 436
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 1325 FLTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd12114    437 APDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
5636-6135 2.24e-81

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 278.51  E-value: 2.24e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5636 PHAPAICAWDGELTYGELDALSSKLAGHLTQLG-VKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDT 5714
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5715 FRHTGAQVVVTSaqhsarwigtnhqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKGVVLEHRAVVTSC 5794
Cdd:cd17648     81 LEDTGARVVITN-------------------------------------STDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5795 WG-RGRAFGITNLS-RVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRND--LVKAISTMDVSCALLTPSVARLLEP 5870
Cdd:cd17648    124 TSlSERYFGRDNGDeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPdrFYAYINREKVTYLSGTPSVLQQYDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5871 SSVPTLQMLVLQGEQVSFADWN--RWPASVQTINGYGPTECSICC--NTYSGKQGF-KSgiIGTSVASVSWVVDPENHDR 5945
Cdd:cd17648    204 ARLPHLKRVDAAGEEFTAPVFEklRSRFAGLIINAYGPTETTVTNhkRFFPGDQRFdKS--LGRPVRNTKCYVLNDAMKR 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5946 LaPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPawLLEGYPGHPGRQGRLYKTGDLVRYDANGNLVCLGRKDSQVKL 6025
Cdd:cd17648    282 V-PVGAVGELYLGGDGVARGYLNRPELTAERFLPNP--FQTEQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKI 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6026 RGQRVELGEVEHH------VRECLPEARQLAVEVilPSGQKDHamLAAFVQLEEGTQNAlldkeasgedsmaqvvflASV 6099
Cdd:cd17648    359 RGQRIEPGEVEAAlasypgVRECAVVAKEDASQA--QSRIQKY--LVGYYLPEPGHVPE------------------SDL 416
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1820002560 6100 EEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd17648    417 LSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
866-1365 4.28e-81

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 278.59  E-value: 4.28e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  866 PDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIF 945
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  946 KQIGAQVVLTSSQHAMLFASSERHQV----TVSKVSTSQLPTVVNfakspvdPGNTAYIIFTSGTTGIPKGVVLQHRAVT 1021
Cdd:cd17656     82 LDSGVRVVLTQRHLKSKLSFNKSTILledpSISQEDTSNIDYINN-------SDDLLYIIYTSGTTGKPKGVQLEHKNMV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1022 TSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRN--NLAKAISTMDVNCALLTPSVARLL- 1098
Cdd:cd17656    155 NLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDveQLFDLVKRHNIEVVFLPVAFLKFIf 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1099 -EPSAVPS----LKRLVLQGEQV----SFADWNRWPGsVQTINGYGPTECSVcCNTYSgkqgFKSGI-------IGTSvA 1162
Cdd:cd17656    235 sEREFINRfptcVKHIITAGEQLvitnEFKEMLHEHN-VHLHNHYGPSETHV-VTTYT----INPEAeipelppIGKP-I 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1163 SLSWVVDAGNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawlLEGYEghagrrgRLYKTGDLVRCDADGN 1242
Cdd:cd17656    308 SNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDP---FDPNE-------RMYRTGDLARYLPDGN 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1243 LVCLGRKDSQVKVRGQRVELGEIEHHVREClpEARQLAVEVILPSGQKEHALLAAFIqldkgnhnalfeekasgedsMAQ 1322
Cdd:cd17656    378 IEFLGRADHQVKIRGYRIELGEIEAQLLNH--PGVSEAVVLDKADDKGEKYLCAYFV--------------------MEQ 435
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 1323 VVFLTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17656    436 ELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
1943-2442 7.50e-81

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 277.62  E-value: 7.50e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1943 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIF 2022
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2023 RQTGAQVVVT---SAQHSARWIGTNHQVVTVSAGSLEQFSTLVNPVDLpakpenaAYVMFTSGSTGTPKGVVLEHRAVVT 2099
Cdd:cd12114     81 ADAGARLVLTdgpDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDL-------AYVIFTSGSTGTPKGVMISHRAALN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2100 SCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRDN--LAKAITDMQVN-WgyltSSVARLLD 2176
Cdd:cd12114    154 TILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPahWAELIERHGVTlW----NSVPALLE 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2177 ---------PCLVPSLKVLVLGGeqvnstDW----------GKWPSSVQTINGyGPTEccvfctgytgiqgfqsgnigTS 2237
Cdd:cd12114    230 mlldvleaaQALLPSLRLVLLSG------DWipldlparlrALAPDARLISLG-GATE--------------------AS 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2238 IASVSWVVDPE----------------------NHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwllegy 2295
Cdd:cd12114    283 IWSIYHPIDEVppdwrsipygrplanqryrvldPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPD------ 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2296 pghegrQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVppsGERDHAMLAAF 2375
Cdd:cd12114    357 ------GERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQA-HPGVARAVVVVL---GDPGGKRLAAF 426
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 2376 IRLDDEtrnspliikyaednstAQIVFLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd12114    427 VVPDND----------------GTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
3463-3976 9.01e-81

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 276.69  E-value: 9.01e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3463 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 3542
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3543 PDHPASRHEEIFEQTGAQVVVAsaqysarwtssschvvtvskalssqlpavvdstntsvrpenaAYIIFTSGSTGVPKGV 3622
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3623 VLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFD-ACIAEIITTLLCGGCICVPSDSDRRnSLAKAISTMDVNWAFLTP 3701
Cdd:COG0318    119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPRFDPE-RVLELIERERVTVLFGVP 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3702 SVARLL------DPGLIPSLKILAIGGEQSSSADWNRWpgsVQK-----IHVYGPTECCIFCTGYTTKQGFE-PSTIGTS 3769
Cdd:COG0318    198 TMLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERF---EERfgvriVEGYGLTETSPVVTVNPEDPGERrPGSVGRP 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3770 VASVS-WVVDPEnhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLlegypghpgrqgrlyKTGDLVQYNA 3848
Cdd:COG0318    275 LPGVEvRIVDED--GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG--WL---------------RTGDLGRLDE 335
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3849 DGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKDHAmLAAFVQLEEGTQnalLDKEAggeds 3928
Cdd:COG0318    336 DGYLYIVGRKKDMIISGGENVYPAEVEEVLAAH-PGVAEAAV-VGVPDEKWGER-VVAFVVLRPGAE---LDAEE----- 404
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 3929 maqvvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:COG0318    405 ---------LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
7621-8120 9.06e-81

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 276.59  E-value: 9.06e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7621 PGAPAICAWDGELTYGELDVLSSNLAGHLVQLG-VNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEI 7699
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7700 FEQTGAQVVVASaqysarwtssschvvtvskalSSQLpavvdstntsvrpenaAYIIFTSGSTGVPKGVVLEHRAVATSC 7779
Cdd:cd17648     81 LEDTGARVVITN---------------------STDL----------------AYAIYTSGTTGKPKGVLVEHGSVVNLR 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7780 LG-HGRAFGITNLS-RVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLLDP 7855
Cdd:cd17648    124 TSlSERYFGRDNGDeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDpdRFYAYINREKVTYLSGTPSVLQQYDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7856 GLIPSLKILAIGGEQSSSADWN----RWPGSVqkIHVYGPTECCIfctgYTTKQGFEPS-----TIGTSVASVSWVVDPE 7926
Cdd:cd17648    204 ARLPHLKRVDAAGEEFTAPVFEklrsRFAGLI--INAYGPTETTV----TNHKRFFPGDqrfdkSLGRPVRNTKCYVLND 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7927 NHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPawLLEGYPGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDS 8006
Cdd:cd17648    278 AMKRV-PVGAVGELYLGGDGVARGYLNRPELTAERFLPNP--FQTEQERARGRNARLYKTGDLVRWLPSGELEYLGRNDF 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8007 QVKVRGQRVELGEVEHHVREClPEARQLAVevilpsgqknhamlavfvqlgkgthIAHLEEKAGGEDSMAQVV-FLTGTE 8085
Cdd:cd17648    355 QVKIRGQRIEPGEVEAALASY-PGVRECAV-------------------------VAKEDASQAQSRIQKYLVgYYLPEP 408
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 8086 EE---------LAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd17648    409 GHvpesdllsfLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
854-1367 1.55e-80

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 275.92  E-value: 1.55e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 933
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 PGHPASRHEEIFKQIGAQVVLTssqhamlfasserhqvtvskvstsqlptvvnfakspvdpgntAYIIFTSGTTGIPKGV 1013
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1014 VLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFD-ACIAEIITTLLYGGC-ICVPSESDRRnnLAKAISTMDVNCALLT 1091
Cdd:COG0318    119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATlVLLPRFDPER--VLELIERERVTVLFGV 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1092 PSVARLL------EPSAVPSLKRLVLQGEQVS---FADWNRWPGsVQTINGYGPTECS-VCCNTYSGKQGFKSGIIGTSV 1161
Cdd:COG0318    197 PTMLARLlrhpefARYDLSSLRLVVSGGAPLPpelLERFEERFG-VRIVEGYGLTETSpVVTVNPEDPGERRPGSVGRPL 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1162 ASLS-WVVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpaWLlegyeghagrrgrlyKTGDLVRCDAD 1240
Cdd:COG0318    276 PGVEvRIVDE--DGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG--WL---------------RTGDLGRLDED 336
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1241 GNLVCLGRKDSQVKVRGQRVELGEIEHHVREClPEARQLAVeVILPSGQKEHALLaAFIQLDKGnhnalfeEKASGEDsm 1320
Cdd:COG0318    337 GYLYIVGRKKDMIISGGENVYPAEVEEVLAAH-PGVAEAAV-VGVPDEKWGERVV-AFVVLRPG-------AELDAEE-- 404
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 1321 aqvvfltgVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:COG0318    405 --------LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
3464-3974 1.65e-80

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 275.59  E-value: 1.65e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3464 HDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 3543
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3544 DHPASRHEEIFEQTGAQVVVASaqysarwtssschvvtvskalssqlpavvdstntsvrPENAAYIIFTSGSTGVPKGVV 3623
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLTN-------------------------------------PDDLAYVIYTSGSTGLPKGVM 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3624 LEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVpSDSDRR---NSLAKAISTMDVNWAFLT 3700
Cdd:cd17645    124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHV-VPSERRldlDALNDYFNQEGITISFLP 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3701 PSVARLLDPGLIPSLKILAIGGEQSSSADWNrwpgSVQKIHVYGPTECCIFCTGYTTKQGFEPSTIGTSVASVSWVVDPE 3780
Cdd:cd17645    203 TGAAEQFMQLDNQSLRVLLTGGDKLKKIERK----GYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3781 NhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegYPGHpgrqgRLYKTGDLVQYNADGNLVYLGRKDS 3860
Cdd:cd17645    279 A-LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-----VPGE-----RMYRTGDLAKFLPDGNIEFLGRLDQ 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3861 QVKVRGQRVELGEVEHHVREcLPEARQLAVeviLPSGQKDH-AMLAAFVQLEEGtqnalLDKEAggedsmaqvvflasVE 3939
Cdd:cd17645    348 QVKIRGYRIEPGEIEPFLMN-HPLIELAAV---LAKEDADGrKYLVAYVTAPEE-----IPHEE--------------LR 404
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1820002560 3940 EELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd17645    405 EWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
4115-4507 3.72e-80

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 273.03  E-value: 3.72e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4115 VYPCSPLQEGLMSLTAKRAGDYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELG-LLQVVVEE-RIQW-- 4190
Cdd:cd19542      1 IYPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtFLQVVLKSlDPPIee 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4191 --TESESLEEYPREDKAVSMGVGDRLARYALIKEPydGGKRWFVWTMHHALYDGWSLPRILHAVKQAYSGVVLERQPSFN 4268
Cdd:cd19542     81 veTDEDSLDALTRDLLDDPTLFGQPPHRLTLLETS--SGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4269 AFIQYLSQQDPEAAAAYWQTALVDCKAALFPTLPPTVTQPVADTTVEYQ-CPPPSQSAT-DITTSTLARAAWAIVTSRYT 4346
Cdd:cd19542    159 DYISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTRRSlAKLEAFCASlGVTLASLFQAAWALVLARYT 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4347 SSDDVVFGATVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQATDMIAHEQTGLQRIAKMSPGARHAC 4426
Cdd:cd19542    239 GSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWPSGT 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4427 GFQTLLVVQPTDDVlGSDDMLGEWRSY-SEMQDFTTYALMVQCVLVKDRVGVTASFDARVIEQWVVEKMLRQFGFVMQQL 4505
Cdd:cd19542    319 LFNTLVSYQNFEAS-PESELSGSSVFElSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEAL 397

                   ..
gi 1820002560 4506 AD 4507
Cdd:cd19542    398 LA 399
AMP-binding pfam00501
AMP-binding enzyme;
5628-6026 5.07e-80

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 273.03  E-value: 5.07e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5628 FTEQAKARPHAPAICAWDGE-LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 5706
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5707 PASRHEDTFRHTGAQVVVTSAQHSARWIGTNHQ-------VVTVSAGSLGQLSTLVNPVGLPAI---------PENAVYI 5770
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEALGklevvklVLVLDRDPVLKEEPLPEEAKPADVppppppppdPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5771 MFTSGSTGIPKGVVLEHRAVVTSC----WGRGRAFGITNLSRVLQFASYTFDACMD-EIITTLMYGGCICVPSDSDRRND 5845
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVlsikRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5846 --LVKAISTMDVSCALLTPSVARLL------EPSSVPTLQMLVLQGEQVSFADWNRW----PASVqtINGYGPTECSICC 5913
Cdd:pfam00501  241 aaLLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFrelfGGAL--VNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5914 NT--YSGKQGFKSGIIGTSVASVSW-VVDPEnHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpawllegypg 5990
Cdd:pfam00501  319 TTplPLDEDLRSLGSVGRPLPGTEVkIVDDE-TGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED---------- 387
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1820002560 5991 hpgrqgRLYKTGDLVRYDANGNLVCLGRKDSQVKLR 6026
Cdd:pfam00501  388 ------GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
4555-5054 1.50e-79

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 274.15  E-value: 1.50e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4555 PDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIF 4634
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4635 RQTGAQVVLASAQYATLWTSLGRSVVIVSEASTSQLPVvtktADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCL 4714
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPP----PPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4715 GHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLAkainamdvnWALL-----------TPSV 4783
Cdd:cd12114    157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAH---------WAELierhgvtlwnsVPAL 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4784 ARML------DPCVVQSLKILVLGGeqvnsaDW----------DRWPKsIQTINAYGPTECSICCTTYSgkqgfkSGTIG 4847
Cdd:cd12114    228 LEMLldvleaAQALLPSLRLVLLSG------DWipldlparlrALAPD-ARLISLGGATEASIWSIYHP------IDEVP 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4848 TSIVSVSW----------VVDPenHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegygghsgrQGRL 4917
Cdd:cd12114    295 PDWRSIPYgrplanqryrVLDP--RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPD------------GERL 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4918 YKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE----HHvrecltEAKQLAVEVIVPEGEGgyAMLAAFVQLGDD 4993
Cdd:cd12114    361 YRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEaalqAH------PGVARAVVVVLGDPGG--KRLAAFVVPDND 432
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 4994 tyntlvkekaggdsltVQVVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd12114    433 ----------------GTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
1506-1895 1.55e-79

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 271.77  E-value: 1.55e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1506 IYPCSPLQEGLM--SLTAKRAGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQVVIEE-NIQWT 1582
Cdd:cd19543      1 IYPLSPMQEGMLfhSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDrKLPWR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1583 ----------EPKS-LEEYLSEDKAVSVGLG-DPLARYAFVKEAcGGKRWFVWTIHHAVYDGWSLPLILHAVKQVYSGGV 1650
Cdd:cd19543     81 eldlshlseaEQEAeLEALAEEDRERGFDLArAPLMRLTLIRLG-DDRYRLVWSFHHILLDGWSLPILLKELFAIYAALG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1651 LQWQPS------FNAFIQYLGQQDLEATVAYWQTALADCEAvlfPTLPPTVTQPVADATVEYQ---CPpLSKATSD---- 1717
Cdd:cd19543    160 EGQPPSlppvrpYRDYIAWLQRQDKEAAEAYWREYLAGFEE---PTPLPKELPADADGSYEPGevsFE-LSAELTArlqe 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1718 ------TTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNTPVTGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQA 1791
Cdd:cd19543    236 larqhgVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQ 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1792 TDMIAHEQTGLQRIAKMGQGPQHAcsFQTLLVVQ--PVDDvldnTLGEWRDHSELQ-------EFTTYTLMLQCMLaAEG 1862
Cdd:cd19543    316 LELREHEYVPLYEIQAWSEGKQAL--FDHLLVFEnyPVDE----SLEEEQDEDGLRitdvsaeEQTNYPLTVVAIP-GEE 388
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1820002560 1863 VQITASFDTRVIEKWVVEKMLRQFSFIMQQLAE 1895
Cdd:cd19543    389 LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAA 421
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
8261-8636 1.88e-79

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 270.72  E-value: 1.88e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8261 VVPASYIQQFYIATGVRAPREAFNYPFIDLSDAVDIQVLQASCSALLEHFPILRTHFV--YFQGKLYQVIPRHQDLPFSI 8338
Cdd:cd19542      1 IYPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVesSAEGTFLQVVLKSLDPPIEE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8339 FEVNgalaEESQAIHIRDLDQ--TSPLGLPTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQEPLLSTTG 8416
Cdd:cd19542     81 VETD----EDSLDALTRDLLDdpTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8417 FHSYLAYVHNQ-RSASINYWSRLLKGSHITNITSkLRPKLGKDTTIRSV-----KVERVIRTPqlptGLTMASLVSSAWA 8490
Cdd:cd19542    157 FSDYISYLQSQsQEESLQYWRKYLQGASPCAFPS-LSPKRPAERSLSSTrrslaKLEAFCASL----GVTLASLFQAAWA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8491 VVLSHISGEEDVVYGLVVAGRNSDLPSITEV-------------------------SVQDQYISLGESDSIGLDDIVQHC 8545
Cdd:cd19542    232 LVLARYTGSRDVVFGYVVSGRDLPVPGIDDIvgpcintlpvrvkldpdwtvldllrQLQQQYLRSLPHQHLSLREIQRAL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8546 TDWPAKSEFDSIIQHQNIEEQPEIQFAGET-TKLQWFKNSFAVSRQLFVFSHprGNSLTITITGNTGILTDQCAEKLLVM 8624
Cdd:cd19542    312 GLWPSGTLFNTLVSYQNFEASPESELSGSSvFELSAAEDPTEYPVAVEVEPS--GDSLKVSLAYSTSVLSEEQAEELLEQ 389
                          410
                   ....*....|..
gi 1820002560 8625 LCDTISQLSDSL 8636
Cdd:cd19542    390 FDDILEALLANP 401
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
424-818 5.83e-79

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 270.23  E-value: 5.83e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  424 MYLCSPLQEGLM--SLTTKRAGDYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQVVVEE-KMQWT 500
Cdd:cd19543      1 IYPLSPMQEGMLfhSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDrKLPWR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  501 E-----------SESLEEYLNEDKAASMGLG-DRLARYALIKEScGGKRWFVWTIHHALYDGWSLPLVLDAVKQVYSG-- 566
Cdd:cd19543     81 EldlshlseaeqEAELEALAEEDRERGFDLArAPLMRLTLIRLG-DDRYRLVWSFHHILLDGWSLPILLKELFAIYAAlg 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  567 ----AALERQPSFNTFIQYVSQQDVKAAAAYWQTALADCEAvlfPPLPSTVTQPVADTTVKYQ---CPPSPEVT------ 633
Cdd:cd19543    160 egqpPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEE---PTPLPKELPADADGSYEPGevsFELSAELTarlqel 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  634 --SSNITTSTLIRAAWAIIASRYTSSEDIVFGTTVTGRNAPITGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQAT 711
Cdd:cd19543    237 arQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  712 EMIAYEQTGLQRIMKMGPGPQHAcgFQTLLVV--HPTddvlssDDTLGEWHSRSD---SELQYF--TTYALTIQCTLAvE 784
Cdd:cd19543    317 ELREHEYVPLYEIQAWSEGKQAL--FDHLLVFenYPV------DESLEEEQDEDGlriTDVSAEeqTNYPLTVVAIPG-E 387
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1820002560  785 GVQITASFDARVVEHWVVEKMLGQFSFVMQQLAE 818
Cdd:cd19543    388 ELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAA 421
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
7609-8122 6.33e-79

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 271.30  E-value: 6.33e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7609 VHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 7688
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7689 PDHPASRHEEIFEQTGAQVVVAsaqysarwtssschvvtvskalssqlpavvdstntsvrpenaAYIIFTSGSTGVPKGV 7768
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7769 VLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFD-ACIAEIITTLLCGGCICVPSDSDRRnSLAKAISTMDVNWAFLTP 7847
Cdd:COG0318    119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPRFDPE-RVLELIERERVTVLFGVP 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7848 SVARLL------DPGLIPSLKILAIGGEQSSSADWNRWpgsVQK-----IHVYGPTECCIFCTGYTTKQGFE-PSTIGTS 7915
Cdd:COG0318    198 TMLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERF---EERfgvriVEGYGLTETSPVVTVNPEDPGERrPGSVGRP 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7916 VASVS-WVVDPEnhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLlegypghpgrqgrlyKTGDLVQYNA 7994
Cdd:COG0318    275 LPGVEvRIVDED--GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG--WL---------------RTGDLGRLDE 335
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7995 DGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKNHAMLAvFVQLgkgthiahleeKAGGEDS 8074
Cdd:COG0318    336 DGYLYIVGRKKDMIISGGENVYPAEVEEVLAAH-PGVAEAAV-VGVPDEKWGERVVA-FVVL-----------RPGAELD 401
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 8075 MAQVVfltgteEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:COG0318    402 AEELR------AFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
4115-4507 8.98e-79

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 269.84  E-value: 8.98e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4115 VYPCSPLQEGLM--SLTAKRAGDYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELGLLQVVVEER-IQWT 4191
Cdd:cd19543      1 IYPLSPMQEGMLfhSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRkLPWR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4192 E-----------SESLEEYPREDKAVSMGVG-DRLARYALIKepYDGGKRWFVWTMHHALYDGWSLPRILHAVKQAYSG- 4258
Cdd:cd19543     81 EldlshlseaeqEAELEALAEEDRERGFDLArAPLMRLTLIR--LGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAAl 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4259 -----VVLERQPSFNAFIQYLSQQDPEAAAAYWQTALVDCKAalfPTLPPTVTQPVADTTVEYQ---CPPPSQsATD--- 4327
Cdd:cd19543    159 gegqpPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEE---PTPLPKELPADADGSYEPGevsFELSAE-LTArlq 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4328 -------ITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQ 4400
Cdd:cd19543    235 elarqhgVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQ 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4401 ATDMIAHEQTGLQRIAKMSPGARHAcgFQTLLVVQ--PTDDVLGSDDMLGEWR-SYSEMQDFTTYALMVQCVLvKDRVGV 4477
Cdd:cd19543    315 QLELREHEYVPLYEIQAWSEGKQAL--FDHLLVFEnyPVDESLEEEQDEDGLRiTDVSAEEQTNYPLTVVAIP-GEELTI 391
                          410       420       430
                   ....*....|....*....|....*....|
gi 1820002560 4478 TASFDARVIEQWVVEKMLRQFGFVMQQLAD 4507
Cdd:cd19543    392 KLSYDAEVFDEATIERLLGHLRRVLEQVAA 421
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
6278-6668 9.10e-79

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 268.79  E-value: 9.10e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6278 YPCSPLQEGLMSLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELG-LLQVVVEE-KIQW--- 6352
Cdd:cd19542      2 YPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtFLQVVLKSlDPPIeev 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6353 -TESKRLEEYLREDKAVSMGLGDPLARYAIIKEAwGGKRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSFNAF 6431
Cdd:cd19542     82 eTDEDSLDALTRDLLDDPTLFGQPPHRLTLLETS-SGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFSDY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6432 IQYLSQQDLEATAAYWQTALADCEATLFPPLPSSVKQLVADT-TVEHQCPLPSRSTSDTT-TSTLIRAAWAIVASRYTSS 6509
Cdd:cd19542    161 ISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSsTRRSLAKLEAFCASLGVtLASLFQAAWALVLARYTGS 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6510 DDVVFGTTITGRNAPVTSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEMIAYEQTGLQQIAKMGPDPQHACGF 6589
Cdd:cd19542    241 RDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWPSGTLF 320
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 6590 QTLLVVQPAGDVLGSDDTLGKWRGYSGLQDFMTYALGVRCTLSAEGVKITASFDARVIEHWVVEKMLGQFSFAMQQLAE 6668
Cdd:cd19542    321 NTLVSYQNFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLA 399
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
5625-6135 1.11e-78

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 270.19  E-value: 1.11e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5625 HDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 5704
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5705 DHPASRHEDTFRHTGAQVVVTSaqhsarwigtnhqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKGVV 5784
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLTN-------------------------------------PDDLAYVIYTSGSTGLPKGVM 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5785 LEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVpSDSDRRNDLVKA---ISTMDVSCALLT 5861
Cdd:cd17645    124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHV-VPSERRLDLDALndyFNQEGITISFLP 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5862 PSVARLLEPSSVPTLQMLVLQGEQVSFADWNrwpaSVQTINGYGPTECSICCNTYSGKQGFKSGIIGTSVASVS-WVVDP 5940
Cdd:cd17645    203 TGAAEQFMQLDNQSLRVLLTGGDKLKKIERK----GYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRvYILDE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5941 ENhdRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegYPGHpgrqgRLYKTGDLVRYDANGNLVCLGRKD 6020
Cdd:cd17645    279 AL--QLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-----VPGE-----RMYRTGDLAKFLPDGNIEFLGRLD 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6021 SQVKLRGQRVELGEVEHHVREcLPEARQLAVeviLPSGQKDH-AMLAAFVQLEEgtqnalldkEASGEdsmaqvvflaSV 6099
Cdd:cd17645    347 QQVKIRGYRIEPGEIEPFLMN-HPLIELAAV---LAKEDADGrKYLVAYVTAPE---------EIPHE----------EL 403
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1820002560 6100 EEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd17645    404 REWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
4555-5054 1.55e-78

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 271.27  E-value: 1.55e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4555 PDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIF 4634
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4635 RQTGAQVVLASAQYATLWtSLGRSVVIVSEASTSQlpVVTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCL 4714
Cdd:cd17656     82 LDSGVRVVLTQRHLKSKL-SFNKSTILLEDPSISQ--EDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4715 GHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRN--NLAKAINAMDVNWALLTPSVARML----- 4787
Cdd:cd17656    159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDveQLFDLVKRHNIEVVFLPVAFLKFIfsere 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4788 -DPCVVQSLKILVLGGEQVNSADWDR---WPKSIQTINAYGPTECSIC--CTTYSGKQGFKSGTIGTSIVSVsWVVDPEN 4861
Cdd:cd17656    239 fINRFPTCVKHIITAGEQLVITNEFKemlHEHNVHLHNHYGPSETHVVttYTINPEAEIPELPPIGKPISNT-WIYILDQ 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4862 HNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawllegYGGHSgrqgRLYKTGDLVRYDADGNLVYLGRKDSQ 4941
Cdd:cd17656    318 EQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDP------FDPNE----RMYRTGDLARYLPDGNIEFLGRADHQ 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4942 VKLRGQRVELGEVEHHVRECltEAKQLAVEVIVPEGEGGYAMLAAFVqlgddtyntlvkekaggdslTVQVVFLDRVEEE 5021
Cdd:cd17656    388 VKIRGYRIELGEIEAQLLNH--PGVSEAVVLDKADDKGEKYLCAYFV--------------------MEQELNISQLREY 445
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 5022 LAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd17656    446 LAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
1506-1895 1.83e-78

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 268.02  E-value: 1.83e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1506 IYPCSPLQEGLMSLTAKRAGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELG-LLQVVIEE-NIQW-- 1581
Cdd:cd19542      1 IYPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtFLQVVLKSlDPPIee 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1582 --TEPKSLEEYLSEDKAVSVGLGDPLARYAFVKEAcGGKRWFVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQWQPSFNA 1659
Cdd:cd19542     81 veTDEDSLDALTRDLLDDPTLFGQPPHRLTLLETS-SGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFSD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1660 FIQYLGQQDLEATVAYWQTALADCEAVLFPTLPPTVTQPVADATVEYQCPPL--SKATSDTTTSTLIRAAWAIVTSRYTT 1737
Cdd:cd19542    160 YISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTRRSLAKLeaFCASLGVTLASLFQAAWALVLARYTG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1738 SDDVVFGTTVTGRNTPVTGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAHEQTGLQRIAKMGQGPQHACS 1817
Cdd:cd19542    240 SRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWPSGTL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1818 FQTLLVVQPVDDVLDNTL-GEWRDH-SELQEFTTYTLMLQCMLAAEGVQITASFDTRVIEKWVVEKMLRQFSFIMQQLAE 1895
Cdd:cd19542    320 FNTLVSYQNFEASPESELsGSSVFElSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLA 399
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
4555-5054 8.77e-78

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 268.11  E-value: 8.77e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4555 PDTPAICAWDGELTYGELDTLSSKLASHLVQLG-VKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHI 4633
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4634 FRQTGAQVVLAsaqyatlwtslgrsvvivseastsqlpvvtktadpsvNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSC 4713
Cdd:cd17648     81 LEDTGARVVIT-------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4714 LGHGQAFGITDHT--RVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNN--LAKAINAMDVNWALLTPSVARMLDP 4789
Cdd:cd17648    124 TSLSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPdrFYAYINREKVTYLSGTPSVLQQYDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4790 CVVQSLKILVLGGEQVNSADWD----RWPKSIqtINAYGPTECSICC--TTYSGKQGFKSgTIGTSIVSVSWVVDPENHN 4863
Cdd:cd17648    204 ARLPHLKRVDAAGEEFTAPVFEklrsRFAGLI--INAYGPTETTVTNhkRFFPGDQRFDK-SLGRPVRNTKCYVLNDAMK 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4864 RLaPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawLLEGYGGHSGRQGRLYKTGDLVRYDADGNLVYLGRKDSQVK 4943
Cdd:cd17648    281 RV-PVGAVGELYLGGDGVARGYLNRPELTAERFLPNP--FQTEQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVK 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4944 LRGQRVELGEVEHH------VRECLTEAKQLAvevivpegeggyamlaafvqlgDDTYNTLVKEKAGGDSLTVQVVFLDR 5017
Cdd:cd17648    358 IRGQRIEPGEVEAAlasypgVRECAVVAKEDA----------------------SQAQSRIQKYLVGYYLPEPGHVPESD 415
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1820002560 5018 VEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd17648    416 LLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
855-1365 1.12e-77

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 267.11  E-value: 1.12e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  855 HDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 934
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  935 GHPASRHEEIFKQIGAQVVLTssqhamlfasserhqvtvskvstsqlptvvnfakspvDPGNTAYIIFTSGTTGIPKGVV 1014
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLT-------------------------------------NPDDLAYVIYTSGSTGLPKGVM 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1015 LQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRN--NLAKAISTMDVNCALLTP 1092
Cdd:cd17645    124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDldALNDYFNQEGITISFLPT 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1093 SVARLLEPSAVPSLKRLVLQGEQVSFADWNrwpgSVQTINGYGPTECSVCCNTYSGKQGFKSGIIGTSVASLSwVVDAGN 1172
Cdd:cd17645    204 GAAEQFMQLDNQSLRVLLTGGDKLKKIERK----GYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTR-VYILDE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1173 HNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAWLLEgyeghagrrgRLYKTGDLVRCDADGNLVCLGRKDSQ 1252
Cdd:cd17645    279 ALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGE----------RMYRTGDLAKFLPDGNIEFLGRLDQQ 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1253 VKVRGQRVELGEIEHhvreclpearQLAvevilpsgQKEHALLAAFIQLDKGNHNALFeekasgedsMAQVVFLTGVEEE 1332
Cdd:cd17645    349 VKIRGYRIEPGEIEP----------FLM--------NHPLIELAAVLAKEDADGRKYL---------VAYVTAPEEIPHE 401
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 1333 -----LAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17645    402 elrewLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
7610-8120 5.48e-77

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 265.19  E-value: 5.48e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7610 HDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 7689
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7690 DHPASRHEEIFEQTGAQVVVASaqysarwtssschvvtvskalssqlpavvdstntsvrPENAAYIIFTSGSTGVPKGVV 7769
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLTN-------------------------------------PDDLAYVIYTSGSTGLPKGVM 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7770 LEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVpSDSDRR---NSLAKAISTMDVNWAFLT 7846
Cdd:cd17645    124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHV-VPSERRldlDALNDYFNQEGITISFLP 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7847 PSVARLLDPGLIPSLKILAIGGEQSSSADWNrwpgSVQKIHVYGPTECCIFCTGYTTKQGFEPSTIGTSVASVSWVVDPE 7926
Cdd:cd17645    203 TGAAEQFMQLDNQSLRVLLTGGDKLKKIERK----GYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7927 NhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwllegYPGHpgrqgRLYKTGDLVQYNADGNLVYLGRKDS 8006
Cdd:cd17645    279 A-LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-----VPGE-----RMYRTGDLAKFLPDGNIEFLGRLDQ 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8007 QVKVRGQRVELGEVEHHVREcLPEARQLAVeviLPSGQKNH-AMLAVFVQLGKGTHIAHLEEKaggedsmaqvvfltgte 8085
Cdd:cd17645    348 QVKIRGYRIEPGEIEPFLMN-HPLIELAAV---LAKEDADGrKYLVAYVTAPEEIPHEELREW----------------- 406
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1820002560 8086 eeLAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd17645    407 --LKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
7182-7573 6.16e-77

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 264.45  E-value: 6.16e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7182 IYPCSPLQEGLI--SLTAKRAGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVVVEE-KIQWT 7258
Cdd:cd19543      1 IYPLSPMQEGMLfhSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDrKLPWR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7259 E-----------SEALEEYLKEDKAVSMGLG-DPLAHYALVKeaWGGKRW-FVWTIHHALYDGGSLPLILHAVKQVYSGA 7325
Cdd:cd19543     81 EldlshlseaeqEAELEALAEEDRERGFDLArAPLMRLTLIR--LGDDRYrLVWSFHHILLDGWSLPILLKELFAIYAAL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7326 V------LERQPSFNAFIQYLGQQDLEATAAYWQTALSDCEAvlfPPLPSTVTQPVADTTVEYQ------CPPLSKA--- 7390
Cdd:cd19543    159 GegqppsLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEE---PTPLPKELPADADGSYEPGevsfelSAELTARlqe 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7391 ---TLDTTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPIAGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQS 7467
Cdd:cd19543    236 larQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQ 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7468 TDMIAHEQTGLQHIAKLGSGPRHAcgFQTLLVVQ--PVDDVLGSDDMLGEWR-SYSKMQDFTTYAlmvqFTLAA---EGV 7541
Cdd:cd19543    316 LELREHEYVPLYEIQAWSEGKQAL--FDHLLVFEnyPVDESLEEEQDEDGLRiTDVSAEEQTNYP----LTVVAipgEEL 389
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1820002560 7542 QITASFDARVIEHWVLEKMLRQFSFIMQQLAE 7573
Cdd:cd19543    390 TIKLSYDAEVFDEATIERLLGHLRRVLEQVAA 421
PRK12316 PRK12316
peptide synthase; Provisional
6295-7358 6.47e-77

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 289.16  E-value: 6.47e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6295 AGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQV-------VVEEKIQWTESKRLEEYLReDKA 6367
Cdd:PRK12316    69 SGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVpldrpleVEFEDCSGLPEAEQEARLR-DEA 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6368 VSMGL------GDPLARYAIIKEAwGGKRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSFNAF-IQY----LS 6436
Cdd:PRK12316   148 QRESLqpfdlcEGPLLRVRLLRLG-EEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALpIQYadyaLW 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6437 QQD-LEA-----TAAYWQTALADCEATLFPPL--PSSVKQLVADTTVEHQCPLPSRSTSDTTTST-------LIRAAWAI 6501
Cdd:PRK12316   227 QRSwLEAgeqerQLEYWRAQLGEEHPVLELPTdhPRPAVPSYRGSRYEFSIDPALAEALRGTARRqgltlfmLLLGAFNV 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6502 VASRYTSSDDVVFGTTITGRNApvTSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEMIAYEQTGLQQIA---K 6578
Cdd:PRK12316   307 LLHRYSGQTDIRVGVPIANRNR--AEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVealK 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6579 MGPDPQHACGFQTLLVVQP-AGDVLGSDDTLG------KWRGYSGLQDFM--TYALGVRctLSAEGVKITASFDARVIE- 6648
Cdd:PRK12316   385 VERSLSHSPLFQVMYNHQPlVADIEALDTVAGlefgqlEWKSRTTQFDLTldTYEKGGR--LHAALTYATDLFEARTVEr 462
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6649 ---HWvvEKMLGqfsfAMQQLAEASadrkVADIDITTTTDRQQL-WAWN---AELPLAvdRCVHDLFTEQALARPNAPAV 6721
Cdd:PRK12316   463 marHW--QNLLR----GMVENPQAR----VDELPMLDAEERGQLvEGWNataAEYPLQ--RGVHRLFEEQVERTPEAPAL 530
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6722 CAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDILRQTGAQ 6801
Cdd:PRK12316   531 AFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQ 610
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6802 VIL------------ASAQNTTLFQSS----------------------------------------------------- 6816
Cdd:PRK12316   611 LLLsqshlgrklplaAGVQVLDLDRPAawlegyseenpgtelnpenlayviytsgstgkpkgagnrhralsnrlcwmqqa 690
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6817 -----NQTVVTVNRSSY------------------ILFPDENREAYPFVR------------------------------ 6843
Cdd:PRK12316   691 yglgvGDTVLQKTPFSFdvsvweffwplmsgarlvVAAPGDHRDPAKLVElinregvdtlhfvpsmlqaflqdedvasct 770
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6844 ----------------------------------PSNAAL-----------------------------------APLGS 6854
Cdd:PRK12316   771 slrrivcsgealpadaqeqvfaklpqaglynlygPTEAAIdvthwtcveeggdsvpigrpianlacyildanlepVPVGV 850
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6855 IGELLVEGPILARGYLNDADKTAAAFVNDPawLVEGHgkhpgrrgRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVE 6934
Cdd:PRK12316   851 LGELYLAGRGLARGYHGRPGLTAERFVPSP--FVAGE--------RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIE 920
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6935 LGEIENRLREcMPRATQMAVEVispagaaeQAKTMVVAFLQLNDEARDallggnvpnddnlsaqvvFPAKVDEKLSNLLP 7014
Cdd:PRK12316   921 LGEIEARLLE-HPWVREAAVLA--------VDGKQLVGYVVLESEGGD------------------WREALKAHLAASLP 973
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7015 SYMMPEVYFAVPQLPMMISGKTDRKRLREIGASFTAQQLAemrtssqgpkrQPSTEAERTMQQLWARMLKVkaDSIGLDD 7094
Cdd:PRK12316   974 EYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYV-----------APRNALERTLAAIWQDVLGV--ERVGLDD 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7095 SFFRLGGDSIVAMKLVGEARRTGLQLSVADVFRHPRLVDLAYVQNSQCSSAAEEVPAfsllgedvnpvqlsqdAAAMcsv 7174
Cdd:PRK12316  1041 NFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGPA----------------SGEV--- 1101
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7175 aasivkdiyPCSPLQEGLISLTAKRAGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSE--LGLLQVVVE 7252
Cdd:PRK12316  1102 ---------ALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGgwQQAYAAPQA 1172
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7253 EKIQWTESEALEEYLK---EDKAVSMGLGD-PLAHYALVKEAWGGKRwFVWTIHHALYDGGSLPLILHAVKQVYSGAVLE 7328
Cdd:PRK12316  1173 GEVLWQRQAASEEELLalcEEAQRSLDLEQgPLLRALLVDMADGSQR-LLLVIHHLVVDGVSWRILLEDLQRAYADLDAD 1251
                         1290      1300      1310
                   ....*....|....*....|....*....|....*
gi 1820002560 7329 ---RQPSFNAFIQYLGQQ--DLEATAAYWQTALSD 7358
Cdd:PRK12316  1252 lpaRTSSYQAWARRLHEHagARAEELDYWQAQLED 1286
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
5624-6137 7.37e-77

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 265.14  E-value: 7.37e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5624 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 5703
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5704 PDHPASRHEDTFRHTGAQVVVTsaqhsarwigtnhqvvtvsagslgqlstlvnpvglpaipenaVYIMFTSGSTGIPKGV 5783
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5784 VLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFD-ACMDEIITTLMYGGCICVPSDSDRRnDLVKAISTMDVSCALLTP 5862
Cdd:COG0318    119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPRFDPE-RVLELIERERVTVLFGVP 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5863 SVARLL------EPSSVPTLQMLVLQGEQVSFADWNRWPA--SVQTINGYGPTECS-ICCNTYSGKQGFKSGIIGTSVAS 5933
Cdd:COG0318    198 TMLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFEErfGVRIVEGYGLTETSpVVTVNPEDPGERRPGSVGRPLPG 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5934 VS-WVVDPEnhDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpaWLlegypghpgrqgrlyKTGDLVRYDANGN 6012
Cdd:COG0318    278 VEvRIVDED--GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG--WL---------------RTGDLGRLDEDGY 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6013 LVCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKDHAmLAAFVQLEEGTQnalLDKEAsgedsmaq 6092
Cdd:COG0318    339 LYIVGRKKDMIISGGENVYPAEVEEVLAAH-PGVAEAAV-VGVPDEKWGER-VVAFVVLRPGAE---LDAEE-------- 404
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 6093 vvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:COG0318    405 ------LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
3475-3974 7.85e-77

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 266.26  E-value: 7.85e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVASAQYSARWTSSSCHVVTVSKALSSQLPAVVDSTNTSvrpENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 3634
Cdd:cd17656     82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNS---DDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3635 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL--DPG 3710
Cdd:cd17656    159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDveQLFDLVKRHNIEVVFLPVAFLKFIfsERE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3711 LIPS----LKILAIGGEQSSSADWNRWPGSVQKIHV---YGPTECCIfCTGYTTKQGFEPST---IGTSVASVsWVVDPE 3780
Cdd:cd17656    239 FINRfptcVKHIITAGEQLVITNEFKEMLHEHNVHLhnhYGPSETHV-VTTYTINPEAEIPElppIGKPISNT-WIYILD 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3781 NHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPawlLEGYPghpgrqgRLYKTGDLVQYNADGNLVYLGRKDS 3860
Cdd:cd17656    317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDP---FDPNE-------RMYRTGDLARYLPDGNIEFLGRADH 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3861 QVKVRGQRVELGEVEHHVREClpEARQLAVEVILPSGQKDHAMLAAFVqleegtqnalldkeaggedsMAQVVFLASVEE 3940
Cdd:cd17656    387 QVKIRGYRIELGEIEAQLLNH--PGVSEAVVLDKADDKGEKYLCAYFV--------------------MEQELNISQLRE 444
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 3941 ELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd17656    445 YLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
5636-6135 2.87e-76

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 264.52  E-value: 2.87e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5636 PHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTF 5715
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5716 RHTGAQVVVT---SAQHSARWIGTNHQVVTVSAGSLGQLSTLVNPvGLPAipenavYIMFTSGSTGIPKGVVLEHRAVVT 5792
Cdd:cd12114     81 ADAGARLVLTdgpDAQLDVAVFDVLILDLDALAAPAPPPPVDVAP-DDLA------YVIFTSGSTGTPKGVMISHRAALN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5793 SCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRN--DLVKAISTMDVSCALLTPSVARLL-- 5868
Cdd:cd12114    154 TILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDpaHWAELIERHGVTLWNSVPALLEMLld 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5869 ----EPSSVPTLQMLVLQGeqvsfaDW----------NRWPASVQTINGyGPTECSICCNTYSgkqgfkSGIIGTSVASV 5934
Cdd:cd12114    234 vleaAQALLPSLRLVLLSG------DWipldlparlrALAPDARLISLG-GATEASIWSIYHP------IDEVPPDWRSI 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5935 SW----------VVDPenHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAwllegypghpgrQGRLYKTGDL 6004
Cdd:cd12114    301 PYgrplanqryrVLDP--RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPD------------GERLYRTGDL 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6005 VRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhHVRECLPEARQLAVEVIlpsGQKDHAMLAAFVQLEEGtqnalldkea 6084
Cdd:cd12114    367 GRYRPDGTLEFLGRRDGQVKVRGYRIELGEIE-AALQAHPGVARAVVVVL---GDPGGKRLAAFVVPDND---------- 432
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 6085 sgedsmAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd12114    433 ------GTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
1943-2442 7.84e-76

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 263.18  E-value: 7.84e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1943 PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIF 2022
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2023 RQTGAQVVVTSAQHSARwIGTNHQVVTVSAGSLEQFSTlvNPVDLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCL 2102
Cdd:cd17656     82 LDSGVRVVLTQRHLKSK-LSFNKSTILLEDPSISQEDT--SNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2103 GHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRD--NLAKAITDMQVNWGYLTSSVARLL----- 2175
Cdd:cd17656    159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDveQLFDLVKRHNIEVVFLPVAFLKFIfsere 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2176 -DPCLVPSLKVLVLGGEQVNSTDWGK---WPSSVQTINGYGPTECCVF--CTGYTGIQGFQSGNIGTSIASVsWVVDPEN 2249
Cdd:cd17656    239 fINRFPTCVKHIITAGEQLVITNEFKemlHEHNVHLHNHYGPSETHVVttYTINPEAEIPELPPIGKPISNT-WIYILDQ 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2250 HGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPawllegYPGHEgrqgRLYKTGDLVRYSSDGNLVCLGRKDSQ 2329
Cdd:cd17656    318 EQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDP------FDPNE----RMYRTGDLARYLPDGNIEFLGRADHQ 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2330 VKVRGQRVELGEVEHHMRKClpEANQLAVEVVPPSGERDHAMLAAFIRLddetrnspliikyaednstaQIVFLTGIEEE 2409
Cdd:cd17656    388 VKIRGYRIELGEIEAQLLNH--PGVSEAVVLDKADDKGEKYLCAYFVME--------------------QELNISQLREY 445
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 2410 LSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd17656    446 LAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
6277-6668 2.16e-75

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 259.83  E-value: 2.16e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6277 MYPCSPLQEGLM--SLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEE-KIQWT 6353
Cdd:cd19543      1 IYPLSPMQEGMLfhSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDrKLPWR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6354 E-----------SKRLEEYLREDKAVSMGLG-DPLARYAIIKeaWGGKRW-FVWTIHHALYDGWSLPRVLQAVKQAYNGA 6420
Cdd:cd19543     81 EldlshlseaeqEAELEALAEEDRERGFDLArAPLMRLTLIR--LGDDRYrLVWSFHHILLDGWSLPILLKELFAIYAAL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6421 V------LETQPSFNAFIQYLSQQDLEATAAYWQTALADCEATlfPPLPSSVKQLVADTTV--EHQCPLPSRSTSDTTTS 6492
Cdd:cd19543    159 GegqppsLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEP--TPLPKELPADADGSYEpgEVSFELSAELTARLQEL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6493 T---------LIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQAT 6563
Cdd:cd19543    237 ArqhgvtlntVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6564 EMIAYEQTGLQQIAKMGPDPQHAcgFQTLLVVQ--PAGDVLGSDDTLGKWRgYSGLQDF--MTYALGVRCTLSaEGVKIT 6639
Cdd:cd19543    317 ELREHEYVPLYEIQAWSEGKQAL--FDHLLVFEnyPVDESLEEEQDEDGLR-ITDVSAEeqTNYPLTVVAIPG-EELTIK 392
                          410       420
                   ....*....|....*....|....*....
gi 1820002560 6640 ASFDARVIEHWVVEKMLGQFSFAMQQLAE 6668
Cdd:cd19543    393 LSYDAEVFDEATIERLLGHLRRVLEQVAA 421
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
1943-2442 2.76e-75

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 260.80  E-value: 2.76e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1943 PHAPAICAWDGELTYGELDALSSKLASHLVQLG-VNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDI 2021
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2022 FRQTGAQVVVTsaqhsarwigtnhqvvtvsagsleqfstlvNPVDLpakpenaAYVMFTSGSTGTPKGVVLEHRAVVTSC 2101
Cdd:cd17648     81 LEDTGARVVIT------------------------------NSTDL-------AYAIYTSGTTGKPKGVLVEHGSVVNLR 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2102 LGHGQAFGVTN--LLRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRDN--LAKAITDMQVNWGYLTSSVARLLDP 2177
Cdd:cd17648    124 TSLSERYFGRDngDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPdrFYAYINREKVTYLSGTPSVLQQYDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2178 CLVPSLKVLVLGGEQVNSTDWGKWPSSV--QTINGYGPTECCVFCTG--YTGIQGFQSgNIGTSIASVSWVVDPENHGRL 2253
Cdd:cd17648    204 ARLPHLKRVDAAGEEFTAPVFEKLRSRFagLIINAYGPTETTVTNHKrfFPGDQRFDK-SLGRPVRNTKCYVLNDAMKRV 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2254 aPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPawLLEGYPGHEGRQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVR 2333
Cdd:cd17648    283 -PVGAVGELYLGGDGVARGYLNRPELTAERFLPNP--FQTEQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIR 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2334 GQRVELGEVEHHMRKClPEANQLAveVVPpsgeRDHAMLAafirldDETRNSPLIIKYAEDnstAQIVFLTGIEEELSER 2413
Cdd:cd17648    360 GQRIEPGEVEAALASY-PGVRECA--VVA----KEDASQA------QSRIQKYLVGYYLPE---PGHVPESDLLSFLRAK 423
                          490       500
                   ....*....|....*....|....*....
gi 1820002560 2414 LPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd17648    424 LPRYMVPARLVRLEGIPVTINGKLDVRAL 452
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
7621-8120 2.96e-75

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 261.64  E-value: 2.96e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7621 PGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 7700
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7701 EQTGAQVVVASAQYSARWTSSSCHVVTVSKALSSQLPAVVDSTNTSvrpENAAYIIFTSGSTGVPKGVVLEHRAVATSCL 7780
Cdd:cd17656     82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNS---DDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7781 GHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLL--DPG 7856
Cdd:cd17656    159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDveQLFDLVKRHNIEVVFLPVAFLKFIfsERE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7857 LIPS----LKILAIGGEQSSSADWNRWPGSVQKIHV---YGPTECCIfCTGYTTKQGFEPST---IGTSVASVsWVVDPE 7926
Cdd:cd17656    239 FINRfptcVKHIITAGEQLVITNEFKEMLHEHNVHLhnhYGPSETHV-VTTYTINPEAEIPElppIGKPISNT-WIYILD 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7927 NHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPawlLEGYPghpgrqgRLYKTGDLVQYNADGNLVYLGRKDS 8006
Cdd:cd17656    317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDP---FDPNE-------RMYRTGDLARYLPDGNIEFLGRADH 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8007 QVKVRGQRVELGEVEHHVREClpEARQLAVEVILPSGQKNHAMLAVFVqlgkgthiahleekaggedsMAQVVFLTGTEE 8086
Cdd:cd17656    387 QVKIRGYRIELGEIEAQLLNH--PGVSEAVVLDKADDKGEKYLCAYFV--------------------MEQELNISQLRE 444
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 8087 ELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd17656    445 YLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1931-2444 9.60e-75

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 258.97  E-value: 9.60e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1931 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 2010
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2011 PDHPASRHEDIFRQTGAQVVVTsaqhsarwigtnhqvvtvsagsleqfstlvnpvdlpakpenaAYVMFTSGSTGTPKGV 2090
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2091 VLEHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDV-CIAEIITTLVHGGCIcVPSDSERRDNLAKAITDMQVNWGYLTS 2169
Cdd:COG0318    119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFgLTVGLLAPLLAGATL-VLLPRFDPERVLELIERERVTVLFGVP 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2170 SVARLL------DPCLVPSLKVLVLGGEQVNSTDWGKWPS--SVQTINGYGPTECCVFCTGYTG-IQGFQSGNIGTSIAS 2240
Cdd:COG0318    198 TMLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFEErfGVRIVEGYGLTETSPVVTVNPEdPGERRPGSVGRPLPG 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2241 VS-WVVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpaWLlegypghegrqgrlyKTGDLVRYSSDGN 2319
Cdd:COG0318    278 VEvRIVDED--GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG--WL---------------RTGDLGRLDEDGY 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2320 LVCLGRKDSQVKVRGQRVELGEVEHHMRKClPEANQLAVEVVP--PSGERdhamLAAFIRLDDETRNSPliikyAEdnst 2397
Cdd:COG0318    339 LYIVGRKKDMIISGGENVYPAEVEEVLAAH-PGVAEAAVVGVPdeKWGER----VVAFVVLRPGAELDA-----EE---- 404
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 2398 aqivfltgIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:COG0318    405 --------LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
425-818 8.37e-74

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 254.54  E-value: 8.37e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  425 YLCSPLQEGLMSLTTKRAGDYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELG-LLQVVVEE-KMQW--- 499
Cdd:cd19542      2 YPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtFLQVVLKSlDPPIeev 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  500 -TESESLEEYLNEDKAASMGLGDRLARYALIKEScGGKRWFVWTIHHALYDGWSLPLVLDAVKQVYSGAALERQPSFNTF 578
Cdd:cd19542     82 eTDEDSLDALTRDLLDDPTLFGQPPHRLTLLETS-SGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFSDY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  579 IQYVSQQDVKAAAAYWQTALADCEAVLFPPLPSTVTQPVADTtvKYQCPPSPEVTSS---NITTSTLIRAAWAIIASRYT 655
Cdd:cd19542    161 ISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLS--STRRSLAKLEAFCaslGVTLASLFQAAWALVLARYT 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  656 SSEDIVFGTTVTGRNAPITGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTGLQRImkmgpgpQHAC 735
Cdd:cd19542    239 GSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREI-------QRAL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  736 G-------FQTLLVVHPTDDVlSSDDTLGEWHSRSDSElQYFTTYALTIQCTLAVEGVQITASFDARVVEHWVVEKMLGQ 808
Cdd:cd19542    312 GlwpsgtlFNTLVSYQNFEAS-PESELSGSSVFELSAA-EDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQ 389
                          410
                   ....*....|
gi 1820002560  809 FSFVMQQLAE 818
Cdd:cd19542    390 FDDILEALLA 399
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
2-283 2.02e-73

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 255.14  E-value: 2.02e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL----EPSHIPSLRILVMGGEQVNSADWDRWPSS---VQTINGYGPTECCIVCTGYTSEQDFTTG- 73
Cdd:cd05930    184 GITVLHLTPSLLRLLlqelELAALPSLRLVLVGGEALPPDLVRRWRELlpgARLVNLYGPTEATVDATYYRVPPDDEEDg 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   74 --TIGTSIASVS-WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawlleGHGGyagrqGRLYKTG 150
Cdd:cd05930    264 rvPIGRPIPNTRvYVLD--ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNP-----FGPG-----ERMYRTG 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  151 DLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVeVVLPlGQKNHATLAAFIQLDKGTHnallke 230
Cdd:cd05930    332 DLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLA-HPGVREAAV-VARE-DGDGEKRLVAYVVPDEGGE------ 402
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560  231 kvggddsiarvVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd05930    403 -----------LDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
5636-6135 7.42e-70

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 245.85  E-value: 7.42e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5636 PHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTF 5715
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5716 RHTGAQVVVTSAQHSARWIGTNHQVV----TVSAGSLGQLSTLVNpvglpaiPENAVYIMFTSGSTGIPKGVVLEHRAVV 5791
Cdd:cd17656     82 LDSGVRVVLTQRHLKSKLSFNKSTILledpSISQEDTSNIDYINN-------SDDLLYIIYTSGTTGKPKGVQLEHKNMV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5792 TSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRR-----NDLVKA--ISTMDVSCALLTPSV 5864
Cdd:cd17656    155 NLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRdveqlFDLVKRhnIEVVFLPVAFLKFIF 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5865 A-RLLEPSSVPTLQMLVLQGEQVSFADWNR---WPASVQTINGYGPTECSIcCNTYSgkqgFKSGI-------IGTSVAS 5933
Cdd:cd17656    235 SeREFINRFPTCVKHIITAGEQLVITNEFKemlHEHNVHLHNHYGPSETHV-VTTYT----INPEAeipelppIGKPISN 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5934 VsWVVDPENHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPawlLEGYPghpgrqgRLYKTGDLVRYDANGNL 6013
Cdd:cd17656    310 T-WIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDP---FDPNE-------RMYRTGDLARYLPDGNI 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6014 VCLGRKDSQVKLRGQRVELGEVEHHVREClpEARQLAVEVILPSGQKDHAMLAAFVqleegtqnalldkeasgedsMAQV 6093
Cdd:cd17656    379 EFLGRADHQVKIRGYRIELGEIEAQLLNH--PGVSEAVVLDKADDKGEKYLCAYFV--------------------MEQE 436
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 6094 VFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd17656    437 LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
6716-7041 1.50e-69

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 243.59  E-value: 1.50e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6716 PNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIL 6795
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6796 RQTGAQVILASAQN---------TT--------------------------------LFQSSN----------------Q 6818
Cdd:cd05930     81 EDSGAKLVLTDPDDlayviytsgSTgkpkgvmvehrglvnlllwmqeaypltpgdrvLQFTSFsfdvsvweifgallagA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6819 TVV----------------------------------------------------------------------------- 6821
Cdd:cd05930    161 TLVvlpeevrkdpealadllaeegitvlhltpsllrlllqelelaalpslrlvlvggealppdlvrrwrellpgarlvnl 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6822 ------TVNRSSYILFPDENREAYP-----------FVRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDP 6884
Cdd:cd05930    241 ygpteaTVDATYYRVPPDDEEDGRVpigrpipntrvYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6885 awlveghgKHPGrrGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLRECmPRATQMAVeVISPAGAAE 6964
Cdd:cd05930    321 --------FGPG--ERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAH-PGVREAAV-VAREDGDGE 388
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 6965 QaktMVVAFLQLNDeardallgGNVPNDDNLSAQvvfpakvdekLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd05930    389 K---RLVAYVVPDE--------GGELDEEELRAH----------LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
610-1493 7.73e-69

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 260.00  E-value: 7.73e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  610 PSTVTQPVADTTVKYQCPpSPEVTSSNITTS-TLIRAAWAIIASRYTSSEDIVFGTtvtgrNAPITGVEAMV----GPTI 684
Cdd:TIGR03443   19 LRPANNRLVEATYSLQLP-SAEVTAGGGSTPfIILLAAFAALVYRLTGDEDIVLGT-----SSNKSGRPFVLrlniTPEL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  685 ATVPLRVRprkgqtVSAFLENLQQQATEMIAYEQTGLQRIMKMGPGPQhacgFQTLLVVHPTDDvlssddtlgewhsrSD 764
Cdd:TIGR03443   93 SFLQLYAK------VSEEEKEGASDIGVPFDELSEHIQAAKKLERTPP----LFRLAFQDAPDN--------------QQ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  765 SELQYFTTYALTIQCTLAVEGVQITASFDARVVEHWVVEKMLGQFSfvmqQLAEAGVEKKVADIETTTLEDRQQlwvwNA 844
Cdd:TIGR03443  149 TTYSTGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLA----QLLSAASSNPDEPIGKVSLITPSQ----KS 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  845 DMP-PAVDR-------CIHDLFAEQARARPD-------ASAVCAWDG--ELTYGELDELSSKLAAHLVQLGVKREDVVPL 907
Cdd:TIGR03443  221 LLPdPTKDLdwsgfrgAIHDIFADNAEKHPDrtcvvetPSFLDPSSKtrSFTYKQINEASNILAHYLLKTGIKRGDVVMI 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  908 CFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRhEEIFKQIG---AQVVL----TSSQHAMLFASSERHQVT-------- 972
Cdd:TIGR03443  301 YAYRGVDLVVAVMGVLKAGATFSVIDPAYPPAR-QTIYLSVAkprALIVIekagTLDQLVRDYIDKELELRTeipalalq 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  973 ---------VSKVSTSQLPTVVNFAKSP----VDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARV 1039
Cdd:TIGR03443  380 ddgslvggsLEGGETDVLAPYQALKDTPtgvvVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKF 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1040 LQFASYTFDACIAEIITTLLYGGCICVPSESDRRN--NLAKAISTMDVNCALLTPSVARLLEPSAV---PSLKRLVLQGE 1114
Cdd:TIGR03443  460 TMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTpgRLAEWMAKYGATVTHLTPAMGQLLSAQATtpiPSLHHAFFVGD 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1115 QVSFADWNRWPG---SVQTINGYGPTEC--SVC---CNTYSGKQGF----------KSGIIgtSVASLswVVDAGNHNRL 1176
Cdd:TIGR03443  540 ILTKRDCLRLQTlaeNVCIVNMYGTTETqrAVSyfeIPSRSSDSTFlknlkdvmpaGKGMK--NVQLL--VVNRNDRTQT 615
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1177 APLGSIGELLVEGPILARGYLNDIDKTEAAFIddPAWLLEgyEGH----------------AGRRGRLYKTGDLVRCDAD 1240
Cdd:TIGR03443  616 CGVGEVGEIYVRAGGLAEGYLGLPELNAEKFV--NNWFVD--PSHwidldkennkperefwLGPRDRLYRTGDLGRYLPD 691
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1241 GNLVCLGRKDSQVKVRGQRVELGEIEHH------VRECLPEARQlavevilpSGQKEHALLAAFIQLDKGNHNALFEEKA 1314
Cdd:TIGR03443  692 GNVECCGRADDQVKIRGFRIELGEIDTHlsqhplVRENVTLVRR--------DKDEEPTLVSYIVPQDKSDELEEFKSEV 763
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1315 SGEDSMAQVV--------FLTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQdigasF-TVQQLAEM-RTSS 1384
Cdd:TIGR03443  764 DDEESSDPVVkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALP-----FpDTAQLAAVaKNRS 838
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1385 QGPKRQPSTEVEQTMQQLWAQVLSIEPNSIGLDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADIFRHPRLVDLA---- 1459
Cdd:TIGR03443  839 ASAADEEFTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKlNVELPLGLIFKSPTIKGFAkevd 918
                          970       980       990
                   ....*....|....*....|....*....|....*....
gi 1820002560 1460 RVQNSQF-----SSAAEEVpafsllgEDVNAVQLSQDAA 1493
Cdd:TIGR03443  919 RLKKGEEladegDSEIEEE-------ETVLELDYAKDAK 950
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
3471-3976 2.25e-66

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 236.58  E-value: 2.25e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 3550
Cdd:TIGR01734   10 AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPSERI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3551 EEIFEQTGAQVVVASAQYSArwTSSSCHVVTVSK---ALSSQLPAVVDStntSVRPENAAYIIFTSGSTGVPKGVVLEHR 3627
Cdd:TIGR01734   90 EMIIEAAGPELVIHTAELSI--DAVGTQIITLSAleqAETSGGPVSFDH---AVKGDDNYYIIYTSGSTGNPKGVQISHD 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3628 AVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGC-ICVPSD-SDRRNSLAKAISTMDVNWAFLTPSVAR 3705
Cdd:TIGR01734  165 NLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTlHCLDKDiTNNFKLLFEELPKTGLNVWVSTPSFVD 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3706 --LLDPGL----IPSLKILAIGGE----QSSSADWNRWPgSVQKIHVYGPTECCIFCTGYTTKQ----GFEPSTIGTSVA 3771
Cdd:TIGR01734  245 mcLLDPNFnqenYPHLTHFLFCGEelpvKTAKALLERFP-KATIYNTYGPTEATVAVTSVKITQeildQYPRLPIGFAKP 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3772 SVSWVVDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllEGYPGhpgrqgrlYKTGDLVQYNaDGN 3851
Cdd:TIGR01734  324 DMNLFIMDEEGEPL-PEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH-----EGQPA--------YRTGDAGTIT-DGQ 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3852 LVYLGRKDSQVKVRGQRVELGEVEHHVReclpEARQLAVEVILPSGQKDH--AMLAAFVQLEEgtqnalldkeaggEDSM 3929
Cdd:TIGR01734  389 LFYQGRLDFQIKLHGYRIELEDIEFNLR----QSSYIESAVVVPKYNKDHkvEYLIAAIVPET-------------EDFE 451
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 3930 AQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:TIGR01734  452 KEFQLTKAIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKALAE 498
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
3022-3430 3.08e-66

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 232.57  E-value: 3.08e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3022 VFPCTPMQEGILTSQGKDPDAYWVCFIYEVipnqETSISLARLQQAWKGVVHQHSLLRTLLVDNvpGSTGTTNVVLKDPQ 3101
Cdd:cd19545      1 IYPCTPLQEGLMALTARQPGAYVGQRVFEL----PPDIDLARLQAAWEQVVQANPILRTRIVQS--DSGGLLQVVVKESP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3102 PSISVFSSEGTAtIELFRSRynPAAqrsIGQLQHHLSICQLNNGKVYLCLDINHAIIDAHSRGILMHDLQEAYDANLNPQ 3181
Cdd:cd19545     75 ISWTESTSLDEY-LEEDRAA--PMG---LGGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3182 STSFRDFASYIKQQSQEEAGRYWAEYLDGVEPCFFPSLgdsggantiPRTVEVPSIDSSAVHMF----CKIWEVTPATII 3257
Cdd:cd19545    149 PPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAVFPPL---------PSSRYQPRPDATLEHSIslpsSASSGVTLATVL 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3258 QTAWALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPLISILPCRIHLHKQLTVLEALKTVQENYASSLSFQTFPLAS 3337
Cdd:cd19545    220 RAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQN 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3338 MHSfLGLGTSA--LFNTALSLQRIDDIGPCSASEITLKMK--EGLDPTEYNITLSAGYSKDAIDISMTFRAGCMDLVQAK 3413
Cdd:cd19545    300 IRR-LGPDARAacNFQTLLVVQPALPSSTSESLELGIEEEseDLEDFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVE 378
                          410
                   ....*....|....*..
gi 1820002560 3414 RLASNFSQAIKAVTTEP 3430
Cdd:cd19545    379 RLLDQFEHVLQQLASAP 395
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
4545-5054 9.60e-64

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 229.01  E-value: 9.60e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4545 DQFAEQaraRPDTPAICAWDGELTYGELDTLSSKLASHLVQLgvKPEDMVPLCF--EKSMWTVVAMLAVLKAGGAFVPLD 4622
Cdd:PRK04813     9 EEFAQT---QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSL--KLPDKSPIIVfgHMSPEMLATFLGAVKAGHAYIPVD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4623 PDHPASRHEHIFRQTGAQVVLASAQYATlwTSLGRSVVIVSEASTSQLPVVTKTADPSVNPGNAAYAIFTSGSTGIPKGV 4702
Cdd:PRK04813    84 VSSPAERIEMIIEVAKPSLIIATEELPL--EILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4703 VLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCIcVPSDSDRRNN---LAKAINAMDVNWALL 4779
Cdd:PRK04813   162 QISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTL-VALPKDMTANfkqLFETLPQLPINVWVS 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4780 TPSVARM--LDPCVVQ----SLKILVLGGE----QVNSADWDRWPKSiQTINAYGPTECSICCT----------TYsgkq 4839
Cdd:PRK04813   241 TPSFADMclLDPSFNEehlpNLTHFLFCGEelphKTAKKLLERFPSA-TIYNTYGPTEATVAVTsieitdemldQY---- 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4840 gfKSGTIGTSIVSVSWVVDPENHNRLaPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpawllEGYgghsgrqgRLYK 4919
Cdd:PRK04813   316 --KRLPIGYAKPDSPLLIIDEEGTKL-PDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF-----DGQ--------PAYH 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4920 TGDLVRYDaDGNLVYLGRKDSQVKLRGQRVELGEVEHHVREClteaKQLAVEVIVP-EGEGGYAMLAAFVQLGDDTYNtl 4998
Cdd:PRK04813   380 TGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQS----SYVESAVVVPyNKDHKVQYLIAYVVPKEEDFE-- 452
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 4999 vKEKAggdsLTVQvvfldrVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:PRK04813   453 -REFE----LTKA------IKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1-199 1.03e-63

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 225.61  E-value: 1.03e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    1 MRVNWALLTPSVARLLEPSHIP---SLRILVMGGEQVNSADWDRW---PSSVQTINGYGPTECCIVCTGYTSEQDFTTGT 74
Cdd:TIGR01733  211 HPVTVLNLTPSLLALLAAALPPalaSLRLVILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLVDPDDAPRE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   75 ----IGTSIASVS-WVVDPkdHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAWlleghggyAGRQGRLYKT 149
Cdd:TIGR01733  291 spvpIGRPLANTRlYVLDD--DLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRT 360
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560  150 GDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAV 199
Cdd:TIGR01733  361 GDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRH-PGVREAVV 409
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
7617-8122 2.18e-62

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 225.02  E-value: 2.18e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 7696
Cdd:TIGR01734   10 AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPSERI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7697 EEIFEQTGAQVVVASAQYSArwTSSSCHVVTVSK---ALSSQLPAVVDStntSVRPENAAYIIFTSGSTGVPKGVVLEHR 7773
Cdd:TIGR01734   90 EMIIEAAGPELVIHTAELSI--DAVGTQIITLSAleqAETSGGPVSFDH---AVKGDDNYYIIYTSGSTGNPKGVQISHD 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7774 AVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGC-ICVPSD-SDRRNSLAKAISTMDVNWAFLTPSVAR 7851
Cdd:TIGR01734  165 NLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTlHCLDKDiTNNFKLLFEELPKTGLNVWVSTPSFVD 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7852 --LLDPGL----IPSLKILAIGGE----QSSSADWNRWPgSVQKIHVYGPTECCIFCTGYTTKQ----GFEPSTIGTSVA 7917
Cdd:TIGR01734  245 mcLLDPNFnqenYPHLTHFLFCGEelpvKTAKALLERFP-KATIYNTYGPTEATVAVTSVKITQeildQYPRLPIGFAKP 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7918 SVSWVVDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllEGYPGhpgrqgrlYKTGDLVQYNaDGN 7997
Cdd:TIGR01734  324 DMNLFIMDEEGEPL-PEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH-----EGQPA--------YRTGDAGTIT-DGQ 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7998 LVYLGRKDSQVKVRGQRVELGEVEHHVReclpEARQLAVEVILPSGQKNHAMLAVfvqlgkgthIAHLEEKAggEDSMAQ 8077
Cdd:TIGR01734  389 LFYQGRLDFQIKLHGYRIELEDIEFNLR----QSSYIESAVVVPKYNKDHKVEYL---------IAAIVPET--EDFEKE 453
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 8078 VVFLTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:TIGR01734  454 FQLTKAIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKALAE 498
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
862-1365 2.06e-61

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 222.08  E-value: 2.06e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  862 ARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRH 941
Cdd:PRK04813    12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  942 EEIFKQIGAQVVLTSSqhAMLFASSERHQVTVSKVSTS-QLPTVVNFAkSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAV 1020
Cdd:PRK04813    92 EMIIEVAKPSLIIATE--ELPLEILGIPVITLDELKDIfATGNPYDFD-HAVKGDDNYYIIFTSGTTGKPKGVQISHDNL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1021 TTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGC-ICVPSE-SDRRNNLAKAISTMDVNCALLTPSVAR-- 1096
Cdd:PRK04813   169 VSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTlVALPKDmTANFKQLFETLPQLPINVWVSTPSFADmc 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1097 LLEPS----AVPSLKRLVLQGEQ--VSFAD--WNRWPGSVqTINGYGPTECSVC----------CNTYsgkqgfKSGIIG 1158
Cdd:PRK04813   249 LLDPSfneeHLPNLTHFLFCGEElpHKTAKklLERFPSAT-IYNTYGPTEATVAvtsieitdemLDQY------KRLPIG 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1159 TSVASLSWVVDAGNHNRLaPLGSIGELLVEGPILARGYLNDIDKTEAAFIDdpawllegYEGHagrrgRLYKTGDLVRCD 1238
Cdd:PRK04813   322 YAKPDSPLLIIDEEGTKL-PDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT--------FDGQ-----PAYHTGDAGYLE 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1239 aDGNLVCLGRKDSQVKVRGQRVELGEIEHHVREClpeaRQLAVEVILPSgQKEHAL--LAAFIQLDKGNHNALFEekasg 1316
Cdd:PRK04813   388 -DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQS----SYVESAVVVPY-NKDHKVqyLIAYVVPKEEDFEREFE----- 456
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1317 edsmaqvvfLT-GVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:PRK04813   457 ---------LTkAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
3471-3974 4.56e-61

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 220.92  E-value: 4.56e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 3550
Cdd:PRK04813    12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3551 EEIFEQTGAQVVVASAQYSArwTSSSCHVVTVSKALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVA 3630
Cdd:PRK04813    92 EMIIEVAKPSLIIATEELPL--EILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3631 TSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGC-ICVPSD-SDRRNSLAKAISTMDVN-WAFlTPSVAR-- 3705
Cdd:PRK04813   170 SFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTlVALPKDmTANFKQLFETLPQLPINvWVS-TPSFADmc 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3706 LLDPGL----IPSLKILAIGGE----QSSSADWNRWPGSVqKIHVYGPTECCIFCTGY-TTKQ---GFEPSTIGTSVASV 3773
Cdd:PRK04813   249 LLDPSFneehLPNLTHFLFCGEelphKTAKKLLERFPSAT-IYNTYGPTEATVAVTSIeITDEmldQYKRLPIGYAKPDS 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3774 SWVVDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllEGYPGhpgrqgrlYKTGDLVqYNADGNLV 3853
Cdd:PRK04813   328 PLLIIDEEGTKL-PDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF-----DGQPA--------YHTGDAG-YLEDGLLF 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3854 YLGRKDSQVKVRGQRVELGEVEHHVREClpeaRQLAVEVILPSgQKDH--AMLAAFVQLEEGTQNALLDkeaggedsmaq 3931
Cdd:PRK04813   393 YQGRIDFQIKLNGYRIELEEIEQNLRQS----SYVESAVVVPY-NKDHkvQYLIAYVVPKEEDFEREFE----------- 456
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 3932 vvFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:PRK04813   457 --LTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2-648 2.86e-60

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 232.05  E-value: 2.86e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL---EPSHIPSLRILVMGGEQVNSADWDRW---PSSVQTINGYGPTECCIVCTGYTSEQDFTTG-- 73
Cdd:COG1020    708 RVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELVRRWrarLPGARLVNLYGPTETTVDSTYYEVTPPDADGgs 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   74 -TIGTSIASVS-WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAwlleghgGYAGrqGRLYKTGD 151
Cdd:COG1020    788 vPIGRPIANTRvYVLD--AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPF-------GFPG--ARLYRTGD 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  152 LVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQlAVEVVLPLGQKNHAtLAAFIQLDKGTHNALLKEk 231
Cdd:COG1020    857 LARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQH-PGVRE-AVVVAREDAPGDKR-LVAYVVPEAGAAAAAALL- 932
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  232 vggddsiarvvflagvEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRlreigasftaqqLAEMRTSSQGPKRQPST 311
Cdd:COG1020    933 ----------------RLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLA------------LPAPAAAAAAAAAAPPA 984
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  312 EAERTMQQLWARVLGIEPDSIGLDDSFFRLGGDSIAAIKLVGEARRTGLQPSVADIFRHPTLAALASLETNQYNITIEET 391
Cdd:COG1020    985 EEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLA 1064
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  392 PPLSLLGENADVAQVRDEAAAMCSVDGSAiedmYLCSPLQEGLMSLTTKRAGDYIMQDVLELRADVDEHAFRAAWEYVVQ 471
Cdd:COG1020   1065 AAAAPLPLPPLLLSLLALLLALLLLLALL----ALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRL 1140
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  472 SIAVLRTRIVQHSELGLLQVVVEEKMQWTESESLEEYLNEDKAASMGLGDRLARYALIKEScggKRWFVWTIHHALYDGW 551
Cdd:COG1020   1141 LVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLL---LLLLLLLLLLLLLLLL 1217
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  552 SLPLVLDAVKQVYSGAALERQPSFNTFIQYVSQQDVKAAAAYWQTALADCEAVLFPPLPSTVTQPVADTTVKYQCPPSPE 631
Cdd:COG1020   1218 LLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALAL 1297
                          650
                   ....*....|....*..
gi 1820002560  632 VTSSNITTSTLIRAAWA 648
Cdd:COG1020   1298 LLLLALLLLLALALALL 1314
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
7617-8120 6.86e-60

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 217.46  E-value: 6.86e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 7696
Cdd:PRK04813    12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7697 EEIFEQTGAQVVVASAQYSArwTSSSCHVVTVSKALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVA 7776
Cdd:PRK04813    92 EMIIEVAKPSLIIATEELPL--EILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7777 TSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGC-ICVPSD-SDRRNSLAKAISTMDVN-WAFlTPSVAR-- 7851
Cdd:PRK04813   170 SFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTlVALPKDmTANFKQLFETLPQLPINvWVS-TPSFADmc 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7852 LLDPGL----IPSLKILAIGGE----QSSSADWNRWPGSVqKIHVYGPTECCIFCTGY-TTKQ---GFEPSTIGTSVASV 7919
Cdd:PRK04813   249 LLDPSFneehLPNLTHFLFCGEelphKTAKKLLERFPSAT-IYNTYGPTEATVAVTSIeITDEmldQYKRLPIGYAKPDS 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7920 SWVVDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawllEGYPGhpgrqgrlYKTGDLVqYNADGNLV 7999
Cdd:PRK04813   328 PLLIIDEEGTKL-PDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF-----DGQPA--------YHTGDAG-YLEDGLLF 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8000 YLGRKDSQVKVRGQRVELGEVEHHVREClpeaRQLAVEVILPSgQKNHAMlavfVQLgkgthIAHLEEKAGGEDSMAQvv 8079
Cdd:PRK04813   393 YQGRIDFQIKLNGYRIELEEIEQNLRQS----SYVESAVVVPY-NKDHKV----QYL-----IAYVVPKEEDFEREFE-- 456
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 8080 fLTGT-EEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:PRK04813   457 -LTKAiKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
PRK05691 PRK05691
peptide synthase; Validated
6257-7148 1.07e-59

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 231.98  E-value: 1.07e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6257 AQVSQDAAAMCSVDASSVEDMYPCSPLQEGLM--SLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIV 6334
Cdd:PRK05691  3237 AQLTQAQLDALPVPAAEIEDVYPLTPMQEGLLlhTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFS 3316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6335 QHSELGLLQVVVE------EKIQW------TESKRLEEYLREDKAVSMGLGD--PL-ARYAIIKEAwggKRWFVWTIHHA 6399
Cdd:PRK05691  3317 WNAGETMLQVIHKpgrtpiDYLDWrglpedGQEQRLQALHKQEREAGFDLLNqpPFhLRLIRVDEA---RYWFMMSNHHI 3393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6400 LYDGW--SLP-----RVLQAVKQAYNgAVLETQPSFNAFIQYLSQQDLEATAAYWQTALADCEATlfPPLPS-------- 6464
Cdd:PRK05691  3394 LIDAWcrSLLmndffEIYTALGEGRE-AQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFERP--TPIPSdrpflreh 3470
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6465 ---SVKQLVAD--TTVE-------------HQCPLpsrstsdtttSTLIRAAWAIVASRYTSSDDVVFGTTITGRNAPVT 6526
Cdd:PRK05691  3471 agdSGGMVVGDcyTRLDaadgarlrelaqaHQLTV----------NTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMP 3540
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6527 SIDAIVGPTIATVPLRVRLQKDQ---TVSSFLGYLQQQATEMIAYEQTGLQQIAKMGPDPQHACGFQTLLVVQPAG---D 6600
Cdd:PRK05691  3541 QMQRTVGLFINSIALRVQLPAAGqrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGQPLFDSLFVFENAPvevS 3620
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6601 VLGSDDTLgKWRGYSGlQDFMTYALGVRCtLSAEGVKITASFDARVIEHWVVEKMLGQFSFAMQQLAEAsADRKVADIDI 6680
Cdd:PRK05691  3621 VLDRAQSL-NASSDSG-RTHTNFPLTAVC-YPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQG-FHGDLSELPL 3696
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6681 TTTTDRQQLWAW--NAELPLAVDRCVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLC 6758
Cdd:PRK05691  3697 LGEQERDFLLDGcnRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALL 3776
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6759 FEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDILRQTGAQVILASA----QNTTLF-----------------QSSN 6817
Cdd:PRK05691  3777 AERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAacreQARALLdelgcanrprllvweevQAGE 3856
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6818 ----------------------------------------------------------QTV------------------- 6820
Cdd:PRK05691  3857 vashnpgiysgpdnlayviytsgstglpkgvmveqrgmlnnqlskvpylalseadviaQTAsqsfdisvwqflaaplfga 3936
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6821 ------------------------VTV----------------------------------------------------- 6823
Cdd:PRK05691  3937 rveivpnaiahdpqgllahvqaqgITVlesvpsliqgmlaedrqaldglrwmlptgeamppelarqwlqrypqiglvnay 4016
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6824 ------------------NRSSY--ILFPDENREAYpfVRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVND 6883
Cdd:PRK05691  4017 gpaecsddvaffrvdlasTRGSYlpIGSPTDNNRLY--LLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPH 4094
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6884 PawlvegHGKhPGRRgrLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAGAa 6963
Cdd:PRK05691  4095 P------FGA-PGER--LYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE-QAEVREAAVAVQEGVNG- 4163
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6964 eqaktmvvaflqlndearDALLGGNVPNDDNLSAQVVFpAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLR- 7042
Cdd:PRK05691  4164 ------------------KHLVGYLVPHQTVLAQGALL-ERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPa 4224
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7043 -EIGASFTAQQLAemrtssqgpkrqPSTEAERTMQQLWARMLKVkaDSIGLDDSFFRLGGDSIVAMKLVGEARRTgLQLS 7121
Cdd:PRK05691  4225 lDIGQLQSQAYLA------------PRNELEQTLATIWADVLKV--ERVGVHDNFFELGGHSLLATQIASRVQKA-LQRN 4289
                         1130      1140      1150
                   ....*....|....*....|....*....|
gi 1820002560 7122 VA--DVFRHPRLVDLA-YVQNSQCSSAAEE 7148
Cdd:PRK05691  4290 VPlrAMFECSTVEELAeYIEGLAGSAIDEQ 4319
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
854-1365 1.51e-59

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 216.55  E-value: 1.51e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAeQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 933
Cdd:TIGR01734    3 IEAIQA-FAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 PGHPASRHEEIFKQIGAQVVLTSSQHAMLFASSERHQVT-VSKVSTSQLPtvVNFaKSPVDPGNTAYIIFTSGTTGIPKG 1012
Cdd:TIGR01734   82 TSIPSERIEMIIEAAGPELVIHTAELSIDAVGTQIITLSaLEQAETSGGP--VSF-DHAVKGDDNYYIIYTSGSTGNPKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1013 VVLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGC-ICVPSE-SDRRNNLAKAISTMDVNCALL 1090
Cdd:TIGR01734  159 VQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTlHCLDKDiTNNFKLLFEELPKTGLNVWVS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1091 TPSVAR--LLEPS----AVPSLKRLVLQGE----QVSFADWNRWPgSVQTINGYGPTECSVCCNTYSGKQ----GFKSGI 1156
Cdd:TIGR01734  239 TPSFVDmcLLDPNfnqeNYPHLTHFLFCGEelpvKTAKALLERFP-KATIYNTYGPTEATVAVTSVKITQeildQYPRLP 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1157 IGTSVASLSWVVDAGNHNRLaPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpawllEGYeghagrrgRLYKTGDLVR 1236
Cdd:TIGR01734  318 IGFAKPDMNLFIMDEEGEPL-PEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH-----EGQ--------PAYRTGDAGT 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1237 CdADGNLVCLGRKDSQVKVRGQRVELGEIEHHVReclpEARQLAVEVILPSGQKEH---ALLAAFIqldkgnhnalfeek 1313
Cdd:TIGR01734  384 I-TDGQLFYQGRLDFQIKLHGYRIELEDIEFNLR----QSSYIESAVVVPKYNKDHkveYLIAAIV-------------- 444
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 1314 ASGEDSMAQVVFLTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:TIGR01734  445 PETEDFEKEFQLTKAIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
3231-4069 1.50e-56

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 219.94  E-value: 1.50e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3231 TVEVPSIDSSAVHMfckiweVTPATIIQTAWALVLSRYTNSTNPCFG--NLSSGRDLPIhnvnsifgplisilpcRIHLH 3308
Cdd:TIGR03443   32 SLQLPSAEVTAGGG------STPFIILLAAFAALVYRLTGDEDIVLGtsSNKSGRPFVL----------------RLNIT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3309 KQLTVLEALKTVQENYASSLSFQTFPLASMHSFL----GLG-TSALFNTALSLQ---RIDDIGPCSASEITLKmkegLDP 3380
Cdd:TIGR03443   90 PELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIqaakKLErTPPLFRLAFQDApdnQQTTYSTGSTTDLTVF----LTP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3381 TEYNITLSAGY-----SKDAIDIsmtfragcmdlvqakrLASNFSQAIKAVTTEPHSRIYSLDILTYNESKKI------- 3448
Cdd:TIGR03443  166 SSPELELSIYYnsllfSSDRITI----------------VADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLpdptkdl 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3449 -W-GWNAdvppaierCVHDLFTEQAKARPHAPAIC----AWDG-----ELTYGELDALSSKLASHLVQLGVNPEDVVPLC 3517
Cdd:TIGR03443  230 dWsGFRG--------AIHDIFADNAEKHPDRTCVVetpsFLDPssktrSFTYKQINEASNILAHYLLKTGIKRGDVVMIY 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3518 FEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRhEEIFEQTG---AQVVVASA----QYSARWTSSSCHVVTVSKA----- 3585
Cdd:TIGR03443  302 AYRGVDLVVAVMGVLKAGATFSVIDPAYPPAR-QTIYLSVAkprALIVIEKAgtldQLVRDYIDKELELRTEIPAlalqd 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3586 ----------------LSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVL 3649
Cdd:TIGR03443  381 dgslvggsleggetdvLAPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFT 460
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3650 QFASYTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLLDPG---LIPSLKILAIGGEQ 3724
Cdd:TIGR03443  461 MLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTpgRLAEWMAKYGATVTHLTPAMGQLLSAQattPIPSLHHAFFVGDI 540
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3725 SSSADWNRWPG---SVQKIHVYGPTECCIFCTGYTTKQGFEPSTI----------GTSVASVSW-VVDPENHNRLAPLGS 3790
Cdd:TIGR03443  541 LTKRDCLRLQTlaeNVCIVNMYGTTETQRAVSYFEIPSRSSDSTFlknlkdvmpaGKGMKNVQLlVVNRNDRTQTCGVGE 620
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3791 MGELLMEGPILARGYLNDVDKTEAAFIddPAWLLEgyPGH----------PGRQ------GRLYKTGDLVQYNADGNLVY 3854
Cdd:TIGR03443  621 VGEIYVRAGGLAEGYLGLPELNAEKFV--NNWFVD--PSHwidldkennkPEREfwlgprDRLYRTGDLGRYLPDGNVEC 696
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3855 LGRKDSQVKVRGQRVELGEVEHH------VREclpearqlavEVILPSGQKDH--AMLAAFVQLEEGTQNALLDKEAGGE 3926
Cdd:TIGR03443  697 CGRADDQVKIRGFRIELGEIDTHlsqhplVRE----------NVTLVRRDKDEepTLVSYIVPQDKSDELEEFKSEVDDE 766
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3927 DSMAQVV--------FLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLreigaSF--TAQQLAEMRTSSQGP 3996
Cdd:TIGR03443  767 ESSDPVVkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL-----PFpdTAQLAAVAKNRSASA 841
                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 3997 KRQPSTEAEQTMQQLWAQVLSLGADIIGLDDSFFRLGGDSIAAMKLVGEARR-MGLHLSVADIFRHPKLADFAG 4069
Cdd:TIGR03443  842 ADEEFTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKkLNVELPLGLIFKSPTIKGFAK 915
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
6304-7135 1.61e-56

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 219.53  E-value: 1.61e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6304 LELRVDVDEDAFRAAWEHVVQLTAALRTRIVQhSELGLLQVV-------VEEKIQWTESKRLEEYLRE------DKAVSM 6370
Cdd:PRK10252    36 VELTGELDAPLLARAVVAGLAEADTLRMRFTE-DNGEVWQWVdpaltfpLPEIIDLRTQPDPHAAAQAlmqadlQQDLRV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6371 GLGDPLARYAIIKeaWGGKRWFvW--TIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSFNAFI----------QYLSQQ 6438
Cdd:PRK10252   115 DSGKPLVFHQLIQ--LGDNRWY-WyqRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPASPFTpfadvveeyqRYRASE 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6439 DLEATAAYWQTALADceatLFPPLPSSVKQLVADTTVEHQCPLPSRSTSDTTTSTLIRAAW--------AIVA---SRYT 6507
Cdd:PRK10252   192 AWQRDAAFWAEQRRQ----LPPPASLSPAPLPGRSASADILRLKLEFTDGAFRQLAAQASGvqrpdlalALVAlwlGRLC 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6508 SSDDVVFGTTITGR--NAPVTSidaiVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEM-----IAYEQtgLQQIAKMG 6580
Cdd:PRK10252   268 GRMDYAAGFIFMRRlgSAALTA----TGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMrrhqrYDAEQ--IVRDSGRA 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6581 PDPQHACGfqTLLVVQP------AGDVLGSDDTLGkwrgySGLQDFMTYALGVRctlSAEGVKITASFDARVIEHWVVEK 6654
Cdd:PRK10252   342 AGDEPLFG--PVLNIKVfdyqldFPGVQAQTHTLA-----TGPVNDLELALFPD---EHGGLSIEILANPQRYDEATLIA 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6655 MLGQFSFAMQQLAEAsADRKVADIDITTTTDRQQLWAWNA---ELPlavDRCVHDLFTEQALARPNAPAVCAWDGELTYG 6731
Cdd:PRK10252   412 HAERLKALIAQFAAD-PALLCGDVDILLPGEYAQLAQVNAtavEIP---ETTLSALVAQQAAKTPDAPALADARYQFSYR 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6732 ELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDILRQTGAQVILASAQNTT 6811
Cdd:PRK10252   488 EMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLP 567
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6812 LFQ-----------------------------------SSNQT------VVT----VNR--------------------- 6825
Cdd:PRK10252   568 RFAdvpdltslcynaplapqgaaplqlsqphhtayiifTSGSTgrpkgvMVGqtaiVNRllwmqnhypltaddvvlqktp 647
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6826 -----SSYILF-------------PDENR--------------------------------------------------E 6837
Cdd:PRK10252   648 csfdvSVWEFFwpfiagaklvmaePEAHRdplamqqffaeygvttthfvpsmlaafvasltpegarqscaslrqvfcsgE 727
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6838 AYP------FVR-----------PSNAAL----------------------------------------APLGSIGELLV 6860
Cdd:PRK10252   728 ALPadlcreWQQltgaplhnlygPTEAAVdvswypafgeelaavrgssvpigypvwntglrildarmrpVPPGVAGDLYL 807
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6861 EGPILARGYLNDADKTAAAFVNDPAwlveghgkHPGrrGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIEN 6940
Cdd:PRK10252   808 TGIQLAQGYLGRPDLTASRFIADPF--------APG--ERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDR 877
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6941 RLRECMPRATQMAVEVISPAGAAEqaktmvvaflqlNDEARDalLGGNVPNDDNLSAQVvfpAKVDEKLSNLLPSYMMPE 7020
Cdd:PRK10252   878 AMQALPDVEQAVTHACVINQAAAT------------GGDARQ--LVGYLVSQSGLPLDT---SALQAQLRERLPPHMVPV 940
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7021 VYFAVPQLPMMISGKTDRKRLreigasfTAQQLAemrtsSQGPKRQPSTEAERTMQQLWARMLKVkaDSIGLDDSFFRLG 7100
Cdd:PRK10252   941 VLLQLDQLPLSANGKLDRKAL-------PLPELK-----AQVPGRAPKTGTETIIAAAFSSLLGC--DVVDADADFFALG 1006
                         1050      1060      1070
                   ....*....|....*....|....*....|....*.
gi 1820002560 7101 GDSIVAMKLVGEARRT-GLQLSVADVFRHPRLVDLA 7135
Cdd:PRK10252  1007 GHSLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLA 1042
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
5632-6135 6.50e-56

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 205.90  E-value: 6.50e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLgvKPEDMVPLCF--EKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 5709
Cdd:PRK04813    12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSL--KLPDKSPIIVfgHMSPEMLATFLGAVKAGHAYIPVDVSSPAE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5710 RHEDtfrhtgaqvVVTSAQHSArWIGTNHQVVTVSAG---SLGQLSTLVNPvGLPAIPENAV------YIMFTSGSTGIP 5780
Cdd:PRK04813    90 RIEM---------IIEVAKPSL-IIATEELPLEILGIpviTLDELKDIFAT-GNPYDFDHAVkgddnyYIIFTSGTTGKP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5781 KGVVLEHRAVVT-SCWGRgRAFGITNLSRVLQFASYTFD-ACMDeIITTLMYGGC-ICVPSD-SDRRNDLVKAISTMDVS 5856
Cdd:PRK04813   159 KGVQISHDNLVSfTNWML-EDFALPEGPQFLNQAPYSFDlSVMD-LYPTLASGGTlVALPKDmTANFKQLFETLPQLPIN 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5857 CALLTPSVAR--LLEPS----SVPTLQMLVLQGEQ--VSFAD--WNRWPASVqTINGYGPTECSIC----------CNTY 5916
Cdd:PRK04813   237 VWVSTPSFADmcLLDPSfneeHLPNLTHFLFCGEElpHKTAKklLERFPSAT-IYNTYGPTEATVAvtsieitdemLDQY 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5917 sgkqgfKSGIIGTSVASVSWVVDPENHDRLaPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpawllEGYPGhpgrqg 5996
Cdd:PRK04813   316 ------KRLPIGYAKPDSPLLIIDEEGTKL-PDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF-----DGQPA------ 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5997 rlYKTGDLVRYDaNGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClpeaRQLAVEVILPSgQKDHA--MLAAFVQLEEG 6074
Cdd:PRK04813   378 --YHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQS----SYVESAVVVPY-NKDHKvqYLIAYVVPKEE 449
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 6075 TQnallDKEASgedsmaqvvFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:PRK04813   450 DF----EREFE---------LTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
PRK12316 PRK12316
peptide synthase; Provisional
2-379 9.15e-55

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 215.98  E-value: 9.15e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL-----EPSHIPSLRILVMGGEQVNSADWDRWPSS---VQTINGYGPTECCIVCTGYTSEQDFTTG 73
Cdd:PRK12316  4784 RVTVLVFPPVYLQQLaehaeRDGEPPSLRVYCFGGEAVAQASYDLAWRAlkpVYLFNGYGPTETTVTVLLWKARDGDACG 4863
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   74 T----IGTSIASVS-WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawlLEGHGGyagrqgRLYK 148
Cdd:PRK12316  4864 AaympIGTPLGNRSgYVLD--GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDP---FGAPGG------RLYR 4932
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  149 TGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVRE--CLPEAKQLAVEVvlPLGQKnhatLAAFIQLDKgthNA 226
Cdd:PRK12316  4933 TGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREhpAVREAVVIAQEG--AVGKQ----LVGYVVPQD---PA 5003
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  227 LLkekvggDDSIARVVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssqgpk 306
Cdd:PRK12316  5004 LA------DADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYV---------- 5067
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560  307 rQPSTEAERTMQQLWARVLGIEpdSIGLDDSFFRLGGDSIAAIKLVGEAR-RTGLQPSVADIFRHPTLAALASL 379
Cdd:PRK12316  5068 -APRSELEQQVAAIWAEVLQLE--RVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTLAAFVEL 5138
PRK12316 PRK12316
peptide synthase; Provisional
23-716 1.22e-54

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 215.59  E-value: 1.22e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRWPSSVQTINGYGPTECCIVCTGYT-SEQDFTTGTIGTSIASVSWVVdPKDHGRLAPLGSVG 101
Cdd:PRK12316  3312 SLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQcVEEGKDAVPIGRPIANRACYI-LDGSLEPVPVGALG 3390
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  102 ELLVEGPILARGYLSDPEKTAAVFINNPawLLEGhggyagrqGRLYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELG 181
Cdd:PRK12316  3391 ELYLGGEGLARGYHNRPGLTAERFVPDP--FVPG--------ERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELG 3460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  182 EVEhhvrECLPEAKQLAVEVVLPLgqkNHATLAAFIQLDKgthnallkekvggDDSIARVVFlagvEEELAKRLPKHMVP 261
Cdd:PRK12316  3461 EIE----ARLLEHPWVREAVVLAV---DGRQLVAYVVPED-------------EAGDLREAL----KAHLKASLPEYMVP 3516
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  262 TVFFALLHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssqgpkrQPSTEAERTMQQLWARVLGIEpdSIGLDDSFFRL 341
Cdd:PRK12316  3517 AHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-----------APVNELERRLAAIWADVLKLE--QVGLTDNFFEL 3583
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  342 GGDSIAAIKLVGEARRTGLQPSVADIFRHPTLAALASLETNQYNITIEETPplsllgenadvaqvrdeaaamcsVDGSAi 421
Cdd:PRK12316  3584 GGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGP-----------------------VSGET- 3639
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  422 edmyLCSPLQEGLMSLTTKRAGDYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQ---HSELGLLQVVVEEKMQ 498
Cdd:PRK12316  3640 ----LLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEdagGWTAEHLPVELGGALL 3715
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  499 W----TESESLEEyLNEDKAASMGLGD-RLARYALIKESCGGKRwFVWTIHHALYDGWSLPLVLDAVKQVYSGAALERQP 573
Cdd:PRK12316  3716 WraelDDAEELER-LGEEAQRSLDLADgPLLRALLATLADGSQR-LLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAP 3793
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  574 -------SFNTFIQ----YVSQQDVKAAAAYWQTALADCEAVLFPPLPSTVTQPVADTTVK-----------YQCPPSPE 631
Cdd:PRK12316  3794 rlpaktsSFKAWAErlqeHARGEALKAELAYWQEQLQGVSSELPCDHPQGALQNRHAASVQtrldreltrrlLQQAPAAY 3873
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  632 VTSSNittsTLIRAAWAIIASRYTSSEDIVFGTTVTGRNAPITGVE--AMVGPTIATVPLRVRPRK--GQTVSAFLENLQ 707
Cdd:PRK12316  3874 RTQVN----DLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDlsRTVGWFTSLFPVRLSPVEdlGASIKAIKEQLR 3949

                   ....*....
gi 1820002560  708 QQATEMIAY 716
Cdd:PRK12316  3950 AIPNKGIGF 3958
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
6706-7041 1.74e-54

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 201.28  E-value: 1.74e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6706 DLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 6785
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6786 HPASRHEDILRQTGAQVILASAQ--------------------------------------------------------- 6808
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSlagragglevavvidealdagpagnpavpvspddlayvmytsgstgrpkgvavthrg 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6809 ---------------NTTLFQSSN-------------------------QTVVTVNR-SSYI-------------LF--- 6831
Cdd:cd12117    161 vvrlvkntnyvtlgpDDRVLQTSPlafdastfeiwgallngarlvlapkGTLLDPDAlGALIaeegvtvlwltaaLFnql 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6832 ----------------------------------------------------------PDENREAYPFVRP-SNAA---- 6848
Cdd:cd12117    241 adedpecfaglrelltggevvspphvrrvlaacpglrlvngygptenttfttshvvteLDEVAGSIPIGRPiANTRvyvl 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6849 -----LAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPawlveghgkhPGRRGRLYKTGDLVYYNKDGNLVYIGRKD 6923
Cdd:cd12117    321 dedgrPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADP----------FGPGERLYRTGDLARWLPDGRLEFLGRID 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6924 GQVKVRGQRVELGEIENRLRECmPRATQMAVEVISPAGAAEQAKTMVVAFLQLNDEArdallggnvpnddnlsaqvvfpa 7003
Cdd:cd12117    391 DQVKIRGFRIELGEIEAALRAH-PGVREAVVVVREDAGGDKRLVAYVVAEGALDAAE----------------------- 446
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 7004 kVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd12117    447 -LRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
6729-6945 5.55e-54

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 197.49  E-value: 5.55e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6729 TYGELEALSTKLAGHLVQL-GVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDILRQTGAQVILASA 6807
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6808 QNTTLFQSSNQTVVTVNRS-----------------------SYILF--------------------------------- 6831
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLelaalddapappppdapsgpddlAYVIYtsgstgrpkgvvvthrslvnllawlarrygldp 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6832 -------------------------------PDEN--------------------------------------------- 6835
Cdd:TIGR01733  161 ddrvlqfaslsfdasveeifgallagatlvvPPEDeerddaallaaliaehpvtvlnltpsllallaaalppalaslrlv 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6836 ---------------REAYPFVR------PSNAA--------------------------------------LAPLGSIG 6856
Cdd:TIGR01733  241 ilggealtpalvdrwRARGPGARlinlygPTETTvwstatlvdpddaprespvpigrplantrlyvldddlrPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6857 ELLVEGPILARGYLNDADKTAAAFVNDPAWlveghgkhPGRRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELG 6936
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELG 392

                   ....*....
gi 1820002560 6937 EIENRLREC 6945
Cdd:TIGR01733  393 EIEAALLRH 401
PRK12316 PRK12316
peptide synthase; Provisional
23-600 6.01e-54

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 213.28  E-value: 6.01e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRWPSSVQT---INGYGPTECCIVCTGYTS-EQDFTTGTIGTSIASV-SWVVDPkdHGRLAPL 97
Cdd:PRK12316   771 SLRRIVCSGEALPADAQEQVFAKLPQaglYNLYGPTEAAIDVTHWTCvEEGGDSVPIGRPIANLaCYILDA--NLEPVPV 848
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   98 GSVGELLVEGPILARGYLSDPEKTAAVFINNPAwlleghggyaGRQGRLYKTGDLVRYDADGNLVCLGRKDSQVKLRGQR 177
Cdd:PRK12316   849 GVLGELYLAGRGLARGYHGRPGLTAERFVPSPF----------VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 918
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  178 VELGEVEHHV--RECLPEAKQLAVEvvlplGQKnhatLAAFIQLdkgthnallkEKVGGDdsiARVVFLAGveeeLAKRL 255
Cdd:PRK12316   919 IELGEIEARLleHPWVREAAVLAVD-----GKQ----LVGYVVL----------ESEGGD---WREALKAH----LAASL 972
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  256 PKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssqgpkrQPSTEAERTMQQLWARVLGIEPdsIGLD 335
Cdd:PRK12316   973 PEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYV-----------APRNALERTLAAIWQDVLGVER--VGLD 1039
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  336 DSFFRLGGDSIAAIKLVGEARRTGLQPSVADIFRHPTLAALASLETNQYNITIEETPplsllgenadvaqvrdeaaamcs 415
Cdd:PRK12316  1040 DNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGP----------------------- 1096
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  416 VDGSAIedmylCSPLQEGLMSLTTKRAGDYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSE--LGLLQVVV 493
Cdd:PRK12316  1097 ASGEVA-----LAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGgwQQAYAAPQ 1171
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  494 EEKMQW---TESESLEEYLNEDKAASMGLGD-RLARYALIKESCGGKRwFVWTIHHALYDGWSLPLVLDAVKQVYSGAAL 569
Cdd:PRK12316  1172 AGEVLWqrqAASEEELLALCEEAQRSLDLEQgPLLRALLVDMADGSQR-LLLVIHHLVVDGVSWRILLEDLQRAYADLDA 1250
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1820002560  570 ERQPSFNTFIQYVSQQDVKAAA-----AYWQTALAD 600
Cdd:PRK12316  1251 DLPARTSSYQAWARRLHEHAGAraeelDYWQAQLED 1286
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
9-283 8.49e-54

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 198.24  E-value: 8.49e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    9 TPSVARLLE------PSHIPSLRILVMGGEQVNSADWDRW----PSSVqTINGYGPTECCIVCTGY--TSEQ--DFTTGT 74
Cdd:cd05945    195 TPSFAAMCLlsptftPESLPSLRHFLFCGEVLPHKTARALqqrfPDAR-IYNTYGPTEATVAVTYIevTPEVldGYDRLP 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   75 IGTSIASVS-WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAWlleghggyagrqgRLYKTGDLV 153
Cdd:cd05945    274 IGYAKPGAKlVILD--EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQ-------------RAYRTGDLV 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  154 RYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQlAVEVVLPLGQKnHATLAAFIQLDKGTHNALLKEkvg 233
Cdd:cd05945    339 RLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQV-PGVKE-AVVVPKYKGEK-VTELIAFVVPKPGAEAGLTKA--- 412
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560  234 gddsiarvvflagVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd05945    413 -------------IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
1676-2539 2.59e-53

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 209.54  E-value: 2.59e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1676 WQTALADCEAVLFPT-LPPTVTQPVADATVEYQCPPLSKATSDTTTS-TLIRAAWAIVTSRYTTSDDVVFGTtvtgrNTP 1753
Cdd:TIGR03443    2 WSERLDNPTLSVLPHdYLRPANNRLVEATYSLQLPSAEVTAGGGSTPfIILLAAFAALVYRLTGDEDIVLGT-----SSN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1754 VTGVEAMVgptiatvpvRLRVQRDQTVFAFLQGLQQQATDMIAHEQTGLQRIAKMGQGPQHACSFQTLLVVQPVDDVlDN 1833
Cdd:TIGR03443   77 KSGRPFVL---------RLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPLFRLAFQDAP-DN 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1834 TlgewrdHSELQEFTTYTLMLQCMLAAEGVQITASFDTRVIEKWVVEKMLRQFSFIMQQlAEAGAEKTVSDIETTTPEDR 1913
Cdd:TIGR03443  147 Q------QTTYSTGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSA-ASSNPDEPIGKVSLITPSQK 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1914 QQLwawnqevP-PAIER-------CVHDLFTEQAKARPHAPAIC----AWDG-----ELTYGELDALSSKLASHLVQLGV 1976
Cdd:TIGR03443  220 SLL-------PdPTKDLdwsgfrgAIHDIFADNAEKHPDRTCVVetpsFLDPssktrSFTYKQINEASNILAHYLLKTGI 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1977 NPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRhEDIFRQTG---AQVVVTSA----QHSARWIGTNHQVVT 2049
Cdd:TIGR03443  293 KRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPAR-QTIYLSVAkprALIVIEKAgtldQLVRDYIDKELELRT 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2050 ------------VSAGSLEQFST--LVNPVDLPAK-------PENAAYVMFTSGSTGTPKGVVLEHRAvvtscLGH---- 2104
Cdd:TIGR03443  372 eipalalqddgsLVGGSLEGGETdvLAPYQALKDTptgvvvgPDSNPTLSFTSGSEGIPKGVLGRHFS-----LAYyfpw 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2105 -GQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVPS--DSERRDNLAKAITDMQVNWGYLTSSVARLLDP---C 2178
Cdd:TIGR03443  447 mAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTadDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAqatT 526
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2179 LVPSLKVLVLGGEQVNSTDWGKWPS---SVQTINGYGPTEccvfcT----GYTGIQGFQSGNI-----------GTSIAS 2240
Cdd:TIGR03443  527 PIPSLHHAFFVGDILTKRDCLRLQTlaeNVCIVNMYGTTE-----TqravSYFEIPSRSSDSTflknlkdvmpaGKGMKN 601
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2241 VSW-VVDPENHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIddPAWLLEgyPGH----------------EGRQG 2303
Cdd:TIGR03443  602 VQLlVVNRNDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFV--NNWFVD--PSHwidldkennkperefwLGPRD 677
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2304 RLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHM-------------RKCLPEANQLAVEVVPPSGERDha 2370
Cdd:TIGR03443  678 RLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLsqhplvrenvtlvRRDKDEEPTLVSYIVPQDKSDE-- 755
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2371 MLAAFIRLDDETRNSPLI---IKYAEdnstaqivFLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLreiga 2447
Cdd:TIGR03443  756 LEEFKSEVDDEESSDPVVkglIKYRK--------LIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL----- 822
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2448 SF--TAQQLAEMRTSSEGPKRQPSTEAERTMQQLWAQVLGIELESIGLDDSFFRLGGDSITAMQ-ISSSARALHLSVSTG 2524
Cdd:TIGR03443  823 PFpdTAQLAAVAKNRSASAADEEFTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRmIFELRKKLNVELPLG 902
                          970
                   ....*....|....*
gi 1820002560 2525 DILKKKTIALIAREI 2539
Cdd:TIGR03443  903 LIFKSPTIKGFAKEV 917
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
2-283 3.05e-53

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 195.93  E-value: 3.05e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLLEPSHIPSLRILVMGGEQVNSADWDRWPSSVQTINGYGPTECCIVCTGYTSEQDFTTGTIGTSIAS 81
Cdd:cd17652    184 RITHVTLPPAALAALPPDDLPDLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPG 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   82 VS-WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawlleghggYAGRQGRLYKTGDLVRYDADGN 160
Cdd:cd17652    264 TRvYVLD--ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADP---------FGAPGSRMYRTGDLARWRADGQ 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  161 LVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAVEVvlplgqknhatlaafiQLDKGTHNALLKEKVGGDDSIAR 240
Cdd:cd17652    333 LEFLGRADDQVKIRGFRIELGEVEAALTEH-PGVAEAVVVV----------------RDDRPGDKRLVAYVVPAPGAAPT 395
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1820002560  241 VvflAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd17652    396 A---AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1939-2442 7.85e-53

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 197.04  E-value: 7.85e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 2018
Cdd:PRK04813    12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2019 EDIFRQTGAQVVVTSAQHSArwigTNHQVVTVSAGSLEQFSTLVNPVDL--PAKPENAAYVMFTSGSTGTPKGVVLEHRA 2096
Cdd:PRK04813    92 EMIIEVAKPSLIIATEELPL----EILGIPVITLDELKDIFATGNPYDFdhAVKGDDNYYIIFTSGTTGKPKGVQISHDN 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2097 VVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGC-ICVPSD-SERRDNLAKAITDMQVNWGYLTSSVAR- 2173
Cdd:PRK04813   168 LVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTlVALPKDmTANFKQLFETLPQLPINVWVSTPSFADm 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2174 -LLDPCL----VPSLKVLVLGGE----QVNSTDWGKWPSSVqTINGYGPTECCVfctGYTGIQ-------GFQSGNIGTS 2237
Cdd:PRK04813   248 cLLDPSFneehLPNLTHFLFCGEelphKTAKKLLERFPSAT-IYNTYGPTEATV---AVTSIEitdemldQYKRLPIGYA 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2238 IASVSWVVDPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpawllEGYPGhegrqgrlYKTGDLVrYSSD 2317
Cdd:PRK04813   324 KPDSPLLIIDEE-GTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF-----DGQPA--------YHTGDAG-YLED 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2318 GNLVCLGRKDSQVKVRGQRVELGEVEHHMRKClpEANQLAVeVVPPsgERDHA--MLAAFIRLDDETRNSPLIIKYAedn 2395
Cdd:PRK04813   389 GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQS--SYVESAV-VVPY--NKDHKvqYLIAYVVPKEEDFEREFELTKA--- 460
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 2396 staqivfltgIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:PRK04813   461 ----------IKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
5367-6230 1.78e-52

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 206.84  E-value: 1.78e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5367 WQTALADCKAALFPT-LPPTVTQPVADTTVEYQCPPPSQSATDITTS-TLVRAAWAIVTSRYTSSDDVVFGAtvtgrNAP 5444
Cdd:TIGR03443    2 WSERLDNPTLSVLPHdYLRPANNRLVEATYSLQLPSAEVTAGGGSTPfIILLAAFAALVYRLTGDEDIVLGT-----SSN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5445 IAGVEAMvgptiatvpLRVCLQKDQTVSTLLECLQQQSTDMIAHEQTGL----QRIAKMSPGARHACGFQTLLVVQPTDd 5520
Cdd:TIGR03443   77 KSGRPFV---------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFdelsEHIQAAKKLERTPPLFRLAFQDAPDN- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5521 vlgsddmlgewrSYSEMQDFTTYALMVQCTLAKDRVEVTASFDARVIEQWVVEKMLRQFgfvmQQLAEAGAEKTVSDIET 5600
Cdd:TIGR03443  147 ------------QQTTYSTGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQL----AQLLSAASSNPDEPIGK 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5601 TTLEDRQQlwawNQNVP-PAIER-------CVHDLFTEQAKARPHAPAIC----AWDG-----ELTYGELDALSSKLAGH 5663
Cdd:TIGR03443  211 VSLITPSQ----KSLLPdPTKDLdwsgfrgAIHDIFADNAEKHPDRTCVVetpsFLDPssktrSFTYKQINEASNILAHY 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5664 LTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFR--HTGAQVVVTSA----QHSARWIGTN 5737
Cdd:TIGR03443  287 LLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSvaKPRALIVIEKAgtldQLVRDYIDKE 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5738 HQVVT------------VSAGSLGQLSTLV---------NPVGLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWG 5796
Cdd:TIGR03443  367 LELRTeipalalqddgsLVGGSLEGGETDVlapyqalkdTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPW 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5797 RGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRND--LVKAISTMDVSCALLTPSVARLLEPSSV- 5873
Cdd:TIGR03443  447 MAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPgrLAEWMAKYGATVTHLTPAMGQLLSAQATt 526
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5874 --PTLQMLVLQGEQVSFADWNRWPA---SVQTINGYGPTECSICCN-----TYSGKQGF----KSGI-IGTSVASVSWVV 5938
Cdd:TIGR03443  527 piPSLHHAFFVGDILTKRDCLRLQTlaeNVCIVNMYGTTETQRAVSyfeipSRSSDSTFlknlKDVMpAGKGMKNVQLLV 606
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5939 dPENHDRLAP--LGSIGELLVEGPILARGYLNDIQKTAAVFIddPAWLLEgyPGH----------PGRQ------GRLYK 6000
Cdd:TIGR03443  607 -VNRNDRTQTcgVGEVGEIYVRAGGLAEGYLGLPELNAEKFV--NNWFVD--PSHwidldkennkPEREfwlgprDRLYR 681
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6001 TGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHH------VRECLPEARQ------LAVEVILPsgQKDHAMLAAF 6068
Cdd:TIGR03443  682 TGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHlsqhplVRENVTLVRRdkdeepTLVSYIVP--QDKSDELEEF 759
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6069 VqleegtqnALLDKEASGEdsmaQVV--------FLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLreiga 6140
Cdd:TIGR03443  760 K--------SEVDDEESSD----PVVkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL----- 822
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6141 SF--TAQQIANMQTSSQDPKRQPSTEAEQTMQKLWAQVLGIELNGIGLDDSFFRLGGDSIAAMKLVGEARR---IGLQLS 6215
Cdd:TIGR03443  823 PFpdTAQLAAVAKNRSASAADEEFTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKklnVELPLG 902
                          970
                   ....*....|....*
gi 1820002560 6216 VadIFRYARLVDLAS 6230
Cdd:TIGR03443  903 L--IFKSPTIKGFAK 915
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
7366-8215 2.22e-52

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 206.45  E-value: 2.22e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7366 PLPSTVTQPVADTTVE-YQCPPLSKATLDTTTS----TLIRAAWAIVTSCYTSSDDVVYGTtvtgrNAPIAGVEAMVGPT 7440
Cdd:TIGR03443   13 VLPHDYLRPANNRLVEaTYSLQLPSAEVTAGGGstpfIILLAAFAALVYRLTGDEDIVLGT-----SSNKSGRPFVLRLN 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7441 I-ATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEqtgLQHIAKLGSGPrhacgfqTLLVVQPVDDVLGSDDMLGEwrsy 7519
Cdd:TIGR03443   88 ItPELSFLQLYAKVSEEEKEGASDIGVPFDELSEH---IQAAKKLERTP-------PLFRLAFQDAPDNQQTTYST---- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7520 skmqdFTTYALMVQFTLAAEGVQITASFDARVIEHWVLEKMLRQFSfimQQLAEASEDSK--VADIDTTTPEDRQQLWAW 7597
Cdd:TIGR03443  154 -----GSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLA---QLLSAASSNPDepIGKVSLITPSQKSLLPDP 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7598 NADVPPAIER-CVHDLFAEQARARPGAPAIC----AWDG-----ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKS 7667
Cdd:TIGR03443  226 TKDLDWSGFRgAIHDIFADNAEKHPDRTCVVetpsFLDPssktrSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRG 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7668 MWTVVAMLAVLKAGGAFVPLDPDHPASRhEEIFEQTG---AQVVVASA----QYSARWTSSSCHVVTVSKA--------- 7731
Cdd:TIGR03443  306 VDLVVAVMGVLKAGATFSVIDPAYPPAR-QTIYLSVAkprALIVIEKAgtldQLVRDYIDKELELRTEIPAlalqddgsl 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7732 ------------LSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFAS 7799
Cdd:TIGR03443  385 vggsleggetdvLAPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSG 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7800 YTFDACIAEIITTLLCGGCICVPSDSDRRN--SLAKAISTMDVNWAFLTPSVARLLDPG---LIPSLKILAIGGEQSSSA 7874
Cdd:TIGR03443  465 IAHDPIQRDMFTPLFLGAQLLVPTADDIGTpgRLAEWMAKYGATVTHLTPAMGQLLSAQattPIPSLHHAFFVGDILTKR 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7875 DWNRWPG---SVQKIHVYGPTECCIFCTGYTTKQGFEPSTI----------GTSVASVSW-VVDPENHNRLAPLGSMGEL 7940
Cdd:TIGR03443  545 DCLRLQTlaeNVCIVNMYGTTETQRAVSYFEIPSRSSDSTFlknlkdvmpaGKGMKNVQLlVVNRNDRTQTCGVGEVGEI 624
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7941 LMEGPILARGYLNDVDKTEAAFIddPAWLLEgyPGH----------PGRQ------GRLYKTGDLVQYNADGNLVYLGRK 8004
Cdd:TIGR03443  625 YVRAGGLAEGYLGLPELNAEKFV--NNWFVD--PSHwidldkennkPEREfwlgprDRLYRTGDLGRYLPDGNVECCGRA 700
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8005 DSQVKVRGQRVELGEVEHH------VREclpearqlavEVILPSGQKNH--AMLAVFVQLGKGTHIAHLEEKAGGEDSMA 8076
Cdd:TIGR03443  701 DDQVKIRGFRIELGEIDTHlsqhplVRE----------NVTLVRRDKDEepTLVSYIVPQDKSDELEEFKSEVDDEESSD 770
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8077 QVV--------FLTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLreigaSF--TAQQLAETQTSSQGPKRQP 8146
Cdd:TIGR03443  771 PVVkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL-----PFpdTAQLAAVAKNRSASAADEE 845
                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8147 LTEAEQTMQQLWARVLGIDADIIGLDDSFFRLGGDSIAAMKLVGEARRT-GLQLSVADIFRHPRLIDLAS 8215
Cdd:TIGR03443  846 FTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKlNVELPLGLIFKSPTIKGFAK 915
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
6716-7041 1.11e-51

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 192.14  E-value: 1.11e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6716 PNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIL 6795
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6796 RQTGAQVILASAQNT------------------------------------------TLFQSS----------------- 6816
Cdd:cd17643     81 ADSGPSLLLTDPDDLayviytsgstgrpkgvvvshanvlalfaatqrwfgfneddvwTLFHSYafdfsvweiwgallhgg 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6817 ----------------------------NQT-----------------------VV------------------------ 6821
Cdd:cd17643    161 rlvvvpyevarspedfarllrdegvtvlNQTpsafyqlveaadrdgrdplalryVIfggealeaamlrpwagrfgldrpq 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6822 ----------TVNRSSYILFPDE--NREAYPFVRP----------SNAALAPLGSIGELLVEGPILARGYLNDADKTAAA 6879
Cdd:cd17643    241 lvnmygitetTVHVTFRPLDAADlpAAAASPIGRPlpglrvyvldADGRPVPPGVVGELYVSGAGVARGYLGRPELTAER 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6880 FVNDPAWLveghgkhPGRRgrLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLRECmPRATQMAVEVisp 6959
Cdd:cd17643    321 FVANPFGG-------PGSR--MYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATH-PSVRDAAVIV--- 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6960 aGAAEQAKTMVVAFLQLNDEARDAllggnvpnddnlsaqvvfPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRK 7039
Cdd:cd17643    388 -REDEPGDTRLVAYVVADDGAAAD------------------IAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRA 448

                   ..
gi 1820002560 7040 RL 7041
Cdd:cd17643    449 AL 450
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
2-283 2.04e-51

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 192.03  E-value: 2.04e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL---EPSHIPSLRILVMGGEQVnSADW-----DRWPSsVQTINGYGPTECCIVCTGYTSEQDFTTG 73
Cdd:cd12117    226 GVTVLWLTAALFNQLadeDPECFAGLRELLTGGEVV-SPPHvrrvlAACPG-LRLVNGYGPTENTTFTTSHVVTELDEVA 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   74 T---IGTSIASVS-WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAwlleghggyaGRQGRLYKT 149
Cdd:cd12117    304 GsipIGRPIANTRvYVLD--EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF----------GPGERLYRT 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  150 GDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAVEVVLPLGQKNHatLAAFiqldkgthnallk 229
Cdd:cd12117    372 GDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAH-PGVREAVVVVREDAGGDKR--LVAY------------- 435
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560  230 ekVGGDDSIArvvfLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd12117    436 --VVAEGALD----AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
2-284 3.48e-51

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 190.66  E-value: 3.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPS-------VARLLEPSHIPSLRILVMGGEQVNSADWDRW-PSSVQTINGYGPTECCIVCTGYTSEQDFTTG 73
Cdd:cd17649    185 GVTVLDLPPAylqqlaeEADRTGDGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARA 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   74 ----TIGTSIASVS-WVVDPkdHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawlleghggYAGRQGRLYK 148
Cdd:cd17649    265 gasmPIGRPLGGRSaYILDA--DLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDP---------FGAPGSRLYR 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  149 TGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVEVVLPLGQKnhaTLAAFIQLDKGTHNALL 228
Cdd:cd17649    334 TGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLE-HPGVREAAVVALDGAGGK---QLVAYVVLRAAAAQPEL 409
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560  229 KekvggddsiarvvflAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLR 284
Cdd:cd17649    410 R---------------AQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
PRK12467 PRK12467
peptide synthase; Provisional
2-377 6.97e-51

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 202.70  E-value: 6.97e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL----EPSHIPSLRILVMGGEQV---NSADWDRWPSSVQTINGYGPTECCIVCTGYTSEQDFTTGT 74
Cdd:PRK12467  3327 RISIACFPPAYLQQFaedaGGADCASLDIYVFGGEAVppaAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEA 3406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   75 ----IGTSIASVS-WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawlleghggYAGRQGRLYKT 149
Cdd:PRK12467  3407 pyapIGRPVAGRSiYVLD--GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP---------FSGSGGRLYRT 3475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  150 GDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVEVVLPLGQKNhatLAAFIQLDkgTHNALLK 229
Cdd:PRK12467  3476 GDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQ-HPSVREAVVLARDGAGGKQ---LVAYVVPA--DPQGDWR 3549
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  230 EKVGGDdsiarvvflagveeeLAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASFTAQQLAemrtssqgpkrqP 309
Cdd:PRK12467  3550 ETLRDH---------------LAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA------------P 3602
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560  310 STEAERTMQQLWARVLGIEpdSIGLDDSFFRLGGDSIAAIKLVGEARR-TGLQPSVADIFRHPTLAALA 377
Cdd:PRK12467  3603 RSEVEQQLAAIWADVLGVE--QVGVTDNFFELGGDSLLALQVLSRIRQsLGLKLSLRDLMSAPTIAELA 3669
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
2-284 1.74e-50

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 189.48  E-value: 1.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL------EPSHIPSLRILVMGGEQVNS----ADWDRWPSSVQTINGYGPTECCIVcTGYTSEQDFT 71
Cdd:cd17651    227 RISRVFLPTVALRALaehgrpLGVRLAALRYLLTGGEQLVLtedlREFCAGLPGLRLHNHYGPTETHVV-TALSLPGDPA 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   72 ----TGTIGTSIASVS-WVVDPkdHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAwlleghggyaGRQGRL 146
Cdd:cd17651    306 awpaPPPIGRPIDNTRvYVLDA--ALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF----------VPGARM 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  147 YKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAVeVVLPLGQkNHATLAAFIQLDKGthna 226
Cdd:cd17651    374 YRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARH-PGVREAVV-LAREDRP-GEKRLVAYVVGDPE---- 446
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560  227 llkekvggddsiaRVVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLR 284
Cdd:cd17651    447 -------------APVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
6705-7041 1.84e-50

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 189.41  E-value: 1.84e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6705 HDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 6784
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6785 DHPASRHEDILRQTGAQVILASA--------------------------------------------------------- 6807
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTAdlaarlpaggdvallgdealaappatpplvpprpdnlayviytsgstgrpkgvmvth 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6808 -----------------------QNTTL----------------------------------------------FQSS-- 6816
Cdd:cd17646    161 agivnrllwmqdeyplgpgdrvlQKTPLsfdvsvwelfwplvagarlvvarpgghrdpaylaalirehgvttchFVPSml 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6817 ------------------------------------------NQ---TVVTVNRSSYILFPDENREAYPFVRP-SNAAL- 6849
Cdd:cd17646    241 rvflaepaagscaslrrvfcsgealppelaarflalpgaelhNLygpTEAAIDVTHWPVRGPAETPSVPIGRPvPNTRLy 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6850 --------APLGSIGELLVEGPILARGYLNDADKTAAAFVNDPAwlveGHGkhpgrrGRLYKTGDLVYYNKDGNLVYIGR 6921
Cdd:cd17646    321 vlddalrpVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF----GPG------SRMYRTGDLARWRPDGALEFLGR 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 KDGQVKVRGQRVELGEIENRLRECmPRATQMAVEVISPAGAAEQaktmVVAFLQLNDEARDALlggnvpnddnlsaqvvf 7001
Cdd:cd17646    391 SDDQVKIRGFRVEPGEIEAALAAH-PAVTHAVVVARAAPAGAAR----LVGYVVPAAGAAGPD----------------- 448
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 7002 PAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd17646    449 TAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
856-1366 5.43e-50

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 187.39  E-value: 5.43e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  856 DLFAEQARARPDASAvCAWDGE-LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 934
Cdd:cd05936      3 DLLEEAARRFPDKTA-LIFMGRkLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  935 GHPASRHEEIFKQIGAQVVLTSSQHAMLFASSERHQVTVskvstsqlptvvnfaksPVDPGNTAYIIFTSGTTGIPKGVV 1014
Cdd:cd05936     82 LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERV-----------------ALTPEDVAVLQYTSGTTGVPKGAM 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1015 LQHR---AVTTSCLGHGEAFGYTDHaRVLQ----FASYTFDACiaeIITTLLYGGCIC-VPSESDRR--NNLAK------ 1078
Cdd:cd05936    145 LTHRnlvANALQIKAWLEDLLEGDD-VVLAalplFHVFGLTVA---LLLPLALGATIVlIPRFRPIGvlKEIRKhrvtif 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1079 -AISTMDVncALLTPSVARLLEPSAVpslkRLVLQG-----EQVsFADWNRWPGsVQTINGYGPTECS--VCCNTYSGKQ 1150
Cdd:cd05936    221 pGVPTMYI--ALLNAPEFKKRDFSSL----RLCISGgaplpVEV-AERFEELTG-VPIVEGYGLTETSpvVAVNPLDGPR 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1151 gfKSGIIGTSVASLSW-VVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpaWLlegyeghagrrgrly 1229
Cdd:cd05936    293 --KPGSIGIPLPGTEVkIVDD--DGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG--WL--------------- 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1230 KTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhhvrECL---PEARQLAVeVILPSGQKEHAlLAAFIQLDKGnh 1306
Cdd:cd05936    352 RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVE----EVLyehPAVAEAAV-VGVPDPYSGEA-VKAFVVLKEG-- 423
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1307 nalfeEKASGEDSMAQvvfltgveeeLAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQ 1366
Cdd:cd05936    424 -----ASLTEEEIIAF----------CREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
4542-5148 7.89e-50

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 198.37  E-value: 7.89e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4542 CVHDQFAEQARARPD------TPAICAWDG---ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVL 4612
Cdd:TIGR03443  237 AIHDIFADNAEKHPDrtcvveTPSFLDPSSktrSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVL 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4613 KAGGAFVPLDPDHPASRhEHIFRQTG---AQVVLASAqyatlwTSLGRSVV--------IVSEASTSQL----------- 4670
Cdd:TIGR03443  317 KAGATFSVIDPAYPPAR-QTIYLSVAkprALIVIEKA------GTLDQLVRdyidkeleLRTEIPALALqddgslvggsl 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4671 ---------PVVTKTADPS---VNPGNAAYAIFTSGSTGIPKGVVLEHKAvvtscLGH-----GQAFGITDHTRVLQFAS 4733
Cdd:TIGR03443  390 eggetdvlaPYQALKDTPTgvvVGPDSNPTLSFTSGSEGIPKGVLGRHFS-----LAYyfpwmAKRFGLSENDKFTMLSG 464
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4734 YTFDACIAEIITTLLCCGCICVPSDSDRRN--NLAKAINAMDVNWALLTPSVARMLdpcVVQ------SLKILVLGGEQV 4805
Cdd:TIGR03443  465 IAHDPIQRDMFTPLFLGAQLLVPTADDIGTpgRLAEWMAKYGATVTHLTPAMGQLL---SAQattpipSLHHAFFVGDIL 541
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4806 NSADWDRwpksIQT-------INAYGPTECS-----ICCTTYSGKQGF--KSGTI---GTSIVSVSW-VVDPENHNRLAP 4867
Cdd:TIGR03443  542 TKRDCLR----LQTlaenvciVNMYGTTETQravsyFEIPSRSSDSTFlkNLKDVmpaGKGMKNVQLlVVNRNDRTQTCG 617
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4868 LGSIGELLVEGPILARGYLNDMEKTEAAFI---------------DDPAWLLEGYgghSGRQGRLYKTGDLVRYDADGNL 4932
Cdd:TIGR03443  618 VGEVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfvdpshwidldkENNKPEREFW---LGPRDRLYRTGDLGRYLPDGNV 694
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4933 VYLGRKDSQVKLRGQRVELGEVEHH------VRECLT-------EAKQLaVEVIVPEGEGgyAMLAAFVQLGDDT----- 4994
Cdd:TIGR03443  695 ECCGRADDQVKIRGFRIELGEIDTHlsqhplVRENVTlvrrdkdEEPTL-VSYIVPQDKS--DELEEFKSEVDDEessdp 771
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4995 -------YNTLVKEkaggdsltvqvvfldrVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLreigaSF--TAQQ 5065
Cdd:TIGR03443  772 vvkglikYRKLIKD----------------IREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL-----PFpdTAQL 830
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5066 LAEMRTSSQGPKRQPSTEAERTMQQLWTRVLGIELNGIGLDDSFFRLGGDSIAAMKLVGEARRT-GLQLSVADVFRHPRL 5144
Cdd:TIGR03443  831 AAVAKNRSASAADEEFTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKlNVELPLGLIFKSPTI 910

                   ....
gi 1820002560 5145 VDLA 5148
Cdd:TIGR03443  911 KGFA 914
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
6704-7041 1.35e-49

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 185.60  E-value: 1.35e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6704 VHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 6783
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6784 PDHPASRHEDILRQ------------------------------------------------------------------ 6797
Cdd:cd12115     81 PAYPPERLRFILEDaqarlvltdpddlayviytsgstgrpkgvaiehrnaaaflqwaaaafsaeelagvlastsicfdls 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6798 ---------TGAQVILA----------SAQNTTL--------------------------------------FQSSNQTV 6820
Cdd:cd12115    161 vfelfgplaTGGKVVLAdnvlalpdlpAAAEVTLintvpsaaaellrhdalpasvrvvnlageplprdlvqrLYARLQVE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6821 VTVN---------RSSYILFPDENREAYPFVRP----------SNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFV 6881
Cdd:cd12115    241 RVVNlygpsedttYSTVAPVPPGASGEVSIGRPlantqayvldRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6882 NDPawlveghgKHPGRRgrLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAG 6961
Cdd:cd12115    321 PDP--------FGPGAR--LYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRS-IPGVREAVVVAIGDAA 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6962 AAEQaktmVVAFLQLndEARDALLggnvpnddnlsaqvvfPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd12115    390 GERR----LVAYIVA--EPGAAGL----------------VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
3-285 2.26e-49

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 184.82  E-value: 2.26e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    3 VNWALLTPSVARLLEPSHIPSLRILVMGGEQVNSADWDRWPSSVQTINGYGPTECCIVCTgYTSEQDFTTGTIGTSIASV 82
Cdd:cd17653    190 VDALMSTPSILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISST-MTELLPGQPVTIGKPIPNS 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   83 S-WVVDPKDhgRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAWllegHGGyagrqgRLYKTGDLVRYDADGNL 161
Cdd:cd17653    269 TcYILDADL--QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW----PGS------RMYRTGDYGRWTEDGGL 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  162 VCLGRKDSQVKLRGQRVELGEVEHHVRECLPEAKQLAVEVVlplgqknHATLAAFIQldkgthnallkekvggDDSIArv 241
Cdd:cd17653    337 EFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVV-------NGRLVAFVT----------------PETVD-- 391
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1820002560  242 vfLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:cd17653    392 --VDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
6706-7043 2.39e-49

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 184.43  E-value: 2.39e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6706 DLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 6785
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6786 HPASRHEDILRQTGAQVIL-ASAQN------------------------------------------------------- 6809
Cdd:cd17653     81 LPSARIQAILRTSGATLLLtTDSPDdlayiiftsgstgipkgvmvphrgvlnyvsqpparldvgpgsrvaqvlsiafdac 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6810 ------------TTLFQSSNQTVVTVNRSSYIL--------------FPD--------------------ENRE------ 6837
Cdd:cd17653    161 igeifstlcnggTLVLADPSDPFAHVARTVDALmstpsilstlspqdFPNlktiflggeavppslldrwsPGRRlynayg 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6838 --------AYPFVRP-------------------SNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPAWlveg 6890
Cdd:cd17653    241 ptectissTMTELLPgqpvtigkpipnstcyildADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW---- 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6891 HGKhpgrrgRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLRECMPRATqmavevispagaaeQAKTMV 6970
Cdd:cd17653    317 PGS------RMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVT--------------QAAAIV 376
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 6971 VaflqlndeardallggnvpnDDNLSAQVVfPAKVD-----EKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:cd17653    377 V--------------------NGRLVAFVT-PETVDvdglrSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
4687-5050 2.53e-49

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 181.33  E-value: 2.53e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4687 AYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLcCGCICVPSDSDRRNNLA 4766
Cdd:cd04433      3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALL-AGGTVVLLPKFDPEAAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4767 KAINAMDVNWALLTPSVARML------DPCVVQSLKILVLGGEQVNSADWDRWPKS--IQTINAYGPTECSICCTTYSGK 4838
Cdd:cd04433     82 ELIEREKVTILLGVPTLLARLlkapesAGYDLSSLRALVSGGAPLPPELLERFEEApgIKLVNGYGLTETGGTVATGPPD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4839 QG-FKSGTIGTSIVSVSW-VVDPEnhNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDdpawlleGYgghsgrqgr 4916
Cdd:cd04433    162 DDaRKPGSVGRPVPGVEVrIVDPD--GGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GW--------- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4917 lYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE-----HH-VREClteakqlAVeVIVPEGEGGYAmLAAFVQL 4990
Cdd:cd04433    224 -YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEavllgHPgVAEA-------AV-VGVPDPEWGER-VVAVVVL 293
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 4991 GDdtyntlvkekagGDSLTVQVVfLDRVEEELAK-RVPEHmmlttFFTLEAMPTTTSGKID 5050
Cdd:cd04433    294 RP------------GADLDAEEL-RAHVRERLAPyKVPRR-----VVFVDALPRTASGKID 336
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
4545-5055 1.07e-48

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 183.92  E-value: 1.07e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4545 DQFAEQARARPDTPAiCAWDGE-LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 4623
Cdd:cd05936      3 DLLEEAARRFPDKTA-LIFMGRkLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4624 DHPASRHEHIFRQTGAQVVLASAQYATLwtslgrsvvIVSEASTSQLPVVTktadpsvnPGNAAYAIFTSGSTGIPKGVV 4703
Cdd:cd05936     82 LYTPRELEHILNDSGAKALIVAVSFTDL---------LAAGAPLGERVALT--------PEDVAVLQYTSGTTGVPKGAM 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4704 LEHK---AVVTSCLGHGQaFGITDHTRVLQ----FASYTFDACIaeiiTTLLCCGC--ICVPSDSDRrnNLAKAINAMDV 4774
Cdd:cd05936    145 LTHRnlvANALQIKAWLE-DLLEGDDVVLAalplFHVFGLTVAL----LLPLALGAtiVLIPRFRPI--GVLKEIRKHRV 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4775 NW---------ALLTPSVARMLDPcvvQSLKILVLGGEQVNSADWDRWPKSIQT--INAYGPTECS--ICCTTYSGKQgf 4841
Cdd:cd05936    218 TIfpgvptmyiALLNAPEFKKRDF---SSLRLCISGGAPLPVEVAERFEELTGVpiVEGYGLTETSpvVAVNPLDGPR-- 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4842 KSGTIGTSIVSVSW-VVDPENHnrLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpaWLlegygghsgrqgrlyKT 4920
Cdd:cd05936    293 KPGSIGIPLPGTEVkIVDDDGE--ELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG--WL---------------RT 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4921 GDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhhvrECLTE--AKQLAVEVIVPEGEGGYAmLAAFVQLgddtyntl 4998
Cdd:cd05936    354 GDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVE----EVLYEhpAVAEAAVVGVPDPYSGEA-VKAFVVL-------- 420
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 4999 vKEkagGDSLTvqvvfldrvEEELAK---------RVPEHMmltTFftLEAMPTTTSGKIDRKRLR 5055
Cdd:cd05936    421 -KE---GASLT---------EEEIIAfcreqlagyKVPRQV---EF--RDELPKSAVGKILRRELR 468
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
3487-3974 2.91e-48

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 181.90  E-value: 2.91e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASA 3566
Cdd:cd17654     17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3567 QysARWTSSSCHVVTVSKALSSqlpavvdstntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNlS 3646
Cdd:cd17654     97 E--LDNAPLSFTPEHRHFNIRT--------------DECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS-E 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3647 RVLQFAS-YTFDACIAEIITTLLCGGCICVPSDSDRRNS--LAKAISTMD-VNWAFLTPSVARLLDPGLIP--------S 3714
Cdd:cd17654    160 DILFLTSpLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPskLADILFKRHrITVLQATPTLFRRFGSQSIKstvlsatsS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3715 LKILAIGGEQSSSADWNR-WPGSVQKIHV---YGPTECCIFCTGYTTKQGFEPSTIGTSV-ASVSWVVDPENHNrlaplg 3789
Cdd:cd17654    240 LRVLALGGEPFPSLVILSsWRGKGNRTRIfniYGITEVSCWALAYKVPEEDSPVQLGSPLlGTVIEVRDQNGSE------ 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3790 SMGELLMEGpiLARGYlndvdkteaaFIDDPawllegypgHPGRQGRLYKTGDLVQYNaDGNLVYLGRKDSQVKVRGQRV 3869
Cdd:cd17654    314 GTGQVFLGG--LNRVC----------ILDDE---------VTVPKGTMRATGDFVTVK-DGELFFLGRKDSQIKRRGKRI 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3870 ELGEVEHHVRECLPEarqLAVEVILpsgqKDHAMLAAFVQLEEGTqnalldkeaggedsmaqvvflASVEEELAK-RLPE 3948
Cdd:cd17654    372 NLDLIQQVIESCLGV---ESCAVTL----SDQQRLIAFIVGESSS---------------------SRIHKELQLtLLSS 423
                          490       500
                   ....*....|....*....|....*.
gi 1820002560 3949 HMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd17654    424 HAIPDTFVQIDKLPLTSHGKVDKSEL 449
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
5626-6136 3.23e-48

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 182.38  E-value: 3.23e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAiCAWDGE-LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 5704
Cdd:cd05936      3 DLLEEAARRFPDKTA-LIFMGRkLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5705 DHPASRHEDTFRHTGAQVVVtsaqhsarwigtnhqVVTVSAGSLGQLSTLVNPVGLPaiPENAVYIMFTSGSTGIPKGVV 5784
Cdd:cd05936     82 LYTPRELEHILNDSGAKALI---------------VAVSFTDLLAAGAPLGERVALT--PEDVAVLQYTSGTTGVPKGAM 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5785 LEHR---AVVTSCW--------GRGRAFGITNLsrvlqFASYTFDACMdeiITTLMYGGCIC-VPSDSDRRndLVKAIST 5852
Cdd:cd05936    145 LTHRnlvANALQIKawledlleGDDVVLAALPL-----FHVFGLTVAL---LLPLALGATIVlIPRFRPIG--VLKEIRK 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5853 MDVS--CAlltpsvarllepssVPTLQMLVLQGEQVSFADWNRW--------PASVQTIN------------GYGPTECS 5910
Cdd:cd05936    215 HRVTifPG--------------VPTMYIALLNAPEFKKRDFSSLrlcisggaPLPVEVAErfeeltgvpiveGYGLTETS 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5911 --ICCNTYSGKQgfKSGIIGTSVASVSW-VVDPEnhDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpaWLleg 5987
Cdd:cd05936    281 pvVAVNPLDGPR--KPGSIGIPLPGTEVkIVDDD--GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG--WL--- 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5988 ypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECL---PEARQLAVeVILPSGQKDHAm 6064
Cdd:cd05936    352 ------------RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVE----EVLyehPAVAEAAV-VGVPDPYSGEA- 413
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 6065 LAAFVQLEEGtqnalldkeasgedsmaqvvflASVEEE-----LAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:cd05936    414 VKAFVVLKEG----------------------ASLTEEeiiafCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
6716-7041 4.14e-48

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 182.11  E-value: 4.14e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6716 PNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIL 6795
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6796 RQ------------------------------------------------------------------------------ 6797
Cdd:cd12116     81 EDaepalvltddalpdrlpaglpvlllalaaaaaapaaprtpvspddlayviytsgstgrpkgvvvshrnlvnflhsmre 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6798 ------------------------------TGAQVILASAQNTT-------LFQSSNQTVVTVNRSSYILFPD---ENR- 6836
Cdd:cd12116    161 rlglgpgdrllavttyafdisllelllpllAGARVVIAPRETQRdpealarLIEAHSITVMQATPATWRMLLDagwQGRa 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6837 --------EAYP------------------------------FVRPSNAAL--------------------APLGSIGEL 6858
Cdd:cd12116    241 gltalcggEALPpdlaarllsrvgslwnlygptettiwstaaRVTAAAGPIpigrplantqvyvldaalrpVPPGVPGEL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6859 LVEGPILARGYLNDADKTAAAFVNDPawlveghgkHPGRRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEI 6938
Cdd:cd12116    321 YIGGDGVAQGYLGRPALTAERFVPDP---------FAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEI 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6939 ENRLREcMPRATQMAVEVIspagaAEQAKTMVVAFLQLNDeardallgGNVPNDDNLSAqvvfpakvdeKLSNLLPSYMM 7018
Cdd:cd12116    392 EAALAA-HPGVAQAAVVVR-----EDGGDRRLVAYVVLKA--------GAAPDAAALRA----------HLRATLPAYMV 447
                          490       500
                   ....*....|....*....|...
gi 1820002560 7019 PEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd12116    448 PSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
7633-8120 5.63e-48

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 181.13  E-value: 5.63e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASA 7712
Cdd:cd17654     17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7713 QysARWTSSSCHVVTVSKALSSqlpavvdstntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNlS 7792
Cdd:cd17654     97 E--LDNAPLSFTPEHRHFNIRT--------------DECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS-E 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7793 RVLQFAS-YTFDACIAEIITTLLCGGCICVPSDSDRRNS--LAKAISTMD-VNWAFLTPSVARLLDPGLIP--------S 7860
Cdd:cd17654    160 DILFLTSpLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPskLADILFKRHrITVLQATPTLFRRFGSQSIKstvlsatsS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7861 LKILAIGGEQSSSADWNR-WPGSVQKIHV---YGPTECCIFCTGYTTKQGFEPSTIGTSV-ASVSWVVDPENHNrlaplg 7935
Cdd:cd17654    240 LRVLALGGEPFPSLVILSsWRGKGNRTRIfniYGITEVSCWALAYKVPEEDSPVQLGSPLlGTVIEVRDQNGSE------ 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7936 SMGELLMEGpiLARGYlndvdkteaaFIDDPawllegypgHPGRQGRLYKTGDLVQYNaDGNLVYLGRKDSQVKVRGQRV 8015
Cdd:cd17654    314 GTGQVFLGG--LNRVC----------ILDDE---------VTVPKGTMRATGDFVTVK-DGELFFLGRKDSQIKRRGKRI 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8016 ELGEVEHHVRECLPEarqLAVEVILPSGQKnhaMLAVFVQLGKGTHIAHleekaggedsmaqvvfltgteeELAK-RLPK 8094
Cdd:cd17654    372 NLDLIQQVIESCLGV---ESCAVTLSDQQR---LIAFIVGESSSSRIHK----------------------ELQLtLLSS 423
                          490       500
                   ....*....|....*....|....*.
gi 1820002560 8095 HMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd17654    424 HAIPDTFVQIDKLPLTSHGKVDKSEL 449
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
6708-7042 1.58e-47

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 181.00  E-value: 1.58e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6708 FTEQALARPNAPAVcAWDGE-LTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 6786
Cdd:cd17651      1 FERQAARTPDAPAL-VAEGRrLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6787 PASRHEDILRQTGAQVILA-----------------SAQNTTLFQSSNQTVVTVNRSS--YILF---------------- 6831
Cdd:cd17651     80 PAERLAFMLADAGPVLVLThpalagelavelvavtlLDQPGAAAGADAEPDPALDADDlaYVIYtsgstgrpkgvvmphr 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6832 -------------------------------------------------PDENRE-------------------AYPFVR 6843
Cdd:cd17651    160 slanlvawqarasslgpgartlqfaglgfdvsvqeifstlcagatlvlpPEEVRTdppalaawldeqrisrvflPTVALR 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6844 -------------------------------------------------PSNAALA------------------------ 6850
Cdd:cd17651    240 alaehgrplgvrlaalrylltggeqlvltedlrefcaglpglrlhnhygPTETHVVtalslpgdpaawpapppigrpidn 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 -------------PLGSIGELLVEGPILARGYLNDADKTAAAFVNDPAwlveghgkhpGRRGRLYKTGDLVYYNKDGNLV 6917
Cdd:cd17651    320 trvyvldaalrpvPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF----------VPGARMYRTGDLARWLPDGELE 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6918 YIGRKDGQVKVRGQRVELGEIENRLRECmPRATQMAVeVISPAGAAEQAktmVVAFLQLNDEARDallggnvpnddnlsa 6997
Cdd:cd17651    390 FLGRADDQVKIRGFRIELGEIEAALARH-PGVREAVV-LAREDRPGEKR---LVAYVVGDPEAPV--------------- 449
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 6998 qvvFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLR 7042
Cdd:cd17651    450 ---DAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
10-283 1.65e-47

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 179.82  E-value: 1.65e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   10 PSVAR-LLEPSHIP-SLRILVMGGEQVNS---ADWDRWPSSVQTINGYGPTECCIVCTGY-TSEQDFTTGTIGTSIA-SV 82
Cdd:cd12115    199 PSAAAeLLRHDALPaSVRVVNLAGEPLPRdlvQRLYARLQVERVVNLYGPSEDTTYSTVApVPPGASGEVSIGRPLAnTQ 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   83 SWVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAwllegHGGyagrqGRLYKTGDLVRYDADGNLV 162
Cdd:cd12115    279 AYVLD--RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF-----GPG-----ARLYRTGDLVRWRPDGLLE 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  163 CLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQlAVeVVLPLGQKNHATLAAFIQLDKGthnallkekvggddsiaRVV 242
Cdd:cd12115    347 FLGRADNQVKVRGFRIELGEIEAALRS-IPGVRE-AV-VVAIGDAAGERRLVAYIVAEPG-----------------AAG 406
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1820002560  243 FLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd12115    407 LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
997-1361 1.90e-47

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 175.94  E-value: 1.90e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  997 TAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCIcVPSESDRRNNL 1076
Cdd:cd04433      2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTV-VLLPKFDPEAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1077 AKAISTMDVNCALLTPSVARLL------EPSAVPSLKRLVLQGEQVSFADWNRW---PGsVQTINGYGPTECSVCCNTYS 1147
Cdd:cd04433     81 LELIEREKVTILLGVPTLLARLlkapesAGYDLSSLRALVSGGAPLPPELLERFeeaPG-IKLVNGYGLTETGGTVATGP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1148 GKQG-FKSGIIGTSVASLSW-VVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDdpawlleGYeghagrr 1225
Cdd:cd04433    160 PDDDaRKPGSVGRPVPGVEVrIVDP--DGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GW------- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1226 grlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREClPEARQLAVeVILPSGQKEHAlLAAFIQLDKGn 1305
Cdd:cd04433    224 ---YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGH-PGVAEAAV-VGVPDPEWGER-VVAVVVLRPG- 296
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 1306 HNALFEEkasgedsmaqvvfltgVEEELAKRLPEHMVPTILFTVKAMPITTSGKID 1361
Cdd:cd04433    297 ADLDAEE----------------LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
2-283 2.91e-47

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 179.41  E-value: 2.91e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL---EPSHIPSLRILVmGGEQVNSADWDRWPSSV-QTINGYGPTECCIVCTGYTSEQDFTTGTIGT 77
Cdd:cd12116    217 SITVMQATPATWRMLldaGWQGRAGLTALC-GGEALPPDLAARLLSRVgSLWNLYGPTETTIWSTAARVTAAAGPIPIGR 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   78 SIASVS-WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawlleghggYAGRQGRLYKTGDLVRYD 156
Cdd:cd12116    296 PLANTQvYVLD--AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDP---------FAGPGSRLYRTGDLVRRR 364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  157 ADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVeVVLPLGQKnhATLAAFIQLDKGThnallkekvGGDd 236
Cdd:cd12116    365 ADGRLEYLGRADGQVKIRGHRIELGEIEAALAA-HPGVAQAAV-VVREDGGD--RRLVAYVVLKAGA---------APD- 430
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560  237 siarvvfLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd12116    431 -------AAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
3022-3430 3.02e-47

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 178.17  E-value: 3.02e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3022 VFPCTPMQEGIL--TSQGKDPDAYWVCFIYEVipnqETSISLARLQQAWKGVVHQHSLLRTLLVDnvPGSTGTTNVVLKD 3099
Cdd:cd19543      1 IYPLSPMQEGMLfhSLLDPGSGAYVEQMVITL----EGPLDPDRFRAAWQAVVDRHPILRTSFVW--EGLGEPLQVVLKD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3100 PQPSISVF------SSEGTATIELFRSR-----YNPAAQRSIgqlqhHLSICQLNNGKVYLCLDINHAIIDAHSRGILMH 3168
Cdd:cd19543     75 RKLPWRELdlshlsEAEQEAELEALAEEdrergFDLARAPLM-----RLTLIRLGDDRYRLVWSFHHILLDGWSLPILLK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3169 DLQEAYDANLN------PQSTSFRDFASYIKQQSQEEAGRYWAEYLDGVE--PCFFPSLGDSGGANTIPRTV--EVPSID 3238
Cdd:cd19543    150 ELFAIYAALGEgqppslPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEepTPLPKELPADADGSYEPGEVsfELSAEL 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3239 SSAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPLISILPCRIHLHKQLTVLEALK 3318
Cdd:cd19543    230 TARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLK 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3319 TVQENYASSLSFQTFPLASMHSFLGLGTsALFNTAL---------SLQRIDDigpcsASEITLKMKEGLDPTEYNITLSA 3389
Cdd:cd19543    310 DLQAQQLELREHEYVPLYEIQAWSEGKQ-ALFDHLLvfenypvdeSLEEEQD-----EDGLRITDVSAEEQTNYPLTVVA 383
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 3390 gYSKDAIDISMTFRAGCMDLVQAKRLASNFSQAIKAVTTEP 3430
Cdd:cd19543    384 -IPGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
5196-5590 3.29e-47

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 178.03  E-value: 3.29e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5196 MYPCSPLQEGLMSLTAKRAGD--YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVV-------VE 5266
Cdd:cd19536      1 MYPLSSLQEGMLFHSLLNPGGsvYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVhrqaqvpVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5267 EKIQW---TESKRLEEYLREDKAVSMGL-GDRLARYALIKEPYDGgkRW-FVWTIHHALYDGWSLPRILQAVKQIYSG-- 5339
Cdd:cd19536     81 ELDLTpleEQLDPLRAYKEETKIRRFDLgRAPLVRAALVRKDERE--RFlLVISDHHSILDGWSLYLLVKEILAVYNQll 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5340 -----AVPERQPsFNAFIQYLGQQDLEAATL-YWQTALADCKAALFPTLPPTVTQ-PVADTTVEYQCPPPSQSAT----- 5407
Cdd:cd19536    159 eykplSLPPAQP-YRDFVAHERASIQQAASErYWREYLAGATLATLPALSEAVGGgPEQDSELLVSVPLPVRSRSlakrs 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5408 DITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGVEAMVGPTIATVPLRVCLQkDQTVSTLLECLQQQSTDMIA 5487
Cdd:cd19536    238 GIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLS-EETVEDLLKRAQEQELESLS 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5488 HEQTGLQRIAKMSPGARHacgFQTLLVVQPTDdvlgSDDMLGEW-RSYSEMQDF------TTYALMVQCTLAKDRVEVTA 5560
Cdd:cd19536    317 HEQVPLADIQRCSEGEPL---FDSIVNFRHFD----LDFGLPEWgSDEGMRRGLlfsefkSNYDVNLSVLPKQDRLELKL 389
                          410       420       430
                   ....*....|....*....|....*....|
gi 1820002560 5561 SFDARVIEQWVVEKMLRQFGFVMQQLAEAG 5590
Cdd:cd19536    390 AYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
6716-7041 3.85e-47

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 178.22  E-value: 3.85e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6716 PNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIL 6795
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6796 RQTGAQVILASAQN---------TT------------------------------------------------------- 6811
Cdd:cd17652     81 ADARPALLLTTPDNlayviytsgSTgrpkgvvvthrglanlaaaqiaafdvgpgsrvlqfaspsfdasvwellmallaga 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6812 ---------------------------------------------------------------------LFQSSNQTVVT 6822
Cdd:cd17652    161 tlvlapaeellpgepladllrehrithvtlppaalaalppddlpdlrtlvvageacpaelvdrwapgrrMINAYGPTETT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6823 VNRSSYILFPDENREayPFVRP----------SNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPAwlveghg 6892
Cdd:cd17652    241 VCATMAGPLPGGGVP--PIGRPvpgtrvyvldARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPF------- 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6893 KHPGrrGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLRECmpratqmavevisPAGAaeQAktmVVA 6972
Cdd:cd17652    312 GAPG--SRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEH-------------PGVA--EA---VVV 371
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 6973 flqlndeARDALLGGN------VPNDDnlsaQVVFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd17652    372 -------VRDDRPGDKrlvayvVPAPG----AAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
23-379 6.88e-47

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 188.33  E-value: 6.88e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRWPSSVQTI--NGYGPTECCIVCTGYTSEQDFTTGTIGTS--IASVSW-----VVDpkDHGR 93
Cdd:PRK10252   718 SLRQVFCSGEALPADLCREWQQLTGAPlhNLYGPTEAAVDVSWYPAFGEELAAVRGSSvpIGYPVWntglrILD--ARMR 795
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   94 LAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAwlleghggyaGRQGRLYKTGDLVRYDADGNLVCLGRKDSQVKL 173
Cdd:PRK10252   796 PVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF----------APGERMYRTGDVARWLDDGAVEYLGRSDDQLKI 865
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  174 RGQRVELGEVEHHVREcLPEAKQ-LAVEVVLplgqkNHAtlaafiqldkgthnallkEKVGGDDS--IARVV-------F 243
Cdd:PRK10252   866 RGQRIELGEIDRAMQA-LPDVEQaVTHACVI-----NQA------------------AATGGDARqlVGYLVsqsglplD 921
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  244 LAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLreigasfTAQQLAemrtsSQGPKRQPSTEAERTMQQLWAR 323
Cdd:PRK10252   922 TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL-------PLPELK-----AQVPGRAPKTGTETIIAAAFSS 989
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  324 VLGIEPDSIglDDSFFRLGGDSIAAIKLVGEARRT-GLQPSVADIFRHPTLAALASL 379
Cdd:PRK10252   990 LLGCDVVDA--DADFFALGGHSLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLATL 1044
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
2-285 2.16e-46

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 177.52  E-value: 2.16e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLLEPSHI---PSLRILVMGGEQVNSADWDRW----PSSVQTINGYGPTECCIVCTGYTSEQDFTTGT 74
Cdd:cd17655    228 RITIIDLTPAHLKLLDAADDsegLSLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDASIYQYEPETDQQV 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   75 ---IGTSIASVS-WVVDPKdhGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawLLEGhggyagrqGRLYKTG 150
Cdd:cd17655    308 svpIGKPLGNTRiYILDQY--GRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDP--FVPG--------ERMYRTG 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  151 DLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVeVVLPLGQKNHaTLAAFIQLDKgthnallke 230
Cdd:cd17655    376 DLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQ-HPDIKEAVV-IARKDEQGQN-YLCAYIVSEK--------- 443
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  231 kvggddSIArvvfLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:cd17655    444 ------ELP----VAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
6716-7042 4.42e-46

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 175.63  E-value: 4.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6716 PNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIL 6795
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6796 RQTGAQVILAS-------------------------------AQNT---------------------------------- 6810
Cdd:cd17649     81 EDSGAGLLLTHhprqlayviytsgstgtpkgvavshgplaahCQATaerygltpgdrelqfasfnfdgaheqllpplicg 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6811 -----------------------------------------------------------------------------TLF 6813
Cdd:cd17649    161 acvvlrpdelwasadelaemvrelgvtvldlppaylqqlaeeadrtgdgrppslrlyifggealspellrrwlkapvRLF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6814 QSSNQTVVTVNRSSYILFPDENR--EAYPFVRP----------SNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFV 6881
Cdd:cd17649    241 NAYGPTEATVTPLVWKCEAGAARagASMPIGRPlggrsayildADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFV 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6882 NDPAwlveghgKHPGrrGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAG 6961
Cdd:cd17649    321 PDPF-------GAPG--SRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLE-HPGVREAAVVALDGAG 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6962 AaeqakTMVVAFLQLNDEARDALLggnvpnddnlsaqvvfPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd17649    391 G-----KQLVAYVVLRAAAAQPEL----------------RAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449

                   .
gi 1820002560 7042 R 7042
Cdd:cd17649    450 P 450
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
424-820 4.46e-46

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 174.56  E-value: 4.46e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  424 MYLCSPLQEGLMSLTTKRAGD--YIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQVV-------VE 494
Cdd:cd19536      1 MYPLSSLQEGMLFHSLLNPGGsvYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVhrqaqvpVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  495 EKMQWTESES---LEEYLNEDKAASMGL-GDRLARYALIKESCGGKRWFVWTIHHALYDGWSLPLVLDAVKQVYSG---- 566
Cdd:cd19536     81 ELDLTPLEEQldpLRAYKEETKIRRFDLgRAPLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQlley 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  567 --AALERQPSFNTFI-QYVSQQDVKAAAAYWQTALADCEAVLFPPLPSTVTQPVADTTVKYQCPPSPEV-----TSSNIT 638
Cdd:cd19536    161 kpLSLPPAQPYRDFVaHERASIQQAASERYWREYLAGATLATLPALSEAVGGGPEQDSELLVSVPLPVRsrslaKRSGIP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  639 TSTLIRAAWAIIASRYTSSEDIVFGTTVTGRNAPITGVEAMVGPTIATVPLRVRpRKGQTVSAFLENLQQQATEMIAYEQ 718
Cdd:cd19536    241 LSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVT-LSEETVEDLLKRAQEQELESLSHEQ 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  719 TGLQRIMKMGPGPQhacgFQTLLVVHPTDDVlssDDTLGEWhSRSDSELQYF------TTYALTIqcTLAVEGVQITASF 792
Cdd:cd19536    320 VPLADIQRCSEGEP----LFDSIVNFRHFDL---DFGLPEW-GSDEGMRRGLlfsefkSNYDVNL--SVLPKQDRLELKL 389
                          410       420       430
                   ....*....|....*....|....*....|
gi 1820002560  793 D--ARVVEHWVVEKMLGQFSFVMQQLAEAG 820
Cdd:cd19536    390 AynSQVLDEEQAQRLAAYYKSAIAELATAP 419
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
1506-1897 6.57e-46

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 174.17  E-value: 6.57e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1506 IYPCSPLQEGLMSLTAKRAGD--YIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQVVIEENI-QWT 1582
Cdd:cd19536      1 MYPLSSLQEGMLFHSLLNPGGsvYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQvPVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1583 EP---------KSLEEYLSEDKAVSVGL-GDPLARYAFVKEACGGKRWFVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQ 1652
Cdd:cd19536     81 ELdltpleeqlDPLRAYKEETKIRRFDLgRAPLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1653 WQ------PSFNAFI-QYLGQQDLEATVAYWQTALADceaVLFPTLPPTVTQPVADA-----TVEYQCPPLSKAT----S 1716
Cdd:cd19536    161 KPlslppaQPYRDFVaHERASIQQAASERYWREYLAG---ATLATLPALSEAVGGGPeqdseLLVSVPLPVRSRSlakrS 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1717 DTTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNTPVTGVEAMVGPTIATVPVRLRVQrDQTVFAFLQGLQQQATDMIA 1796
Cdd:cd19536    238 GIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLS-EETVEDLLKRAQEQELESLS 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1797 HEQTGLQRIAKMGQGPQhacSFQTLLVVQPVDdvLDNTLGEW-----RDHSELQEFTTYTLMLQCMLAAEGVQITASFD- 1870
Cdd:cd19536    317 HEQVPLADIQRCSEGEP---LFDSIVNFRHFD--LDFGLPEWgsdegMRRGLLFSEFKSNYDVNLSVLPKQDRLELKLAy 391
                          410       420
                   ....*....|....*....|....*...
gi 1820002560 1871 -TRVIEKWVVEKMLRQFSFIMQQLAEAG 1897
Cdd:cd19536    392 nSQVLDEEQAQRLAAYYKSAIAELATAP 419
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
877-1366 1.48e-45

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 175.78  E-value: 1.48e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRheeifkqigaqvvlts 956
Cdd:cd17647     20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR---------------- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  957 sQHAMLFASSERHQVTVSKVStsqlptVVnfakspVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDH 1036
Cdd:cd17647     84 -QNIYLGVAKPRGLIVIRAAG------VV------VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1037 ARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNN--LAKAISTMDVNCALLTPSVARLLEPSAV---PSLKRLVL 1111
Cdd:cd17647    151 DKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPgrLAEWMAKYGATVTHLTPAMGQLLTAQATtpfPKLHHAFF 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1112 QGEQVSFADWNRWPG---SVQTINGYGPTECSVCCN-----TYSGKQGF----KSGI-IGTSVASLSW-VVDAGNHNRLA 1177
Cdd:cd17647    231 VGDILTKRDCLRLQTlaeNVRIVNMYGTTETQRAVSyfevpSRSSDPTFlknlKDVMpAGRGMLNVQLlVVNRNDRTQIC 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1178 PLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpaWLLEgyEGH----------------AGRRGRLYKTGDLVRCDADG 1241
Cdd:cd17647    311 GIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNN--WFVE--PDHwnyldkdnnepwrqfwLGPRDRLYRTGDLGRYLPNG 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1242 NLVCLGRKDSQVKVRGQRVELGEIEHH------VRECLPEARQlavevilpsGQKEHALLAAFI--QLDKGNHNALFEEK 1313
Cdd:cd17647    387 DCECCGRADDQVKIRGFRIELGEIDTHisqhplVRENITLVRR---------DKDEEPTLVSYIvpRFDKPDDESFAQED 457
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 1314 ASGEDSMAQVV--------FLTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQ 1366
Cdd:cd17647    458 VPKEVSTDPIVkgligyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
6703-7041 3.35e-45

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 173.39  E-value: 3.35e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6703 CVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL 6782
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6783 DPDHPASRHEDILRQTGAQVILASAQN------------------------------------------TTLFQS----- 6815
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLTQPENlayviytsgstgkpkgvmiehqslvnlshglikeygitssdrVLQFASiafdv 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6816 ----------SNQTVV---------------------------------------------------------------- 6821
Cdd:cd17644    161 aaeeiyvtllSGATLVlrpeemrssledfvqyiqqwqltvlslppaywhllvlelllstidlpsslrlvivggeavqpel 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6822 -----------------------TVNRSSY-ILFP-DENREAYPFVRP----------SNAALAPLGSIGELLVEGPILA 6866
Cdd:cd17644    241 vrqwqknvgnfiqlinvygpteaTIAATVCrLTQLtERNITSVPIGRPiantqvyildENLQPVPVGVPGELHIGGVGLA 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6867 RGYLNDADKTAAAFVNDPAWLVEGHgkhpgrrgRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcm 6946
Cdd:cd17644    321 RGYLNRPELTAEKFISHPFNSSESE--------RLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQ-- 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6947 pratqmavevispagaAEQAKTMVVAflqlndeARDallggNVPNDDNLSAQVV-------FPAKVDEKLSNLLPSYMMP 7019
Cdd:cd17644    391 ----------------HNDVKTAVVI-------VRE-----DQPGNKRLVAYIVphyeespSTVELRQFLKAKLPDYMIP 442
                          490       500
                   ....*....|....*....|..
gi 1820002560 7020 EVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd17644    443 SAFVVLEELPLTPNGKIDRRAL 464
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
1503-1916 3.83e-45

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 172.90  E-value: 3.83e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1503 VEDIYPCSPLQEGL----MSLTAKRAgdYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQVVIEE- 1577
Cdd:pfam00668    1 VQDEYPLSPAQKRMwfleKLEPHSSA--YNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEEr 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1578 -------NIQWTEPKSLE----EYLSEDKAVSVGL-GDPLARYAFVKEACGGKRWFvWTIHHAVYDGWSLPLILHAVKQV 1645
Cdd:pfam00668   79 pfeleiiDISDLSESEEEeaieAFIQRDLQSPFDLeKGPLFRAGLFRIAENRHHLL-LSMHHIIVDGVSLGILLRDLADL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1646 YSGG------VLQWQPSFNAFI----QYLGQQDLEATVAYWQTALADCEAVLfpTLPPTVTQPVA------------DAT 1703
Cdd:pfam00668  158 YQQLlkgeplPLPPKTPYKDYAewlqQYLQSEDYQKDAAYWLEQLEGELPVL--QLPKDYARPADrsfkgdrlsftlDED 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1704 VEYQCPPLSKATSdTTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNTPvtGVEAMVGPTIATVPVRLRVQRDQTVFAF 1783
Cdd:pfam00668  236 TEELLRKLAKAHG-TTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTFSEL 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1784 LQGLQQQATDMIAHEQTGLQRIA-------KMGQGP--QHACSFQTLLVVQPVDDVLDNTLGEWRDHSELQEFTTYTLML 1854
Cdd:pfam00668  313 IKRVQEDLLSAEPHQGYPFGDLVndlrlprDLSRHPlfDPMFSFQNYLGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSL 392
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 1855 QCMLAAEGVQITASFDTRVIEKWVVEKMLRQFSFIMQQLAEAGAEKtVSDIETTTPEDRQQL 1916
Cdd:pfam00668  393 TASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQP-LSELDLLSDAEKQKL 453
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
4551-5057 4.00e-45

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 175.69  E-value: 4.00e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAICaWDGE------LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 4624
Cdd:COG0365     19 AEGRGDKVALI-WEGEdgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPG 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4625 HPASRHEHIFRQTGAQVVLASAQYATLwtslGRSVV---IVSEAsTSQLP------VVTKTADPSVNPGNAAYA------ 4689
Cdd:COG0365     98 FGAEALADRIEDAEAKVLITADGGLRG----GKVIDlkeKVDEA-LEELPslehviVVGRTGADVPMEGDLDWDellaaa 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4690 -----------------IFTSGSTGIPKGVVLEHKAVVTSCLGHGQA-FGITDHTRVLqfasytfdaCIAEI--ITTL-- 4747
Cdd:COG0365    173 saefepeptdaddplfiLYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFW---------CTADIgwATGHsy 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4748 -----LCCGCICV-------PSDSDRrnnLAKAINAMDVNWALLTPSVARML---DPCVVQ-----SLKILVLGGEQVNS 4807
Cdd:COG0365    244 ivygpLLNGATVVlyegrpdFPDPGR---LWELIEKYGVTVFFTAPTAIRALmkaGDEPLKkydlsSLRLLGSAGEPLNP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4808 ADWDRWPKSIQT--INAYGPTECSICCTTYSGKQGFKSGTIGTSI--VSVSwVVDPENhNRLAPlGSIGELLVEGPI--L 4881
Cdd:COG0365    321 EVWEWWYEAVGVpiVDGWGQTETGGIFISNLPGLPVKPGSMGKPVpgYDVA-VVDEDG-NPVPP-GEEGELVIKGPWpgM 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4882 ARGYLNDMEKTEAAFIDDpawlLEGYgghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE-----H 4956
Cdd:COG0365    398 FRGYWNDPERYRETYFGR----FPGW----------YRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIEsalvsH 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4957 H-VREClteakqlAVeVIVPEGEGGYAMLaAFVqlgddtynTLVKEKAGGDSLTVQVVflDRVEEELAKR-VPEHMmltt 5034
Cdd:COG0365    464 PaVAEA-------AV-VGVPDEIRGQVVK-AFV--------VLKPGVEPSDELAKELQ--AHVREELGPYaYPREI---- 520
                          570       580
                   ....*....|....*....|...
gi 1820002560 5035 FFTlEAMPTTTSGKIDRKRLREI 5057
Cdd:COG0365    521 EFV-DELPKTRSGKIMRRLLRKI 542
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
3462-3977 7.04e-45

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 174.91  E-value: 7.04e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3462 CVHDLFTEQAKARPHAPAICaWDGE------LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAG 3535
Cdd:COG0365     10 IAYNCLDRHAEGRGDKVALI-WEGEdgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3536 GAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYsARWTSSSCHVVTVSKALSsQLPA-----VVDSTNTSVRPENA---- 3606
Cdd:COG0365     89 AVHSPVFPGFGAEALADRIEDAEAKVLITADGG-LRGGKVIDLKEKVDEALE-ELPSlehviVVGRTGADVPMEGDldwd 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3607 --------------------AYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRA-FGITNLSRVLqfasytfdaCIAEI-- 3663
Cdd:COG0365    167 ellaaasaefepeptdaddpLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFW---------CTADIgw 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3664 IT--------TLLCGGCICV------PSDSDRrnsLAKAISTMDVNWAFLTPSVARLL---DPGLI-----PSLKILAIG 3721
Cdd:COG0365    238 ATghsyivygPLLNGATVVLyegrpdFPDPGR---LWELIEKYGVTVFFTAPTAIRALmkaGDEPLkkydlSSLRLLGSA 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3722 GEQSSSADWNRWpgsVQKIHV-----YGPTE-CCIFCT---------GYTTKQGFepstiGTSVAsvswVVDPENhNRLA 3786
Cdd:COG0365    315 GEPLNPEVWEWW---YEAVGVpivdgWGQTEtGGIFISnlpglpvkpGSMGKPVP-----GYDVA----VVDEDG-NPVP 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3787 PlGSMGELLMEGPI--LARGYLNDVDKTEAAFIDDpawllegYPGhpgrqgrLYKTGDLVQYNADGNLVYLGRKDSQVKV 3864
Cdd:COG0365    382 P-GEEGELVIKGPWpgMFRGYWNDPERYRETYFGR-------FPG-------WYRTGDGARRDEDGYFWILGRSDDVINV 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3865 RGQRVELGEVE-----HH-VREClpearqlAVeVILPSGQKDHAMLaAFVQLEEGTQnalldkeagGEDSMAQVVFlASV 3938
Cdd:COG0365    447 SGHRIGTAEIEsalvsHPaVAEA-------AV-VGVPDEIRGQVVK-AFVVLKPGVE---------PSDELAKELQ-AHV 507
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 3939 EEELAKrlpeHMVP-TVFF--SLlhfPTTTSGKTDRKRLREI 3977
Cdd:COG0365    508 REELGP----YAYPrEIEFvdEL---PKTRSGKIMRRLLRKI 542
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
2-283 1.28e-44

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 172.46  E-value: 1.28e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL----EPSHIPSLRILVMGGEQVNSADWDRWP--SSVQTINGYGPTECCIVCTGYTSEQDFTTGT- 74
Cdd:cd17646    229 GVTTCHFVPSMLRVFlaepAAGSCASLRRVFCSGEALPPELAARFLalPGAELHNLYGPTEAAIDVTHWPVRGPAETPSv 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   75 -IGTSIASVS-WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAwlleGHGGyagrqgRLYKTGDL 152
Cdd:cd17646    309 pIGRPVPNTRlYVLD--DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF----GPGS------RMYRTGDL 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  153 VRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAVEVV-LPLGqknHATLAAFIQLDKGthnallkeK 231
Cdd:cd17646    377 ARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAH-PAVTHAVVVARaAPAG---AARLVGYVVPAAG--------A 444
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560  232 VGGDDsiarvvflAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd17646    445 AGPDT--------AALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
7753-8116 1.94e-44

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 167.08  E-value: 1.94e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7753 AYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRnSLA 7832
Cdd:cd04433      3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE-AAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7833 KAISTMDVNWAFLTPSVARLLDPGL------IPSLKILAIGGEQSSSADWNRW---PGsVQKIHVYGPTECCIFCTGYTT 7903
Cdd:cd04433     82 ELIEREKVTILLGVPTLLARLLKAPesagydLSSLRALVSGGAPLPPELLERFeeaPG-IKLVNGYGLTETGGTVATGPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7904 KQGFE-PSTIGTSVASVSW-VVDPEnhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdpawlleGYpghpgrqg 7981
Cdd:cd04433    161 DDDARkPGSVGRPVPGVEVrIVDPD--GGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GW-------- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7982 rlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKNHAmLAVFVQLGKGTH 8061
Cdd:cd04433    224 --YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGH-PGVAEAAV-VGVPDPEWGER-VVAVVVLRPGAD 298
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 8062 IahleekaggedsmaqvvfltgTEEEL----AKRLPKHMVPTVFFALLHFPMTTSGKAD 8116
Cdd:cd04433    299 L---------------------DAEELrahvRERLAPYKVPRRVVFVDALPRTASGKID 336
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
7182-7577 2.16e-44

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 169.55  E-value: 2.16e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7182 IYPCSPLQEGLISLTAKRAGD--YIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVV-------VE 7252
Cdd:cd19536      1 MYPLSSLQEGMLFHSLLNPGGsvYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVhrqaqvpVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7253 EKIQWTESEA---LEEYLKEDKAVSMGL-GDPLAHYALVKEAWGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSG---- 7324
Cdd:cd19536     81 ELDLTPLEEQldpLRAYKEETKIRRFDLgRAPLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQlley 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7325 ---AVLERQPsFNAFI-QYLGQQDLEATAAYWQTALSDCE-AVLFPPLPSTVTQPVADT-TVEYQCPPLSKATLDT---- 7394
Cdd:cd19536    161 kplSLPPAQP-YRDFVaHERASIQQAASERYWREYLAGATlATLPALSEAVGGGPEQDSeLLVSVPLPVRSRSLAKrsgi 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7395 TTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPIAGVEAMVGPTIATVPVRLRVQrDQTVFAFLQGLQQQSTDMIAHE 7474
Cdd:cd19536    240 PLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLS-EETVEDLLKRAQEQELESLSHE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7475 QTGLQHIAKLGSGPRHacgFQTLLVVQ--PVDDVLGSDDMLGEWRSYSKmQDFTTYALMVQFTLAAEGVQITASFD--AR 7550
Cdd:cd19536    319 QVPLADIQRCSEGEPL---FDSIVNFRhfDLDFGLPEWGSDEGMRRGLL-FSEFKSNYDVNLSVLPKQDRLELKLAynSQ 394
                          410       420
                   ....*....|....*....|....*..
gi 1820002560 7551 VIEHwvlEKMLRQFSFIMQQLAEASED 7577
Cdd:cd19536    395 VLDE---EQAQRLAAYYKSAIAELATA 418
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
6277-6669 9.72e-44

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 167.63  E-value: 9.72e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6277 MYPCSPLQEGLMSLTAKRAGD--YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVV-------VE 6347
Cdd:cd19536      1 MYPLSSLQEGMLFHSLLNPGGsvYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVhrqaqvpVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6348 EKIQW---TESKRLEEYLREDKAVSMGL-GDPLARYAIIKEAWGGKRWFVWTIHHALYDGWSLPRVLQAVKQAYNG---- 6419
Cdd:cd19536     81 ELDLTpleEQLDPLRAYKEETKIRRFDLgRAPLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQlley 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6420 ---AVLETQPsFNAFI-QYLSQQDLEATAAYWQTALADCE-ATLFPPLPSSVKQLVADTTVEHQCPLPSRSTSDTTTS-- 6492
Cdd:cd19536    161 kplSLPPAQP-YRDFVaHERASIQQAASERYWREYLAGATlATLPALSEAVGGGPEQDSELLVSVPLPVRSRSLAKRSgi 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6493 ---TLIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTSIDAIVGPTIATVPLRVRLQkDQTVSSFLGYLQQQATEMIAYE 6569
Cdd:cd19536    240 plsTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLS-EETVEDLLKRAQEQELESLSHE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6570 QTGLQQIAKMGPDP---QHACGFQTLLVVQPAGDVLGSDDTLGKwrgysGLQDFMTYALGVRCTLSAEGVKITASFD--A 6644
Cdd:cd19536    319 QVPLADIQRCSEGEplfDSIVNFRHFDLDFGLPEWGSDEGMRRG-----LLFSEFKSNYDVNLSVLPKQDRLELKLAynS 393
                          410       420
                   ....*....|....*....|....*
gi 1820002560 6645 RVIEHWVVEKMLGQFSFAMQQLAEA 6669
Cdd:cd19536    394 QVLDEEQAQRLAAYYKSAIAELATA 418
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
3607-3970 1.06e-43

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 165.15  E-value: 1.06e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3607 AYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRnSLA 3686
Cdd:cd04433      3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE-AAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3687 KAISTMDVNWAFLTPSVARLLDPGL------IPSLKILAIGGEQSSSADWNRW---PGsVQKIHVYGPTECCIFCTGYTT 3757
Cdd:cd04433     82 ELIEREKVTILLGVPTLLARLLKAPesagydLSSLRALVSGGAPLPPELLERFeeaPG-IKLVNGYGLTETGGTVATGPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3758 KQGFE-PSTIGTSVASVSW-VVDPEnhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdpawlleGYpghpgrqg 3835
Cdd:cd04433    161 DDDARkPGSVGRPVPGVEVrIVDPD--GGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GW-------- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3836 rlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKDHAmLAAFVQLEEGtq 3915
Cdd:cd04433    224 --YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGH-PGVAEAAV-VGVPDPEWGER-VVAVVVLRPG-- 296
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 3916 nALLDKEAggedsmaqvvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTD 3970
Cdd:cd04433    297 -ADLDAEE--------------LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
1955-2442 1.69e-43

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 168.03  E-value: 1.69e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSA 2034
Cdd:cd17654     17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2035 QhsarwigtNHQVVTVSAGSLEQFstlvnpvDLPAkPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLl 2114
Cdd:cd17654     97 E--------LDNAPLSFTPEHRHF-------NIRT-DECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSE- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2115 RALQFTA-YTFDVCIAEIITTLVHGGCICVPSDSERRDN--LAKAI-TDMQVNWGYLTSSVARLLDPCLVP--------S 2182
Cdd:cd17654    160 DILFLTSpLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPskLADILfKRHRITVLQATPTLFRRFGSQSIKstvlsatsS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2183 LKVLVLGGEQ-----VNSTdWGKWPSSVQTINGYGPTECCVFCTGYTgIQGFQSG-NIGTSI-ASVSWVVDPENHGrlap 2255
Cdd:cd17654    240 LRVLALGGEPfpslvILSS-WRGKGNRTRIFNIYGITEVSCWALAYK-VPEEDSPvQLGSPLlGTVIEVRDQNGSE---- 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2256 lgSIGELLVEGpiLARGYlndvdktqaaFIDDPawllegypgHEGRQGRLYKTGDLVRySSDGNLVCLGRKDSQVKVRGQ 2335
Cdd:cd17654    314 --GTGQVFLGG--LNRVC----------ILDDE---------VTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGK 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2336 RVELGEVEHHMRKCLPEAnQLAVEVVppsgerDHAMLAAFIRLddeTRNSPLIIKYaednstaqiVFLTgieeelseRLP 2415
Cdd:cd17654    370 RINLDLIQQVIESCLGVE-SCAVTLS------DQQRLIAFIVG---ESSSSRIHKE---------LQLT--------LLS 422
                          490       500
                   ....*....|....*....|....*..
gi 1820002560 2416 QHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd17654    423 SHAIPDTFVQIDKLPLTSHGKVDKSEL 449
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
22-283 1.88e-43

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 167.87  E-value: 1.88e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   22 PSLRILVMGGEQVNSADWDRW-----PSSVQTINGYGPTECCIVCTGYT-SEQDFTTGT---IGTSIASVSW-VVDpkDH 91
Cdd:cd17643    210 LALRYVIFGGEALEAAMLRPWagrfgLDRPQLVNMYGITETTVHVTFRPlDAADLPAAAaspIGRPLPGLRVyVLD--AD 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   92 GRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAwlleghgGYAGRqgRLYKTGDLVRYDADGNLVCLGRKDSQV 171
Cdd:cd17643    288 GRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF-------GGPGS--RMYRTGDLARRLPDGELEYLGRADEQV 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  172 KLRGQRVELGEVEHHVREClPEAKQLAVeVVLPLGQKNHATLAAFIqldkgthnallkekvgGDDSIARVVflAGVEEEL 251
Cdd:cd17643    359 KIRGFRIELGEIEAALATH-PSVRDAAV-IVREDEPGDTRLVAYVV----------------ADDGAAADI--AELRALL 418
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1820002560  252 AKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd17643    419 KELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
6705-7041 1.90e-43

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 167.73  E-value: 1.90e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6705 HDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 6784
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6785 DHPASRHEDILRQTGAQVILASAQN------------------------------------------------------- 6809
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLTNPDDlayviytsgstglpkgvmiehhnlvnlcewhrpyfgvtpadkslvyasfsfdasa 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6810 -------------------------------------------------TTLFQSSNQTVVT-------VNRSSYILF-- 6831
Cdd:cd17645    161 weifphltagaalhvvpserrldldalndyfnqegitisflptgaaeqfMQLDNQSLRVLLTggdklkkIERKGYKLVnn 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6832 --PDEN------------REAYPFVRP----------SNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPawl 6887
Cdd:cd17645    241 ygPTENtvvatsfeidkpYANIPIGKPidntrvyildEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHP--- 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6888 veghgKHPGRRgrLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAGaaeqAK 6967
Cdd:cd17645    318 -----FVPGER--MYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMN-HPLIELAAVLAKEDAD----GR 385
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 6968 TMVVAFLQLNDEARdallggnvpnddnlsaqvvfPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd17645    386 KYLVAYVTAPEEIP--------------------HEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
4555-5054 2.68e-43

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 167.26  E-value: 2.68e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4555 PDTPAIC----AWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 4630
Cdd:cd17654      1 PDRPALIidqtTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4631 EHIFRQTGAQVVLASAQYatlwTSLGRSVVIVSEASTSQLPvvtktadpsvnpGNAAYAIFTSGSTGIPKGVVLEHKAVV 4710
Cdd:cd17654     81 LTVMKKCHVSYLLQNKEL----DNAPLSFTPEHRHFNIRTD------------ECLAYVIHTSGTTGTPKIVAVPHKCIL 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4711 TSCLGHGQAFGITdHTRVLQFAS-YTFDACIAEIITTLLCCGCICVPSDSDRR--NNLAKAINAMD-VNWALLTPSVARM 4786
Cdd:cd17654    145 PNIQHFRSLFNIT-SEDILFLTSpLTFDPSVVEIFLSLSSGATLLIVPTSVKVlpSKLADILFKRHrITVLQATPTLFRR 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4787 LDPCVVQ--------SLKILVLGGEQ-----VNSAdWDRWPKSIQTINAYGPTECSICCTTYSGKQGFKSGTIGTSIV-S 4852
Cdd:cd17654    224 FGSQSIKstvlsatsSLRVLALGGEPfpslvILSS-WRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLgT 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4853 VSWVVDPENHNrlaplgSIGELLVEGpiLARGYlndmekteaaFIDDPawllegyggHSGRQGRLYKTGDLVRYDaDGNL 4932
Cdd:cd17654    303 VIEVRDQNGSE------GTGQVFLGG--LNRVC----------ILDDE---------VTVPKGTMRATGDFVTVK-DGEL 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4933 VYLGRKDSQVKLRGQRVELGEVEHHVRECLTEaKQLAVEVIVPEgeggyaMLAAF-VQLGDDtyntlvkekaggdsltvq 5011
Cdd:cd17654    355 FFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQQ------RLIAFiVGESSS------------------ 409
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 5012 vvflDRVEEELAK-RVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd17654    410 ----SRIHKELQLtLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
6712-7041 3.17e-43

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 167.04  E-value: 3.17e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6712 ALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 6791
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6792 EDILRQTGAQVILA-----------------------SAQNTTLF--------------QSSNQ---------------- 6818
Cdd:cd05945     81 REILDAAKPALLIAdgddnayiiftsgstgrpkgvqiSHDNLVSFtnwmlsdfplgpgdVFLNQapfsfdlsvmdlypal 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6819 ----TVVTVNRSSY----------------------------ILFPDENREAYP-------------------------- 6840
Cdd:cd05945    161 asgaTLVPVPRDATadpkqlfrflaehgitvwvstpsfaamcLLSPTFTPESLPslrhflfcgevlphktaralqqrfpd 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6841 --------------------FVRPSNAALAPL-----------------------GSIGELLVEGPILARGYLNDADKTA 6877
Cdd:cd05945    241 ariyntygpteatvavtyieVTPEVLDGYDRLpigyakpgaklvildedgrpvppGEKGELVISGPSVSKGYLNNPEKTA 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6878 AAFVndpawlveghgKHPGRRGrlYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLRECmpraTQMAVEVI 6957
Cdd:cd05945    321 AAFF-----------PDEGQRA--YRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQV----PGVKEAVV 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6958 SPAGAAEqAKTMVVAFLQLNDEARDALlggnvpnddnlsaqvvfPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTD 7037
Cdd:cd05945    384 VPKYKGE-KVTELIAFVVPKPGAEAGL-----------------TKAIKAELAERLPPYMIPRRFVYLDELPLNANGKID 445

                   ....
gi 1820002560 7038 RKRL 7041
Cdd:cd05945    446 RKAL 449
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
5193-5609 8.83e-43

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 165.97  E-value: 8.83e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5193 VEDMYPCSPLQEGL----MSLTAKRAgdYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEEK 5268
Cdd:pfam00668    1 VQDEYPLSPAQKRMwfleKLEPHSSA--YNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5269 ---IQWTESKRL---------EEYLREDKAVSMGL-GDRLARYALIKepYDGGKRWFVWTIHHALYDGWSLPRILQAVKQ 5335
Cdd:pfam00668   79 pfeLEIIDISDLseseeeeaiEAFIQRDLQSPFDLeKGPLFRAGLFR--IAENRHHLLLSMHHIIVDGVSLGILLRDLAD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5336 IYSGAVPERQ------PSFNAFI----QYLGQQDLEAATLYWQTALADCKAALfpTLPPTVTQPVADTTVEYQ----CPP 5401
Cdd:pfam00668  157 LYQQLLKGEPlplppkTPYKDYAewlqQYLQSEDYQKDAAYWLEQLEGELPVL--QLPKDYARPADRSFKGDRlsftLDE 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5402 PS-------QSATDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGVEAMVGPTIATVPLRVCLQKDQTVSTL 5474
Cdd:pfam00668  235 DTeellrklAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTFSEL 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5475 LECLQQQSTDMIAHEQTGLQRIAKMSPGAR---HACGFQTLLVVQPTddvLGSDDMLGEWRSY-------SEMQDFTTYA 5544
Cdd:pfam00668  313 IKRVQEDLLSAEPHQGYPFGDLVNDLRLPRdlsRHPLFDPMFSFQNY---LGQDSQEEEFQLSeldlsvsSVIEEEAKYD 389
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5545 L--MVQCTLAKDRVEV---TASFDARVIEQWvvekmLRQFGFVMQQLAEAGAEKtVSDIETTTLEDRQQL 5609
Cdd:pfam00668  390 LslTASERGGGLTIKIdynTSLFDEETIERF-----AEHFKELLEQAIAHPSQP-LSELDLLSDAEKQKL 453
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
7608-8123 1.38e-42

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 167.98  E-value: 1.38e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7608 CVHDLFAEQARARPGAPAICaWDGE------LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAG 7681
Cdd:COG0365     10 IAYNCLDRHAEGRGDKVALI-WEGEdgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7682 GAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYsARWTSSSCHVVTVSKALSsQLPA-----VVDSTNTSVRPENA---- 7752
Cdd:COG0365     89 AVHSPVFPGFGAEALADRIEDAEAKVLITADGG-LRGGKVIDLKEKVDEALE-ELPSlehviVVGRTGADVPMEGDldwd 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7753 --------------------AYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRA-FGITNLSRVLqfasytfdaCIAEI-- 7809
Cdd:COG0365    167 ellaaasaefepeptdaddpLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFW---------CTADIgw 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7810 IT--------TLLCGGCICV------PSDSDRrnsLAKAISTMDVNWAFLTPSVARLL---DPGLI-----PSLKILAIG 7867
Cdd:COG0365    238 ATghsyivygPLLNGATVVLyegrpdFPDPGR---LWELIEKYGVTVFFTAPTAIRALmkaGDEPLkkydlSSLRLLGSA 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7868 GEQSSSADWNRWpgsVQKIHV-----YGPTE-CCIFCT---------GYTTKQGFepstiGTSVAsvswVVDPENhNRLA 7932
Cdd:COG0365    315 GEPLNPEVWEWW---YEAVGVpivdgWGQTEtGGIFISnlpglpvkpGSMGKPVP-----GYDVA----VVDEDG-NPVP 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7933 PlGSMGELLMEGPI--LARGYLNDVDKTEAAFIDDpawllegYPGhpgrqgrLYKTGDLVQYNADGNLVYLGRKDSQVKV 8010
Cdd:COG0365    382 P-GEEGELVIKGPWpgMFRGYWNDPERYRETYFGR-------FPG-------WYRTGDGARRDEDGYFWILGRSDDVINV 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8011 RGQRVELGEVE-----HH-VREClpearqlAVeVILPSGQKNHAMLAvFVQLgkgthiahleeKAGGEDSMAqvvfltgT 8084
Cdd:COG0365    447 SGHRIGTAEIEsalvsHPaVAEA-------AV-VGVPDEIRGQVVKA-FVVL-----------KPGVEPSDE-------L 499
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 8085 EEEL----AKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREI 8123
Cdd:COG0365    500 AKELqahvREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKI 542
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
855-1368 1.80e-42

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 167.60  E-value: 1.80e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  855 HDLFAEQARARPDASAVCaWDGE------LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGA 928
Cdd:COG0365     12 YNCLDRHAEGRGDKVALI-WEGEdgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  929 FVPLDPGHPASRHEEIFKQIGAQVVLTSS---------------QHAMLFASSERHQVTVSKVSTS-QLPTVVNFAKS-- 990
Cdd:COG0365     91 HSPVFPGFGAEALADRIEDAEAKVLITADgglrggkvidlkekvDEALEELPSLEHVIVVGRTGADvPMEGDLDWDELla 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  991 ---------PVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEA-FGYTDHARVLQFA--------SYTFDACIA 1052
Cdd:COG0365    171 aasaefepePTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTAdigwatghSYIVYGPLL 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1053 EIITTLLYGGcICVPSESDRrnnLAKAISTMDVNCALLTPSVARLL--------EPSAVPSLKRLVLQGEQVSFADWNRW 1124
Cdd:COG0365    251 NGATVVLYEG-RPDFPDPGR---LWELIEKYGVTVFFTAPTAIRALmkagdeplKKYDLSSLRLLGSAGEPLNPEVWEWW 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1125 ---PGsVQTINGYGPTECSVCCNTYSGKQGFKSGIIGtsVASLSWVV----DAGNHnrlAPLGSIGELLVEGPI--LARG 1195
Cdd:COG0365    327 yeaVG-VPIVDGWGQTETGGIFISNLPGLPVKPGSMG--KPVPGYDVavvdEDGNP---VPPGEEGELVIKGPWpgMFRG 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1196 YLNDIDKTEAAFIDDpawllegYEGhagrrgrLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIE-----HH-V 1269
Cdd:COG0365    401 YWNDPERYRETYFGR-------FPG-------WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIEsalvsHPaV 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1270 REClpearqlAVeVILPSGQKEHALLaAFIQLDKGnhnalfeekASGEDSMAQVVFltgveEELAKRLPEHMVPTILFTV 1349
Cdd:COG0365    467 AEA-------AV-VGVPDEIRGQVVK-AFVVLKPG---------VEPSDELAKELQ-----AHVREELGPYAYPREIEFV 523
                          570
                   ....*....|....*....
gi 1820002560 1350 KAMPITTSGKIDRKRLQDI 1368
Cdd:COG0365    524 DELPKTRSGKIMRRLLRKI 542
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
8-283 2.32e-42

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 164.92  E-value: 2.32e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    8 LTPSVARLL----EPSHIP---SLRILVMGGEQVNSADWDRWPSSV----QTINGYGPTECCIVCTGY----TSEQDFTT 72
Cdd:cd17644    203 LPPAYWHLLvlelLLSTIDlpsSLRLVIVGGEAVQPELVRQWQKNVgnfiQLINVYGPTEATIAATVCrltqLTERNITS 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   73 GTIGTSIASVS-WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAWLLEGHggyagrqgRLYKTGD 151
Cdd:cd17644    283 VPIGRPIANTQvYILD--ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESE--------RLYKTGD 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  152 LVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECLPEAKQLAVEVVL----PLGQKNhatLAAFIqldkgthnal 227
Cdd:cd17644    353 LARYLPDGNIEYLGRIDNQVKIRGFRIELGEIE----AVLSQHNDVKTAVVIvredQPGNKR---LVAYI---------- 415
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560  228 lkekVGGDDSIARVVFLagvEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd17644    416 ----VPHYEESPSTVEL---RQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
7179-7594 2.51e-42

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 164.43  E-value: 2.51e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7179 VKDIYPCSPLQEGL----ISLTAKRAgdYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVVVEEK 7254
Cdd:pfam00668    1 VQDEYPLSPAQKRMwfleKLEPHSSA--YNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7255 -IQW-----------TESEALEEYLKEDKAVSMGL-GDPLAHYALVKEAWGGKRWFvWTIHHALYDGGSLPLILHAVKQV 7321
Cdd:pfam00668   79 pFELeiidisdlsesEEEEAIEAFIQRDLQSPFDLeKGPLFRAGLFRIAENRHHLL-LSMHHIIVDGVSLGILLRDLADL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7322 YSGAVLERQ------PSFNAFI----QYLGQQDLEATAAYWQTALSDCEAVLfpPLPSTVTQPVADTTVEYQ----CPPL 7387
Cdd:pfam00668  158 YQQLLKGEPlplppkTPYKDYAewlqQYLQSEDYQKDAAYWLEQLEGELPVL--QLPKDYARPADRSFKGDRlsftLDED 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7388 SKATL-------DTTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPiaGVEAMVGPTIATVPVRLRVQRDQTVFAFL 7460
Cdd:pfam00668  236 TEELLrklakahGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTFSELI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7461 QGLQQQSTDMIAHEQTGLQHIAKLGSGPR---HACGFQTLLVVQPvddVLGSDDMLGEW-RSYSKM------QDFTTYAL 7530
Cdd:pfam00668  314 KRVQEDLLSAEPHQGYPFGDLVNDLRLPRdlsRHPLFDPMFSFQN---YLGQDSQEEEFqLSELDLsvssviEEEAKYDL 390
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 7531 MVQFTLAAEGVQITASFDARVIEhwvLEKMLRQFSFIMQQLAEASED--SKVADIDTTTPEDRQQL 7594
Cdd:pfam00668  391 SLTASERGGGLTIKIDYNTSLFD---EETIERFAEHFKELLEQAIAHpsQPLSELDLLSDAEKQKL 453
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
5769-6131 3.17e-42

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 160.91  E-value: 3.17e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5769 YIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRnDLVK 5848
Cdd:cd04433      4 LILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE-AALE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5849 AISTMDVSCALLTPSVARLL------EPSSVPTLQMLVLQGEQVSFADWNRWPAS--VQTINGYGPTECSICCNTYSGKQ 5920
Cdd:cd04433     83 LIEREKVTILLGVPTLLARLlkapesAGYDLSSLRALVSGGAPLPPELLERFEEApgIKLVNGYGLTETGGTVATGPPDD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5921 G-FKSGIIGTSVASVSW-VVDPEnhDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDdpawlleGYpghpgrqgrl 5998
Cdd:cd04433    163 DaRKPGSVGRPVPGVEVrIVDPD--GGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GW---------- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5999 YKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQLAVeVILPSGQKDHAmLAAFVQLEEGtqna 6078
Cdd:cd04433    224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGH-PGVAEAAV-VGVPDPEWGER-VVAVVVLRPG---- 296
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 6079 lldKEASGEDSMAQVvflasveeelAKRLPEHMVPTVFFSLLHFPTTTSGKTD 6131
Cdd:cd04433    297 ---ADLDAEELRAHV----------RERLAPYKVPRRVVFVDALPRTASGKID 336
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
866-1365 4.91e-42

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 163.80  E-value: 4.91e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  866 PDASAVC----AWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRH 941
Cdd:cd17654      1 PDRPALIidqtTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  942 EEIFKQIGAQVVLTSSQHAMLFASSErhqvtvskvstsqlPTVVNFAKSpvDPGNTAYIIFTSGTTGIPKGVVLQHRAVT 1021
Cdd:cd17654     81 LTVMKKCHVSYLLQNKELDNAPLSFT--------------PEHRHFNIR--TDECLAYVIHTSGTTGTPKIVAVPHKCIL 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1022 TSCLGHGEAFGYTdHARVLQFAS-YTFDACIAEIITTLLYGGC-ICVPSESDRRNN-LAKAISTMD-VNCALLTPSVARL 1097
Cdd:cd17654    145 PNIQHFRSLFNIT-SEDILFLTSpLTFDPSVVEIFLSLSSGATlLIVPTSVKVLPSkLADILFKRHrITVLQATPTLFRR 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1098 LEP--------SAVPSLKRLVLQGEQ----VSFADWNRWPGSVQTINGYGPTECSVCCNTYSGKQGFKSGIIGTSVASLS 1165
Cdd:cd17654    224 FGSqsikstvlSATSSLRVLALGGEPfpslVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTV 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1166 -WVVDAGNHNrlaplgSIGELLVEGpiLARGYlndidkteaaFIDDPawllegyegHAGRRGRLYKTGDLVRCDaDGNLV 1244
Cdd:cd17654    304 iEVRDQNGSE------GTGQVFLGG--LNRVC----------ILDDE---------VTVPKGTMRATGDFVTVK-DGELF 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1245 CLGRKDSQVKVRGQRVELGEIEHHVRECLPEarqLAVEVILPSGQKehalLAAFIqLDKGNHNALFEEkasgedsmaqvV 1324
Cdd:cd17654    356 FLGRKDSQIKRRGKRINLDLIQQVIESCLGV---ESCAVTLSDQQR----LIAFI-VGESSSSRIHKE-----------L 416
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 1325 FLTgveeelakRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd17654    417 QLT--------LLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
85-378 9.99e-42

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 171.79  E-value: 9.99e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   85 VVDPKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNpaWLLE-----------GHGG---YAGRQGRLYKTG 150
Cdd:TIGR03443  606 VVNRNDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNN--WFVDpshwidldkenNKPErefWLGPRDRLYRTG 683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  151 DLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHH------VREclpeakqlavEVVLPLGQKN-HATLAAFI--QLDK 221
Cdd:TIGR03443  684 DLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHlsqhplVRE----------NVTLVRRDKDeEPTLVSYIvpQDKS 753
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  222 GTHNALLKEKVGGDDSIARVVFLAG-------VEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLreigaSF--TA 292
Cdd:TIGR03443  754 DELEEFKSEVDDEESSDPVVKGLIKyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL-----PFpdTA 828
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  293 QQLAEMRTSSQGPKRQPSTEAERTMQQLWARVLGIEPDSIGLDDSFFRLGGDSIAAIKLVGEARRT-GLQPSVADIFRHP 371
Cdd:TIGR03443  829 QLAAVAKNRSASAADEEFTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKlNVELPLGLIFKSP 908

                   ....*..
gi 1820002560  372 TLAALAS 378
Cdd:TIGR03443  909 TIKGFAK 915
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
6716-7041 1.12e-41

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 162.64  E-value: 1.12e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6716 PNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIL 6795
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6796 RQTGAQVIL----------------------------------------------------AS----------------- 6806
Cdd:cd17650     81 EDSGAKLLLtqpedlayviytsgttgkpkgvmvehrnvahaahawrreyeldsfpvrllqmASfsfdvfagdfarsllng 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6807 ---------------------------------------------------------------------------AQNTT 6811
Cdd:cd17650    161 gtlvicpdevkldpaalydlilksritlmestpalirpvmayvyrngldlsamrllivgsdgckaqdfktlaarfGQGMR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6812 LFQSSNQTVVTVNRSSYILFPDENREA--YPFVRP-SNAAL---------APLGSIGELLVEGPILARGYLNDADKTAAA 6879
Cdd:cd17650    241 IINSYGVTEATIDSTYYEEGRDPLGDSanVPIGRPlPNTAMyvlderlqpQPVGVAGELYIGGAGVARGYLNRPELTAER 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6880 FVNDPawLVEGhgkhpgrrGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISP 6959
Cdd:cd17650    321 FVENP--FAPG--------ERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLAR-HPAIDEAVVAVRED 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6960 AGAaeqaktmvvaflqlndEARdallggnvpnddnLSAQVVFPAKVD-----EKLSNLLPSYMMPEVYFAVPQLPMMISG 7034
Cdd:cd17650    390 KGG----------------EAR-------------LCAYVVAAATLNtaelrAFLAKELPSYMIPSYYVQLDALPLTPNG 440

                   ....*..
gi 1820002560 7035 KTDRKRL 7041
Cdd:cd17650    441 KVDRRAL 447
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
1933-2443 1.92e-41

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 162.35  E-value: 1.92e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAiCAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 2011
Cdd:cd05936      3 DLLEEAARRFPDKTA-LIFMGRkLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2012 DHPASRHEDIFRQTGAQVVVtsaqhsarwigtnhqVVTVSAGSLEQFSTLVNPVDLPakPENAAYVMFTSGSTGTPKGVV 2091
Cdd:cd05936     82 LYTPRELEHILNDSGAKALI---------------VAVSFTDLLAAGAPLGERVALT--PEDVAVLQYTSGTTGVPKGAM 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2092 LEHR---AVVTSCLGHGQAF--GVTNLLRALQ-FTAYTFDVCiaeIITTLVHGGCIcVPSDSERRDNLAKAITDMQVN-- 2163
Cdd:cd05936    145 LTHRnlvANALQIKAWLEDLleGDDVVLAALPlFHVFGLTVA---LLLPLALGATI-VLIPRFRPIGVLKEIRKHRVTif 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2164 ------WGYLTSSVARLldPCLVPSLKVLVLGG----EQVnSTDWGKwPSSVQTINGYGPTECC--VFCTGYTGIQgfQS 2231
Cdd:cd05936    221 pgvptmYIALLNAPEFK--KRDFSSLRLCISGGaplpVEV-AERFEE-LTGVPIVEGYGLTETSpvVAVNPLDGPR--KP 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2232 GNIGTSIASVSW-VVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpaWLlegypghegrqgrlyKTGD 2310
Cdd:cd05936    295 GSIGIPLPGTEVkIVDDD--GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG--WL---------------RTGD 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2311 LVRYSSDGNLVCLGRKDSQVKVRGQRV---ELGEV--EHhmrkclPEANQLAVEVVPP--SGErdhaMLAAFIRLDDETR 2383
Cdd:cd05936    356 IGYMDEDGYFFIVDRKKDMIIVGGFNVyprEVEEVlyEH------PAVAEAAVVGVPDpySGE----AVKAFVVLKEGAS 425
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 2384 NSPL-IIKYAEdnstaqivfltgieeelsERLPQHMVPTVFFALVHFPTTTSGKTDRKRLR 2443
Cdd:cd05936    426 LTEEeIIAFCR------------------EQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
421-839 2.55e-41

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 161.73  E-value: 2.55e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  421 IEDMYLCSPLQEGL----MSLTTKRAgdYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQVVVEEK 496
Cdd:pfam00668    1 VQDEYPLSPAQKRMwfleKLEPHSSA--YNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  497 ---------MQWTESES---LEEYLNEDKAASMGL-GDRLARYALIKESCGGKRWFvWTIHHALYDGWSLPLVLDAVKQV 563
Cdd:pfam00668   79 pfeleiidiSDLSESEEeeaIEAFIQRDLQSPFDLeKGPLFRAGLFRIAENRHHLL-LSMHHIIVDGVSLGILLRDLADL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  564 YSGAALERQ------PSFNTFI----QYVSQQDVKAAAAYWQTALADCEAVLfpPLPSTVTQPVADTTV--KYQCPPSPE 631
Cdd:pfam00668  158 YQQLLKGEPlplppkTPYKDYAewlqQYLQSEDYQKDAAYWLEQLEGELPVL--QLPKDYARPADRSFKgdRLSFTLDED 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  632 VTS--------SNITTSTLIRAAWAIIASRYTSSEDIVFGTTVTGRNAPitGVEAMVGPTIATVPLRVRPRKGQTVSAFL 703
Cdd:pfam00668  236 TEEllrklakaHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTFSELI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  704 ENLQQQATEMIAYEQTGLQRIMKMGPGPQ---HACGFQTLLV--VHPTDDVLSSDDTLGEWHSRSDSELQYFTTYALTIQ 778
Cdd:pfam00668  314 KRVQEDLLSAEPHQGYPFGDLVNDLRLPRdlsRHPLFDPMFSfqNYLGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLT 393
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  779 CTLAVEGVQITASFDARVVEHWVVEKMLGQFSFVMQQLAEaGVEKKVADIETTTLEDRQQL 839
Cdd:pfam00668  394 ASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIA-HPSQPLSELDLLSDAEKQKL 453
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
2-285 3.27e-41

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 161.13  E-value: 3.27e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL------EPSHIPSLRILVMGGEQVNSADWDRWPS--SVQTINGYGPTECCIVCTGYTSEQDFT-T 72
Cdd:COG0318    189 RVTVLFGVPTMLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFEErfGVRIVEGYGLTETSPVVTVNPEDPGERrP 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   73 GTIGTSIASVS-WVVDPkdHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinnpawllegHGGYagrqgrlYKTGD 151
Cdd:COG0318    269 GSVGRPLPGVEvRIVDE--DGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF----------RDGW-------LRTGD 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  152 LVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAVeVVLP---LGQknhaTLAAFIQLDKGTHnall 228
Cdd:COG0318    330 LGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAH-PGVAEAAV-VGVPdekWGE----RVVAFVVLRPGAE---- 399
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  229 kekvggddsiarvVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:COG0318    400 -------------LDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1930-2445 9.34e-41

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 162.59  E-value: 9.34e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1930 CVHDLFTEQAKARPHAPAICaWDGE------LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAG 2003
Cdd:COG0365     10 IAYNCLDRHAEGRGDKVALI-WEGEdgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2004 GAFVPLDPDHPASRHEDIFRQTGAQVVVTSAQHSARW---------------IGTNHQVVTVSAGS-------------- 2054
Cdd:COG0365     89 AVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGkvidlkekvdealeeLPSLEHVIVVGRTGadvpmegdldwdel 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2055 LEQFSTLVNPVDLPAkpENAAYVMFTSGSTGTPKGVVLEHRAVvtsclghgqafgvtnLLRALQFTAYTFDV-------C 2127
Cdd:COG0365    169 LAAASAEFEPEPTDA--DDPLFILYTSGTTGKPKGVVHTHGGY---------------LVHAATTAKYVLDLkpgdvfwC 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2128 IAEI--IT--------TLVHGGCICV------PSDSERrdnLAKAITDMQVNWGYLTSSVARLL---DPCLV-----PSL 2183
Cdd:COG0365    232 TADIgwATghsyivygPLLNGATVVLyegrpdFPDPGR---LWELIEKYGVTVFFTAPTAIRALmkaGDEPLkkydlSSL 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2184 KVLVLGGEQVNSTDWGKWPSSVQT--INGYGPTE-CCVFCT---------GYTGIQGFqsgniGTSIAsvswVVDPEnhG 2251
Cdd:COG0365    309 RLLGSAGEPLNPEVWEWWYEAVGVpiVDGWGQTEtGGIFISnlpglpvkpGSMGKPVP-----GYDVA----VVDED--G 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2252 RLAPLGSIGELLVEGPI--LARGYLNDVDKTQAAFIDDpawllegYPGhegrqgrLYKTGDLVRYSSDGNLVCLGRKDSQ 2329
Cdd:COG0365    378 NPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYFGR-------FPG-------WYRTGDGARRDEDGYFWILGRSDDV 443
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2330 VKVRGQRVELGEVEhhmrkclpeaNQLA-----VE--VVP-PSGERDHAMLaAFIRLDDETRNSPLIIKyaEdnstaqiv 2401
Cdd:COG0365    444 INVSGHRIGTAEIE----------SALVshpavAEaaVVGvPDEIRGQVVK-AFVVLKPGVEPSDELAK--E-------- 502
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 2402 fltgIEEELSERLPQHMVPtvffALVHF----PTTTSGKTDRKRLREI 2445
Cdd:COG0365    503 ----LQAHVREELGPYAYP----REIEFvdelPKTRSGKIMRRLLRKI 542
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
6707-7043 1.39e-40

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 160.19  E-value: 1.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6707 LFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 6786
Cdd:cd17655      2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6787 PASRHEDILRQTGAQVIL-------------------------------------------------------------- 6804
Cdd:cd17655     82 PEERIQYILEDSGADILLtqshlqppiafiglidlldedtiyheesenlepvsksddlayviytsgstgkpkgvmiehrg 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6805 -----------------------------ASAQ----------------------------------------------- 6808
Cdd:cd17655    162 vvnlvewankviyqgehlrvalfasisfdASVTeifasllsgntlyivrketvldgqaltqyirqnritiidltpahlkl 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6809 ------------------------------------NTTLFQSSNQTVVTVNRSSYILFPDENREAYP-----------F 6841
Cdd:cd17655    242 ldaaddseglslkhlivggealstelakkiielfgtNPTITNAYGPTETTVDASIYQYEPETDQQVSVpigkplgntriY 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPAwlveghgkHPGrrGRLYKTGDLVYYNKDGNLVYIGR 6921
Cdd:cd17655    322 ILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF--------VPG--ERMYRTGDLARWLPDGNIEFLGR 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 KDGQVKVRGQRVELGEIENRLrecmpratQMAVEVispagaaeqAKTMVVAflqLNDEARDALLGGNVPNDDNLSaqvvf 7001
Cdd:cd17655    392 IDHQVKIRGYRIELGEIEARL--------LQHPDI---------KEAVVIA---RKDEQGQNYLCAYIVSEKELP----- 446
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 7002 PAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:cd17655    447 VAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
3465-3975 1.73e-40

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 159.65  E-value: 1.73e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAiCAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 3543
Cdd:cd05936      3 DLLEEAARRFPDKTA-LIFMGRkLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3544 DHPASRHEEIFEQTGAQVVVAsaqysarwtssschVVTVSKALSSQLPAVVDSTNTsvrPENAAYIIFTSGSTGVPKGVV 3623
Cdd:cd05936     82 LYTPRELEHILNDSGAKALIV--------------AVSFTDLLAAGAPLGERVALT---PEDVAVLQYTSGTTGVPKGAM 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3624 LEHR---AVATSCLGHGrAFGITNLSRVLQ----FASYTFDACiaeIITTLLCGGCIC-VPSDSDRRnsLAKAISTMDVN 3695
Cdd:cd05936    145 LTHRnlvANALQIKAWL-EDLLEGDDVVLAalplFHVFGLTVA---LLLPLALGATIVlIPRFRPIG--VLKEIRKHRVT 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3696 W---------AFLTPSVARLLDPgliPSLKILAIGGEQSSSADWNRWPGSVQKIHV--YGPTECC--IFCTGYTTKQgfE 3762
Cdd:cd05936    219 IfpgvptmyiALLNAPEFKKRDF---SSLRLCISGGAPLPVEVAERFEELTGVPIVegYGLTETSpvVAVNPLDGPR--K 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3763 PSTIGTSVASVSW-VVDPENHnrLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLlegypghpgrqgrlyKTG 3841
Cdd:cd05936    294 PGSIGIPLPGTEVkIVDDDGE--ELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG--WL---------------RTG 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3842 DLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvrECL---PEARQLAVeVILPSGQKDHAmLAAFVQLEEGtqnal 3918
Cdd:cd05936    355 DIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVE----EVLyehPAVAEAAV-VGVPDPYSGEA-VKAFVVLKEG----- 423
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 3919 ldkeaggedsmaqvvflASVEEE-----LAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd05936    424 -----------------ASLTEEeiiafCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
6716-7041 1.83e-40

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 159.10  E-value: 1.83e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6716 PNAPAVCAWDGELTYGELEALSTKLAGHLVQLG-VKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDI 6794
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6795 LRQTGAQVILASAQN---------TT----------------------------------LFQSS-------NQTVVTV- 6823
Cdd:cd17648     81 LEDTGARVVITNSTDlayaiytsgTTgkpkgvlvehgsvvnlrtslseryfgrdngdeavLFFSNyvfdffvEQMTLALl 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6824 NRSSYILFPDE------------NREA----------------------------------------------------- 6838
Cdd:cd17648    161 NGQKLVVPPDEmrfdpdrfyayiNREKvtylsgtpsvlqqydlarlphlkrvdaageeftapvfeklrsrfagliinayg 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6839 ------------YPFVRPSNAALA------------------PLGSIGELLVEGPILARGYLNDADKTAAAFVNDPawLV 6888
Cdd:cd17648    241 ptettvtnhkrfFPGDQRFDKSLGrpvrntkcyvlndamkrvPVGAVGELYLGGDGVARGYLNRPELTAERFLPNP--FQ 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6889 EGHGKHPGRRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLRECmPRATQMAveVISPAGAAEQAKT 6968
Cdd:cd17648    319 TEQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASY-PGVRECA--VVAKEDASQAQSR 395
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 6969 mvvaflqlndeARDALLGGNVPNDDNLSAQVVFPAkvdekLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd17648    396 -----------IQKYLVGYYLPEPGHVPESDLLSF-----LRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
9-283 1.95e-40

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 158.78  E-value: 1.95e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    9 TPSVARLL------EPSHIPSLRILVMGGEQVNSADW----DRWPSSVQTINGYGPTECCIVcTGYTSEQDFTTGT---- 74
Cdd:cd17650    192 TPALIRPVmayvyrNGLDLSAMRLLIVGSDGCKAQDFktlaARFGQGMRIINSYGVTEATID-STYYEEGRDPLGDsanv 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   75 -IGTSIASVS-WVVDPKDhgRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAwlleghggyaGRQGRLYKTGDL 152
Cdd:cd17650    271 pIGRPLPNTAmYVLDERL--QPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF----------APGERMYRTGDL 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  153 VRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVEVVLPLGQknHATLAAFIQLDKGTHNALLKekv 232
Cdd:cd17650    339 ARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLAR-HPAIDEAVVAVREDKGG--EARLCAYVVAAATLNTAELR--- 412
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  233 ggddsiarvvflagveEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd17650    413 ----------------AFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
6274-6689 2.19e-40

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 159.04  E-value: 2.19e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6274 VEDMYPCSPLQEGL----MSLTAKRAgdYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEEK 6349
Cdd:pfam00668    1 VQDEYPLSPAQKRMwfleKLEPHSSA--YNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6350 ---IQWTESKRL---------EEYLREDKAVSMGL-GDPLARYAIIKEAWGGKRWFvWTIHHALYDGWSLPRVLQAVKQA 6416
Cdd:pfam00668   79 pfeLEIIDISDLseseeeeaiEAFIQRDLQSPFDLeKGPLFRAGLFRIAENRHHLL-LSMHHIIVDGVSLGILLRDLADL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6417 YNGAVLETQ------PSFNAFI----QYLSQQDLEATAAYWQTALADCEATLfpPLPSSVKQLVADTTVEHQcplpSRST 6486
Cdd:pfam00668  158 YQQLLKGEPlplppkTPYKDYAewlqQYLQSEDYQKDAAYWLEQLEGELPVL--QLPKDYARPADRSFKGDR----LSFT 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6487 SDTTTSTLIR---------------AAWAIVASRYTSSDDVVFGTTITGRNAPvtSIDAIVGPTIATVPLRVRLQKDQTV 6551
Cdd:pfam00668  232 LDEDTEELLRklakahgttlndvllAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTF 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6552 SSFLGYLQQQATEMIAYEQTGLQQIAKMGPDPQ---HACGFQTLLVVQPAGDVLGSDDTLGKWRGYSGLQDFM----TYA 6624
Cdd:pfam00668  310 SELIKRVQEDLLSAEPHQGYPFGDLVNDLRLPRdlsRHPLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSVIeeeaKYD 389
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6625 L--GVRCTLSAEGVKI---TASFDARVIEHWvvekmLGQFSFAMQQLAEASADrKVADIDITTTTDRQQL 6689
Cdd:pfam00668  390 LslTASERGGGLTIKIdynTSLFDEETIERF-----AEHFKELLEQAIAHPSQ-PLSELDLLSDAEKQKL 453
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
9-283 2.56e-40

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 158.72  E-value: 2.56e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    9 TPSVARLLEPSHIPSLRILVMGGEQVNSADWDRWPSSV--QTINGYGPTECCIVCTGYTSE-QDFTTGTIGTSIASVSWV 85
Cdd:cd17648    194 TPSVLQQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFagLIINAYGPTETTVTNHKRFFPgDQRFDKSLGRPVRNTKCY 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   86 VDPKDHGRLaPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawLLEGHGGYAGRQGRLYKTGDLVRYDADGNLVCLG 165
Cdd:cd17648    274 VLNDAMKRV-PVGAVGELYLGGDGVARGYLNRPELTAERFLPNP--FQTEQERARGRNARLYKTGDLVRWLPSGELEYLG 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  166 RKDSQVKLRGQRVELGEVEHH------VRECLPEAKQLAVEVVLPlGQKNhatLAAFIQLDKGTHNAllkekvggddsia 239
Cdd:cd17648    351 RNDFQVKIRGQRIEPGEVEAAlasypgVRECAVVAKEDASQAQSR-IQKY---LVGYYLPEPGHVPE------------- 413
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1820002560  240 rvvflAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd17648    414 -----SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
PRK05691 PRK05691
peptide synthase; Validated
10-378 2.64e-40

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 168.04  E-value: 2.64e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   10 PS-VARLLEPSHIP--SLRILVMGGEQVN---SADW-DRWPSsVQTINGYGPTECCIVCTGYTSEQDFTTGT---IGTsi 79
Cdd:PRK05691  3968 PSlIQGMLAEDRQAldGLRWMLPTGEAMPpelARQWlQRYPQ-IGLVNAYGPAECSDDVAFFRVDLASTRGSylpIGS-- 4044
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   80 asvswvvdPKDHGRL---------APLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawlleghggYAGRQGRLYKTG 150
Cdd:PRK05691  4045 --------PTDNNRLylldealelVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHP---------FGAPGERLYRTG 4107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  151 DLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVEVVLPLGQKNhatLAAFIQLDKGTHN--ALL 228
Cdd:PRK05691  4108 DLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE-QAEVREAAVAVQEGVNGKH---LVGYLVPHQTVLAqgALL 4183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  229 KEkvggddsiarvvflagVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLR--EIGASFTAQQLAemrtssqgpk 306
Cdd:PRK05691  4184 ER----------------IKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPalDIGQLQSQAYLA---------- 4237
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560  307 rqPSTEAERTMQQLWARVLGIEpdSIGLDDSFFRLGGDSIAAIKLVGEARRTgLQPSVA--DIFRHPTLAALAS 378
Cdd:PRK05691  4238 --PRNELEQTLATIWADVLKVE--RVGVHDNFFELGGHSLLATQIASRVQKA-LQRNVPlrAMFECSTVEELAE 4306
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
4116-4509 3.39e-40

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 157.23  E-value: 3.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4116 YPCSPLQEGLMSLTAKRAGD--YIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELGLLQVVVEERI-QWTE 4192
Cdd:cd19536      2 YPLSSLQEGMLFHSLLNPGGsvYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQvPVTE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4193 ---------SESLEEYPREDKAVSMGV-GDRLARYALIKEPYDGgkRW-FVWTMHHALYDGWSLPRILHAVKQAYSGV-- 4259
Cdd:cd19536     82 ldltpleeqLDPLRAYKEETKIRRFDLgRAPLVRAALVRKDERE--RFlLVISDHHSILDGWSLYLLVKEILAVYNQLle 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4260 -----VLERQPsFNAFI-QYLSQQDPEAAAAYWQTALVDCKAALFPTLPPTVTQ-PVADTTVEYQCPPPSQSAT-----D 4327
Cdd:cd19536    160 ykplsLPPAQP-YRDFVaHERASIQQAASERYWREYLAGATLATLPALSEAVGGgPEQDSELLVSVPLPVRSRSlakrsG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4328 ITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGGEAIVGPTIATVPVRLRVQrDQTVFAFLQGVQQQATDMIAH 4407
Cdd:cd19536    239 IPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLS-EETVEDLLKRAQEQELESLSH 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4408 EQTGLQRIAKMSPGARHacgFQTLLVVQPTDdvlgSDDMLGEW-RSYSEMQDF------TTYALMVQCVLVKDRVGVTAS 4480
Cdd:cd19536    318 EQVPLADIQRCSEGEPL---FDSIVNFRHFD----LDFGLPEWgSDEGMRRGLlfsefkSNYDVNLSVLPKQDRLELKLA 390
                          410       420
                   ....*....|....*....|....*....
gi 1820002560 4481 FDARVIEQWVVEKMLRQFGFVMQQLADAG 4509
Cdd:cd19536    391 YNSQVLDEEQAQRLAAYYKSAIAELATAP 419
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
7611-8121 6.31e-40

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 157.72  E-value: 6.31e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAiCAWDGE-LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 7689
Cdd:cd05936      3 DLLEEAARRFPDKTA-LIFMGRkLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7690 DHPASRHEEIFEQTGAQVVVAsaqysarwtssschVVTVSKALSSQLPAVVDSTNTsvrPENAAYIIFTSGSTGVPKGVV 7769
Cdd:cd05936     82 LYTPRELEHILNDSGAKALIV--------------AVSFTDLLAAGAPLGERVALT---PEDVAVLQYTSGTTGVPKGAM 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7770 LEHR---AVATSCLGHGrAFGITNLSRVLQ----FASYTFDACiaeIITTLLCGGCIC-VPSDSDRRnsLAKAISTMDVN 7841
Cdd:cd05936    145 LTHRnlvANALQIKAWL-EDLLEGDDVVLAalplFHVFGLTVA---LLLPLALGATIVlIPRFRPIG--VLKEIRKHRVT 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7842 W---------AFLTPSVARLLDPgliPSLKILAIGGEQSSSADWNRWPGSVQKIHV--YGPTECC--IFCTGYTTKQgfE 7908
Cdd:cd05936    219 IfpgvptmyiALLNAPEFKKRDF---SSLRLCISGGAPLPVEVAERFEELTGVPIVegYGLTETSpvVAVNPLDGPR--K 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7909 PSTIGTSVASVSW-VVDPENHnrLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLlegypghpgrqgrlyKTG 7987
Cdd:cd05936    294 PGSIGIPLPGTEVkIVDDDGE--ELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG--WL---------------RTG 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7988 DLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvrECL---PEARQLAVeVILPSGQKNHAMLAvFVQLGKGTHIah 8064
Cdd:cd05936    355 DIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVE----EVLyehPAVAEAAV-VGVPDPYSGEAVKA-FVVLKEGASL-- 426
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 8065 leekaggedsmaqvvfltgTEEEL----AKRLPKHMVPTVFFALLHFPMTTSGKADRKRLR 8121
Cdd:cd05936    427 -------------------TEEEIiafcREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
6716-7041 1.25e-39

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 157.05  E-value: 1.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6716 PNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIL 6795
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6796 RQTGAQVIL------------------------ASAQNTT-----------LFQS-----------SNQ----TVVTVNR 6825
Cdd:cd12114     81 ADAGARLVLtdgpdaqldvavfdvlildldalaAPAPPPPvdvapddlayvIFTSgstgtpkgvmiSHRaalnTILDINR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6826 --------------------SSYILF-----------PDENREAYPF--------------------------------- 6841
Cdd:cd12114    161 rfavgpddrvlalsslsfdlSVYDIFgalsagatlvlPDEARRRDPAhwaelierhgvtlwnsvpallemlldvleaaqa 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 ------------------------VRPSNAALAPLG----------------------SI-------------------- 6855
Cdd:cd12114    241 llpslrlvllsgdwipldlparlrALAPDARLISLGgateasiwsiyhpidevppdwrSIpygrplanqryrvldprgrd 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6856 ------GELLVEGPILARGYLNDADKTAAAFVNDPAwlveghgkhpgrRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVR 6929
Cdd:cd12114    321 cpdwvpGELWIGGRGVALGYLGDPELTAARFVTHPD------------GERLYRTGDLGRYRPDGTLEFLGRRDGQVKVR 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6930 GQRVELGEIENRLrECMPRATQMAVEVISPAGAAEQAktmvvAFLqlndeardallggnVPNDDnlsAQVVFPAKVDEKL 7009
Cdd:cd12114    389 GYRIELGEIEAAL-QAHPGVARAVVVVLGDPGGKRLA-----AFV--------------VPDND---GTPIAPDALRAFL 445
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1820002560 7010 SNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd12114    446 AQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
854-1367 1.27e-39

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 158.04  E-value: 1.27e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVP-- 931
Cdd:PRK06187     8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPin 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  932 --LDPghpasrhEEIF---KQIGAQVVLTSSQHAMLFASSERHQVTVSKV-------STSQLPTVVNF-----AKSP--- 991
Cdd:PRK06187    88 irLKP-------EEIAyilNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVivegdgpAAPLAPEVGEYeellaAASDtfd 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  992 ---VDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVL----QFASYTFDACIAeiitTLLYGGCI 1064
Cdd:PRK06187   161 fpdIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHAWGLPYL----ALMAGAKQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1065 CVPSESDRRnNLAKAIstmdvncALLTPSVArllepSAVPSLKRLVLQGEQVSFADWNRW----------PGS------- 1127
Cdd:PRK06187   237 VIPRRFDPE-NLLDLI-------ETERVTFF-----FAVPTIWQMLLKAPRAYFVDFSSLrlviyggaalPPAllrefke 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1128 ---VQTINGYGPTECS--VCCN----------TYSGKQGFksGIIGTSVAslswVVDAgNHNRLAP-LGSIGELLVEGPI 1191
Cdd:PRK06187   304 kfgIDLVQGYGMTETSpvVSVLppedqlpgqwTKRRSAGR--PLPGVEAR----IVDD-DGDELPPdGGEVGEIIVRGPW 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1192 LARGYLNDIDKTEAAFIDDpaWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIE----H 1267
Cdd:PRK06187   377 LMQGYWNRPEATAETIDGG--WL---------------HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEdalyG 439
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1268 H--VREClpearqlAVeVILP---SGQKEHallaAFIQLDKGnhnalfeeKASGEDSMAQvvFLTGVeeeLAK-RLPEHm 1341
Cdd:PRK06187   440 HpaVAEV-------AV-IGVPdekWGERPV----AVVVLKPG--------ATLDAKELRA--FLRGR---LAKfKLPKR- 493
                          570       580
                   ....*....|....*....|....*.
gi 1820002560 1342 vptILFtVKAMPITTSGKIDRKRLQD 1367
Cdd:PRK06187   494 ---IAF-VDELPRTSVGKILKRVLRE 515
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
2075-2438 1.68e-39

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 152.82  E-value: 1.68e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2075 AYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCIcVPSDSERRDNLA 2154
Cdd:cd04433      3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTV-VLLPKFDPEAAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2155 KAITDMQVNWGYLTSSVARLLDPCL------VPSLKVLVLGGEQVNSTDWGKWPSS--VQTINGYGPTECCVFCTGYTG- 2225
Cdd:cd04433     82 ELIEREKVTILLGVPTLLARLLKAPesagydLSSLRALVSGGAPLPPELLERFEEApgIKLVNGYGLTETGGTVATGPPd 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2226 IQGFQSGNIGTSIASVSW-VVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDdpawlleGYpghegrqgr 2304
Cdd:cd04433    162 DDARKPGSVGRPVPGVEVrIVDPD--GGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GW--------- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2305 lYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKClPEANQLAVEVVPPS--GERdhamLAAFIRLDDEt 2382
Cdd:cd04433    224 -YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGH-PGVAEAAVVGVPDPewGER----VVAVVVLRPG- 296
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 2383 rnspliikyaEDNSTAQIVfltgieEELSERLPQHMVPTVFFALVHFPTTTSGKTD 2438
Cdd:cd04433    297 ----------ADLDAEELR------AHVRERLAPYKVPRRVVFVDALPRTASGKID 336
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
878-1337 2.50e-39

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 155.83  E-value: 2.50e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIfkqigaqvvLTSS 957
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYI---------LNDS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  958 QHAMLFASserhqvtvskvstsqlptvvnfakspvDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHA 1037
Cdd:cd05907     77 EAKALFVE---------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1038 RVLQF--ASYTFdACIAEIITTLLYGGCICVPSesdRRNNLAKAISTmdvncalLTP----SVARLLEP-------SAVP 1104
Cdd:cd05907    130 RHLSFlpLAHVF-ERRAGLYVPLLAGARIYFAS---SAETLLDDLSE-------VRPtvflAVPRVWEKvyaaikvKAVP 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1105 SLKRLVLQ---GEQVSFA---------DWNRWPGS--VQTINGYGPTECS--VCCNTysgKQGFKSGIIGtsvaslsWVV 1168
Cdd:cd05907    199 GLKRKLFDlavGGRLRFAasggaplpaELLHFFRAlgIPVYEGYGLTETSavVTLNP---PGDNRIGTVG-------KPL 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1169 DaGNHNRLAPlgsIGELLVEGPILARGYLNDIDKTEAAFIDDPaWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGR 1248
Cdd:cd05907    269 P-GVEVRIAD---DGEILVRGPNVMLGYYKNPEATAEALDADG-WL---------------HTGDLGEIDEDGFLHITGR 328
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1249 -KDSQVKVRGQRVELGEIEHHVREClpearqLAVEVILPSGQKEhALLAAFIQLDKGNHNALFEEKASGEDSMAQVVFLT 1327
Cdd:cd05907    329 kKDLIITSGGKNISPEPIENALKAS------PLISQAVVIGDGR-PFLVALIVPDPEALEAWAEEHGIAYTDVAELAANP 401
                          490
                   ....*....|
gi 1820002560 1328 GVEEELAKRL 1337
Cdd:cd05907    402 AVRAEIEAAV 411
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
4560-5049 5.70e-39

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 155.45  E-value: 5.70e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4560 ICAWDG-ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTG 4638
Cdd:cd05911      3 IDADTGkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4639 AQVVLASAQ-YATLWTSL-----GRSVVIVSEASTSQLPVVTKTADPSVNPGNA------------AYAIFTSGSTGIPK 4700
Cdd:cd05911     83 PKVIFTDPDgLEKVKEAAkelgpKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDlppplkdgkddtAAILYSSGTTGLPK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4701 GVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDAcIAEIITTLLC--CGCICVPSDSDRRNNLAKAINAMDVNWAL 4778
Cdd:cd05911    163 GVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYH-IYGLFTTLASllNGATVIIMPKFDSELFLDLIEKYKITFLY 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4779 LTPSVARML--DPCVV----QSLKILVLGGEQVNSADWDRWPKSIQT---INAYGPTECS-ICCTTYSGKQgfKSGTIGT 4848
Cdd:cd05911    242 LVPPIAAALakSPLLDkydlSSLRVILSGGAPLSKELQELLAKRFPNatiKQGYGMTETGgILTVNPDGDD--KPGSVGR 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4849 SIVSVSW-VVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAFIDDpAWLlegygghsgrqgrlyKTGDLVRYD 4927
Cdd:cd05911    320 LLPNVEAkIVDDDGKDSLGP-NEPGEICVRGPQVMKGYYNNPEATKETFDED-GWL---------------HTGDIGYFD 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4928 ADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREcLTEAKQLAVeVIVPEGEGGYAMlAAFVqlgddtyntlVKEKagGDS 5007
Cdd:cd05911    383 EDGYLYIVDRKKELIKYKGFQVAPAELEAVLLE-HPGVADAAV-IGIPDEVSGELP-RAYV----------VRKP--GEK 447
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 5008 LTvqvvfLDRVEEELAKRVPEHMMLT--TFFTlEAMPTTTSGKI 5049
Cdd:cd05911    448 LT-----EKEVKDYVAKKVASYKQLRggVVFV-DEIPKSASGKI 485
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
4558-5055 1.68e-38

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 153.00  E-value: 1.68e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4558 PAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQT 4637
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4638 GAQVVLASAQyatlwtslgrsvvivseastsqlpvvtktadpsvnpgNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHG 4717
Cdd:cd05919     82 EARLVVTSAD-------------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4718 -QAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVpSDSDRRNNLAKAINAmdvnwALLTPSV--------ARMLD 4788
Cdd:cd05919    125 rEALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAV-LNPGWPTAERVLATL-----ARFRPTVlygvptfyANLLD 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4789 PCVVQ-----SLKILVLGGEQVNSADWDRWPKS--IQTINAYGPTEcsICCTTYSGKQGfkSGTIGTSIVSVSW----VV 4857
Cdd:cd05919    199 SCAGSpdalrSLRLCVSAGEALPRGLGERWMEHfgGPILDGIGATE--VGHIFLSNRPG--AWRLGSTGRPVPGyeirLV 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4858 DPENHNrlAPLGSIGELLVEGPILARGYLNDMEKTEAAFiddpawllegygghsgrQGRLYKTGDLVRYDADGNLVYLGR 4937
Cdd:cd05919    275 DEEGHT--IPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-----------------NGGWYRTGDKFCRDADGWYTHAGR 335
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4938 KDSQVKLRGQRVELGEVEHHVreCLTEAKQLAVEVIVPEGEGGyAMLAAFVQLGDDtyntlvkekaggdsLTVQVVFLDR 5017
Cdd:cd05919    336 ADDMLKVGGQWVSPVEVESLI--IQHPAVAEAAVVAVPESTGL-SRLTAFVVLKSP--------------AAPQESLARD 398
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 5018 VEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLR 5055
Cdd:cd05919    399 IHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
4547-5056 2.34e-38

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 154.57  E-value: 2.34e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHP 4626
Cdd:PRK06187    12 LRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLK 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4627 ASRHEHIFRQTGAQVVLASAQYATLWTSL------GRSVVIVSEASTSQLPVVTKTAD------------PSVNPGNAAY 4688
Cdd:PRK06187    92 PEEIAYILNDAEDRVVLVDSEFVPLLAAIlpqlptVRTVIVEGDGPAAPLAPEVGEYEellaaasdtfdfPDIDENDAAA 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4689 AIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVL----QFASYTFDACIAeiitTLLCCGCICVPsdsdRR-- 4762
Cdd:PRK06187   172 MLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHAWGLPYL----ALMAGAKQVIP----RRfd 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4763 -NNLAKAINAMDVNWALLTPSVARML-----DPCV-VQSLKILVLGGEQVNSADWDRWPK--SIQTINAYGPTECS--IC 4831
Cdd:PRK06187   244 pENLLDLIETERVTFFFAVPTIWQMLlkaprAYFVdFSSLRLVIYGGAALPPALLREFKEkfGIDLVQGYGMTETSpvVS 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4832 CTTYS---GKQGFKSGTIGTSIVSVSW-VVDPENhNRLAP-LGSIGELLVEGPILARGYLNDMEKTEAAFIDDpaWLleg 4906
Cdd:PRK06187   324 VLPPEdqlPGQWTKRRSAGRPLPGVEArIVDDDG-DELPPdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG--WL--- 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4907 ygghsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE----HH--VREClteakqlAVeVIVPEGEGG 4980
Cdd:PRK06187   398 ------------HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEdalyGHpaVAEV-------AV-IGVPDEKWG 457
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 4981 YAMLaAFVQLGDDtyntlvkEKAGGDSLTvqvVFLdrvEEELAK-RVPEHMmltTFftLEAMPTTTSGKIDRKRLRE 5056
Cdd:PRK06187   458 ERPV-AVVVLKPG-------ATLDAKELR---AFL---RGRLAKfKLPKRI---AF--VDELPRTSVGKILKRVLRE 515
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
5623-6138 2.74e-38

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 155.27  E-value: 2.74e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5623 CVHDLFTEQAKARPHAPAICaWDGE------LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAG 5696
Cdd:COG0365     10 IAYNCLDRHAEGRGDKVALI-WEGEdgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5697 GAFVPLDPDHPASRHEDTFRHTGAQVVVTSAqhSARWIGTNHQVVTVSAGSLGQLSTL-----VNPVGLPAIPENAV--- 5768
Cdd:COG0365     89 AVHSPVFPGFGAEALADRIEDAEAKVLITAD--GGLRGGKVIDLKEKVDEALEELPSLehvivVGRTGADVPMEGDLdwd 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5769 ---------------------YIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRA-FGITNLSRVLQFA--------SYTFD 5818
Cdd:COG0365    167 ellaaasaefepeptdaddplFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTAdigwatghSYIVY 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5819 ACMdeII--TTLMYGGcICVPSDSDRrndLVKAISTMDVSCALLTPSVARLL--------EPSSVPTLQMLVLQGEQVSF 5888
Cdd:COG0365    247 GPL--LNgaTVVLYEG-RPDFPDPGR---LWELIEKYGVTVFFTAPTAIRALmkagdeplKKYDLSSLRLLGSAGEPLNP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5889 ADWNRWPASVQT--INGYGPTECSICCNTYSGKQGFKSGIIGT-----SVAsvswVVDPENHDrlAPLGSIGELLVEGPI 5961
Cdd:COG0365    321 EVWEWWYEAVGVpiVDGWGQTETGGIFISNLPGLPVKPGSMGKpvpgyDVA----VVDEDGNP--VPPGEEGELVIKGPW 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5962 --LARGYLNDIQKTAAVFIDDpawllegYPGhpgrqgrLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVE--- 6036
Cdd:COG0365    395 pgMFRGYWNDPERYRETYFGR-------FPG-------WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIEsal 460
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6037 --HH-VREClpearqlAVeVILPSGQKDHAMLaAFVQLEEGTQnalldkeasGEDSMAQVVFlASVEEELAKrlpeHMVP 6113
Cdd:COG0365    461 vsHPaVAEA-------AV-VGVPDEIRGQVVK-AFVVLKPGVE---------PSDELAKELQ-AHVREELGP----YAYP 517
                          570       580
                   ....*....|....*....|....*...
gi 1820002560 6114 -TVFF--SLlhfPTTTSGKTDRKRLREI 6138
Cdd:COG0365    518 rEIEFvdEL---PKTRSGKIMRRLLRKI 542
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
3019-3448 1.11e-37

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 150.95  E-value: 1.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3019 VEDVFPCTPMQEGILTSQGKDPD--AYWVCFIYEVIPNqetsISLARLQQAWKGVVHQHSLLRTLLVDnvpGSTGTTNVV 3096
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHssAYNMPAVLKLTGE----LDPERLEKALQELINRHDALRTVFIR---QENGEPVQV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3097 LKDPQP------SISVFS-SEGTATIELFRSRynpaaqrsigQLQHHL----------SICQLNNGKVYLCLDINHAIID 3159
Cdd:pfam00668   74 ILEERPfeleiiDISDLSeSEEEEAIEAFIQR----------DLQSPFdlekgplfraGLFRIAENRHHLLLSMHHIIVD 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3160 AHSRGILMHDLQEAYDANLN------PQSTSFRDFA----SYIKQQSQEEAGRYWAEYLDGVEPC------FFPSLGDSG 3223
Cdd:pfam00668  144 GVSLGILLRDLADLYQQLLKgeplplPPKTPYKDYAewlqQYLQSEDYQKDAAYWLEQLEGELPVlqlpkdYARPADRSF 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3224 GANTIprTVEVPSIDSSAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPihNVNSIFGPLISILPC 3303
Cdd:pfam00668  224 KGDRL--SFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPL 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3304 RIHLHKQLTVLEALKTVQENYASSLSFQTFPLASMHSFLGL----GTSALFNTALSLQRIddigPCSASEITLKMKEGLD 3379
Cdd:pfam00668  300 RIDPKGGKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLRLprdlSRHPLFDPMFSFQNY----LGQDSQEEEFQLSELD 375
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 3380 P---------TEYNITLSAGYSKDAIDISMTFRAGCMDLVQAKRLASNFSQAIKAVTTEPHSRIYSLDILTYNESKKI 3448
Cdd:pfam00668  376 LsvssvieeeAKYDLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
4114-4528 1.25e-37

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 150.56  E-value: 1.25e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4114 DVYPCSPLQEGL----MSLTAKRAgdYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELGLLQVVVEER-I 4188
Cdd:pfam00668    3 DEYPLSPAQKRMwfleKLEPHSSA--YNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERpF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4189 QW-----------TESESLEEYPREDKAVSMGV-GDRLARYALIKepYDGGKRWFVWTMHHALYDGWSLPRILHAVKQAY 4256
Cdd:pfam00668   81 ELeiidisdlsesEEEEAIEAFIQRDLQSPFDLeKGPLFRAGLFR--IAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4257 SGVVLERQ------PSFNAFI----QYLSQQDPEAAAAYWQTALvdcKAALFPT-LPPTVTQPVADTTVEYQ----CPPP 4321
Cdd:pfam00668  159 QQLLKGEPlplppkTPYKDYAewlqQYLQSEDYQKDAAYWLEQL---EGELPVLqLPKDYARPADRSFKGDRlsftLDED 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4322 S-------QSATDITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGGEAIVGPTIATVPVRLRVQRDQTVFAFL 4394
Cdd:pfam00668  236 TeellrklAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTFSELI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4395 QGVQQQATDMIAHEQTGLQRIAKMSPGAR---HACGFQTLLVVQPTddvLGSDDMLGEWRSY-------SEMQDFTTYAL 4464
Cdd:pfam00668  314 KRVQEDLLSAEPHQGYPFGDLVNDLRLPRdlsRHPLFDPMFSFQNY---LGQDSQEEEFQLSeldlsvsSVIEEEAKYDL 390
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 4465 MVQCVLVKDRVGVTASFDARVIEQWVVEKMLRQFGFVMQQLAdAGEEKKVAGIETTTTGDRQQL 4528
Cdd:pfam00668  391 SLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAI-AHPSQPLSELDLLSDAEKQKL 453
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
877-1360 4.35e-37

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 149.67  E-value: 4.35e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpgHPASRHEEI---FKQIGAQVV 953
Cdd:cd05911     10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAA---NPIYTADELahqLKISKPKVI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  954 LTSSQH-------AMLFASSERHQVTVSKVSTSQLPTVV----------NFAKSPVDPGN-TAYIIFTSGTTGIPKGVVL 1015
Cdd:cd05911     87 FTDPDGlekvkeaAKELGPKDKIIVLDDKPDGVLSIEDLlsptlgeedeDLPPPLKDGKDdTAAILYSSGTTGLPKGVCL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1016 QHRAVTTSCLGHGEAFGYTDHARVLQFASYTFD--ACIAEIITTLLYGGCICVPSESDRRNNLaKAISTMDVNCALLTPS 1093
Cdd:cd05911    167 SHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiYGLFTTLASLLNGATVIIMPKFDSELFL-DLIEKYKITFLYLVPP 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1094 VARLLEPSA------VPSLKRLV-----LQGEQVSFADwNRWPGsVQTINGYGPTECSVCCnTYSGKQGFKSGIIGTSVA 1162
Cdd:cd05911    246 IAAALAKSPlldkydLSSLRVILsggapLSKELQELLA-KRFPN-ATIKQGYGMTETGGIL-TVNPDGDDKPGSVGRLLP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1163 S--LSWVVDAGnhNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpAWLlegyeghagrrgrlyKTGDLVRCDAD 1240
Cdd:cd05911    323 NveAKIVDDDG--KDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDED-GWL---------------HTGDIGYFDED 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1241 GNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQLAVeVILP---SGQkehaLLAAFIQLDKGnhnalfeEKASGE 1317
Cdd:cd05911    385 GYLYIVDRKKELIKYKGFQVAPAELEAVLLE-HPGVADAAV-IGIPdevSGE----LPRAYVVRKPG-------EKLTEK 451
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 1318 DsmaqvvfltgVEEELAKRLPEH--MVPTILFtVKAMPITTSGKI 1360
Cdd:cd05911    452 E----------VKDYVAKKVASYkqLRGGVVF-VDEIPKSASGKI 485
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
3023-3430 5.31e-37

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 147.98  E-value: 5.31e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3023 FPCTPMQEGIL---TSQGKDpDAYWVCFIYEVipnqETSISLARLQQAWKGVVHQHSLLRTLLVDNvpGSTGTTNVVLKD 3099
Cdd:cd19536      2 YPLSSLQEGMLfhsLLNPGG-SVYLHNYTYTV----GRRLNLDLLLEALQVLIDRHDILRTSFIED--GLGQPVQVVHRQ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3100 PQPSISVFS----SEGTATIELFRSRYNPAAQRSIGQLQHHLSICQLN-NGKVYLCLDINHAIIDAHSRGILMHDLQEAY 3174
Cdd:cd19536     75 AQVPVTELDltplEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDeRERFLLVISDHHSILDGWSLYLLVKEILAVY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3175 DANL------NPQSTSFRDF-ASYIKQQSQEEAGRYWAEYLDGVE--PCFFPSLGDSGGANTIPRTVEVPSIDSSaVHMF 3245
Cdd:cd19536    155 NQLLeykplsLPPAQPYRDFvAHERASIQQAASERYWREYLAGATlaTLPALSEAVGGGPEQDSELLVSVPLPVR-SRSL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3246 CKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPLISILPCRIHLHKQlTVLEALKTVQENYA 3325
Cdd:cd19536    234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLSEE-TVEDLLKRAQEQEL 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3326 SSLSFQTFPLASMHSflgLGTS-ALFNTALSLQRIDDIGpcSASEITLKMKEGLD------PTEYNITLSAGYSKDAIDI 3398
Cdd:cd19536    313 ESLSHEQVPLADIQR---CSEGePLFDSIVNFRHFDLDF--GLPEWGSDEGMRRGllfsefKSNYDVNLSVLPKQDRLEL 387
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1820002560 3399 SMTFRAGCMDLVQAKRLASNFSQAIKAVTTEP 3430
Cdd:cd19536    388 KLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
5196-5586 6.13e-37

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 147.84  E-value: 6.13e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5196 MYPCSPLQEGLM--SLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEE------ 5267
Cdd:cd19547      1 VYPLAPMQEGMLfrGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDlappwa 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5268 KIQWTE------SKRLEEYLREDKAVSMGLGD-RLARYALIKEpyDGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGA 5340
Cdd:cd19547     81 LLDWSGedpdrrAELLERLLADDRAAGLSLADcPLYRLTLVRL--GGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEEL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5341 VPERQPSFNA---FIQYLGQQDLEAA-----TLYWQTALADCKAALFPTLPP---------------TVTQPVADTTVEY 5397
Cdd:cd19547    159 AHGREPQLSPcrpYRDYVRWIRARTAqseesERFWREYLRDLTPSPFSTAPAdregefdtvvhefpeQLTRLVNEAARGY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5398 qcpppsqsatDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGVEAMVGPTIATVPLRVCLQKDQTVSTLLEC 5477
Cdd:cd19547    239 ----------GVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLET 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5478 LQQQSTDMIAHEQTGLQRIAKMSPGARHACG--FQTLLVVQ--PTDDVlgSDDMLGEWRSYSEMQDFTTYALMVqCTLAK 5553
Cdd:cd19547    309 IHRDLATTAAHGHVPLAQIKSWASGERLSGGrvFDNLVAFEnyPEDNL--PGDDLSIQIIDLHAQEKTEYPIGL-IVLPL 385
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1820002560 5554 DRVEVTASFDARVIEQWVVEKMLRQFGFVMQQL 5586
Cdd:cd19547    386 QKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQL 418
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
23-283 9.22e-37

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 147.70  E-value: 9.22e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADwdrwPSSVQTINGYGPTECCIVCTGYTSEQDFTTGTIGTSIASVSWVVDPKDHgRLAPLGSVGE 102
Cdd:cd17645    216 SLRVLLTGGDKLKKIE----RKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEAL-QLQPIGVAGE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  103 LLVEGPILARGYLSDPEKTAAVFINNPAWLLEghggyagrqgRLYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGE 182
Cdd:cd17645    291 LCIAGEGLARGYLNRPELTAEKFIVHPFVPGE----------RMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGE 360
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  183 VEHHVREcLPEAKQLAvevVLPLGQKNHAT-LAAFIQLDKGTHNALLKEKVGGDdsiarvvflagveeelakrLPKHMVP 261
Cdd:cd17645    361 IEPFLMN-HPLIELAA---VLAKEDADGRKyLVAYVTAPEEIPHEELREWLKND-------------------LPDYMIP 417
                          250       260
                   ....*....|....*....|..
gi 1820002560  262 TVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd17645    418 TYFVHLKALPLTANGKVDRKAL 439
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
1506-1893 1.10e-36

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 147.07  E-value: 1.10e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1506 IYPCSPLQEGLM--SLTAKRAGDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQVVIEE------ 1577
Cdd:cd19547      1 VYPLAPMQEGMLfrGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDlappwa 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1578 NIQWTEPKS------LEEYLSEDKAVSVGLGD-PLARYAFVKEAcGGKRWFVWTIHHAVYDGWSLPLILHAVKQVYSGGV 1650
Cdd:cd19547     81 LLDWSGEDPdrraelLERLLADDRAAGLSLADcPLYRLTLVRLG-GGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1651 LQWQPSFNA---FIQYLG-----QQDLEATVAYWQTALADCEAVLFPTLPP---------------TVTQPVADATVEYq 1707
Cdd:cd19547    160 HGREPQLSPcrpYRDYVRwirarTAQSEESERFWREYLRDLTPSPFSTAPAdregefdtvvhefpeQLTRLVNEAARGY- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1708 cpplskatsDTTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNTPVTGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGL 1787
Cdd:cd19547    239 ---------GVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETI 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1788 QQQATDMIAHEQTGLQRIAKMGQGPQHACS--FQTLLVVQ--PVDDVLDNTLGEWRDHSELQEFTTYTLMLqCMLAAEGV 1863
Cdd:cd19547    310 HRDLATTAAHGHVPLAQIKSWASGERLSGGrvFDNLVAFEnyPEDNLPGDDLSIQIIDLHAQEKTEYPIGL-IVLPLQKL 388
                          410       420       430
                   ....*....|....*....|....*....|
gi 1820002560 1864 QITASFDTRVIEKWVVEKMLRQFSFIMQQL 1893
Cdd:cd19547    389 AFHFNYDTTHFTRAQVDRFIEVFRLLTEQL 418
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
6704-7043 2.00e-36

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 147.26  E-value: 2.00e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6704 VHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 6783
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6784 PDHPASRHEDILRQTGAQVILASAQN----TT------------LFQSSNQ----------------------------- 6818
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVTALILytsgTTgrpkgvmlthrnLLANAAAiaaalgltpgdvvlvalplfhvfgltvgl 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6819 --------TVVTVNRSSYILF-------------------------PDENR----------------------------- 6836
Cdd:COG0318    161 lapllagaTLVLLPRFDPERVlelierervtvlfgvptmlarllrhPEFARydlsslrlvvsggaplppellerfeerfg 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6837 ----------EAYPFV--RPSNAALAPLGSIG------------------------ELLVEGPILARGYLNDADKTAAAF 6880
Cdd:COG0318    241 vrivegygltETSPVVtvNPEDPGERRPGSVGrplpgvevrivdedgrelppgevgEIVVRGPNVMKGYWNDPEATAEAF 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6881 vndpawlveghgkhpgrRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLRECmPRATQMAVeVISPA 6960
Cdd:COG0318    321 -----------------RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAH-PGVAEAAV-VGVPD 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6961 GAAEQAktmVVAFLQLNDEARdallggnvpnddnlsaqvVFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKR 7040
Cdd:COG0318    382 EKWGER---VVAFVVLRPGAE------------------LDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRA 440

                   ...
gi 1820002560 7041 LRE 7043
Cdd:COG0318    441 LRE 443
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
7182-7571 4.23e-36

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 145.53  E-value: 4.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7182 IYPCSPLQEGLI--SLTAKRAGDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVVVEE------ 7253
Cdd:cd19547      1 VYPLAPMQEGMLfrGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDlappwa 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7254 KIQWTE------SEALEEYLKEDKAVSMGLGD-PLAHYALVKEAwGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAV 7326
Cdd:cd19547     81 LLDWSGedpdrrAELLERLLADDRAAGLSLADcPLYRLTLVRLG-GGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7327 LERQPSFNA---FIQYLGQqdLEATAA-------YWQTALSDCEAVLFPPLPSTvTQPVADTTVEYQCPPLSKATLDT-- 7394
Cdd:cd19547    160 HGREPQLSPcrpYRDYVRW--IRARTAqseeserFWREYLRDLTPSPFSTAPAD-REGEFDTVVHEFPEQLTRLVNEAar 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7395 ----TTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPIAGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDM 7470
Cdd:cd19547    237 gygvTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATT 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7471 IAHEQTGLQHIAKLGSGPRHACG--FQTLLVVQ--PVDDVlgSDDMLGEWRSYSKMQDFTTYALMVqFTLAAEGVQITAS 7546
Cdd:cd19547    317 AAHGHVPLAQIKSWASGERLSGGrvFDNLVAFEnyPEDNL--PGDDLSIQIIDLHAQEKTEYPIGL-IVLPLQKLAFHFN 393
                          410       420
                   ....*....|....*....|....*
gi 1820002560 7547 FDARVIEHWVLEKMLRQFSFIMQQL 7571
Cdd:cd19547    394 YDTTHFTRAQVDRFIEVFRLLTEQL 418
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
424-816 5.61e-36

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 145.15  E-value: 5.61e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  424 MYLCSPLQEGLM--SLTTKRAGDYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQVVVEE------ 495
Cdd:cd19547      1 VYPLAPMQEGMLfrGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDlappwa 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  496 KMQWTE------SESLEEYLNEDKAASMGLGD-RLARYALIKEScGGKRWFVWTIHHALYDGWSLPLVLDAVKQVYSGAA 568
Cdd:cd19547     81 LLDWSGedpdrrAELLERLLADDRAAGLSLADcPLYRLTLVRLG-GGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  569 LERQPSFNT---FIQYVSQQDVKAAAA-----YWQTALADCEAVLFPPLPS---------------TVTQPVADTTVKYq 625
Cdd:cd19547    160 HGREPQLSPcrpYRDYVRWIRARTAQSeeserFWREYLRDLTPSPFSTAPAdregefdtvvhefpeQLTRLVNEAARGY- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  626 cppspevtssNITTSTLIRAAWAIIASRYTSSEDIVFGTTVTGRNAPITGVEAMVGPTIATVPLRVRPRKGQTVSAFLEN 705
Cdd:cd19547    239 ----------GVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLET 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  706 LQQQATEMIAYEQTGLQRIMKMGPGPQHACG--FQTLLVV--HPTDDVLSSDDTLgewhSRSDSELQYFTTYALTIqCTL 781
Cdd:cd19547    309 IHRDLATTAAHGHVPLAQIKSWASGERLSGGrvFDNLVAFenYPEDNLPGDDLSI----QIIDLHAQEKTEYPIGL-IVL 383
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1820002560  782 AVEGVQITASFDARVVEHWVVEKMLGQFSFVMQQL 816
Cdd:cd19547    384 PLQKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQL 418
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
5647-6135 1.27e-35

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 146.12  E-value: 1.27e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5647 ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRhedtfrhtgaQVVVTS 5726
Cdd:cd17647     20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR----------QNIYLG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5727 AQHSARWIGTNHQVVTVSAGSLGQLStlvnpvglpaipenavyimFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNL 5806
Cdd:cd17647     90 VAKPRGLIVIRAAGVVVGPDSNPTLS-------------------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5807 SRVLQFASYTFDACMDEIITTLMYGGCICVPSDSD--RRNDLVKAISTMDVSCALLTPSVARLLEPSSV---PTLQMLVL 5881
Cdd:cd17647    151 DKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDigTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATtpfPKLHHAFF 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5882 QGEQVSFADWNRWPA---SVQTINGYGPTECSICCN-----TYSGKQGF----KSGI-IGTSVASVSW-VVDPENHDRLA 5947
Cdd:cd17647    231 VGDILTKRDCLRLQTlaeNVRIVNMYGTTETQRAVSyfevpSRSSDPTFlknlKDVMpAGRGMLNVQLlVVNRNDRTQIC 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5948 PLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpaWLLEgyPGH----------PGRQ------GRLYKTGDLVRYDANG 6011
Cdd:cd17647    311 GIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNN--WFVE--PDHwnyldkdnnePWRQfwlgprDRLYRTGDLGRYLPNG 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6012 NLVCLGRKDSQVKLRGQRVELGEVEHH------VRECLPEARQlavevilpsGQKDHAMLAAFV------QLEEGTQNAL 6079
Cdd:cd17647    387 DCECCGRADDQVKIRGFRIELGEIDTHisqhplVRENITLVRR---------DKDEEPTLVSYIvprfdkPDDESFAQED 457
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6080 LDKEASGEDSMAQVV----FLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd17647    458 VPKEVSTDPIVKGLIgyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
17-283 1.48e-35

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 145.11  E-value: 1.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   17 EPSHIPSLRILVMGGeqvnsaDW----------DRWPSSVQTINGyGPTECCIVCTGYT-SEQDFTTGTI--GTSIASVS 83
Cdd:cd12114    238 AQALLPSLRLVLLSG------DWipldlparlrALAPDARLISLG-GATEASIWSIYHPiDEVPPDWRSIpyGRPLANQR 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   84 W-VVDPkdHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAwlleghggyagrQGRLYKTGDLVRYDADGNLV 162
Cdd:cd12114    311 YrVLDP--RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPD------------GERLYRTGDLGRYRPDGTLE 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  163 CLGRKDSQVKLRGQRVELGEVEhHVRECLPEAKQLAVEVvlpLGQKNHATLAAFIQLDKGthnallkekvggddsiARVV 242
Cdd:cd12114    377 FLGRRDGQVKVRGYRIELGEIE-AALQAHPGVARAVVVV---LGDPGGKRLAAFVVPDND----------------GTPI 436
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1820002560  243 FLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd12114    437 APDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
4115-4505 5.68e-35

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 142.07  E-value: 5.68e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4115 VYPCSPLQEGLM--SLTAKRAGDYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELGLLQVVVEE------ 4186
Cdd:cd19547      1 VYPLAPMQEGMLfrGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDlappwa 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4187 RIQWTE------SESLEEYPREDKAVSMGVGD-RLARYALIKEpyDGGKRWFVWTMHHALYDGWSLPRILHAVKQAYSGV 4259
Cdd:cd19547     81 LLDWSGedpdrrAELLERLLADDRAAGLSLADcPLYRLTLVRL--GGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEEL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4260 VLERQPS------FNAFIQYLSQQDP--EAAAAYWQTALVDCKAALFPTLPP---------------TVTQPVADTTVEY 4316
Cdd:cd19547    159 AHGREPQlspcrpYRDYVRWIRARTAqsEESERFWREYLRDLTPSPFSTAPAdregefdtvvhefpeQLTRLVNEAARGY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4317 qcpppsqsatDITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQTVFAFLQG 4396
Cdd:cd19547    239 ----------GVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLET 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4397 VQQQATDMIAHEQTGLQRIAKMSPGARHACG--FQTLLVVQ--PTDDVlgSDDMLGEWRSYSEMQDFTTYALMVqCVLVK 4472
Cdd:cd19547    309 IHRDLATTAAHGHVPLAQIKSWASGERLSGGrvFDNLVAFEnyPEDNL--PGDDLSIQIIDLHAQEKTEYPIGL-IVLPL 385
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1820002560 4473 DRVGVTASFDARVIEQWVVEKMLRQFGFVMQQL 4505
Cdd:cd19547    386 QKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQL 418
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
8261-8635 9.22e-35

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 140.90  E-value: 9.22e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8261 VVPASYIQQFYIATGVRAPREAFNYPFIDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQ-GKLYQVIPRHQDLPFSif 8339
Cdd:cd19545      1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDsGGLLQVVVKESPISWT-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8340 evngalaEESQAIHIRDLDQTSPLGLPTS---FTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQEPLLSTTG 8416
Cdd:cd19545     79 -------ESTSLDEYLEEDRAAPMGLGGPlvrLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPP 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8417 FHSYLAYVHNQR-SASINYWSRLLKGS----HITNITSKLRPKLGkdttirsVKVERVIRTPQ-LPTGLTMASLVSSAWA 8490
Cdd:cd19545    152 FSRFVKYLRQLDdEAAAEFWRSYLAGLdpavFPPLPSSRYQPRPD-------ATLEHSISLPSsASSGVTLATVLRAAWA 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8491 VVLSHISGEEDVVYGLVVAGRNSDLPSITEV-------------------------SVQDQYISLGESDSIGLDDIVQHC 8545
Cdd:cd19545    225 LVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIvgptiatvplrvridpeqsvedflqTVQKDLLDMIPFEHTGLQNIRRLG 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8546 TDWPAKSEFDS--IIQHQNIEEQPEIQFAG---ETTKLQWFkNSFAVSrqlfVFSHPRGNSLTITITGNTGILTDQCAEK 8620
Cdd:cd19545    305 PDARAACNFQTllVVQPALPSSTSESLELGieeESEDLEDF-SSYGLT----LECQLSGSGLRVRARYDSSVISEEQVER 379
                          410
                   ....*....|....*
gi 1820002560 8621 LLVMLCDTISQLSDS 8635
Cdd:cd19545    380 LLDQFEHVLQQLASA 394
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
5624-6137 1.13e-34

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 143.40  E-value: 1.13e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5624 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 5703
Cdd:PRK06187     8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5704 PDHPASRHEDTFRHTGAQVVVTSAQHS------ARWIGTNHQVVTVSAGSlgqLSTLVNPVG--------------LPAI 5763
Cdd:PRK06187    88 IRLKPEEIAYILNDAEDRVVLVDSEFVpllaaiLPQLPTVRTVIVEGDGP---AAPLAPEVGeyeellaaasdtfdFPDI 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5764 PENAVYIMF-TSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVL----QFASYTFDACmdeiITTLMYGGCICVPs 5838
Cdd:PRK06187   165 DENDAAAMLyTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHAWGLP----YLALMAGAKQVIP- 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5839 dsdRRND---LVKAISTMDVSCALLtpsvarllepssVPT-LQMLvLQGEQVSFADWNRW----------PAS------- 5897
Cdd:PRK06187   240 ---RRFDpenLLDLIETERVTFFFA------------VPTiWQML-LKAPRAYFVDFSSLrlviyggaalPPAllrefke 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5898 ---VQTINGYGPTECS--ICCNTYS---GKQGFKSGIIGTSVASVSW-VVDPENhDRLAP-LGSIGELLVEGPILARGYL 5967
Cdd:PRK06187   304 kfgIDLVQGYGMTETSpvVSVLPPEdqlPGQWTKRRSAGRPLPGVEArIVDDDG-DELPPdGGEVGEIIVRGPWLMQGYW 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5968 NDIQKTAAVFIDDpaWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVE----HH--VRE 6041
Cdd:PRK06187   383 NRPEATAETIDGG--WL---------------HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEdalyGHpaVAE 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6042 ClpearqlAVeVILP---SGQKDHamlaAFVQLEEGtqnalldKEASGEDsmaqvvFLASVEEELAK-RLPEHM--VPTV 6115
Cdd:PRK06187   446 V-------AV-IGVPdekWGERPV----AVVVLKPG-------ATLDAKE------LRAFLRGRLAKfKLPKRIafVDEL 500
                          570       580
                   ....*....|....*....|..
gi 1820002560 6116 ffsllhfPTTTSGKTDRKRLRE 6137
Cdd:PRK06187   501 -------PRTSVGKILKRVLRE 515
AMP-binding pfam00501
AMP-binding enzyme;
2-174 1.24e-34

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 140.91  E-value: 1.24e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL------EPSHIPSLRILVMGGEQVNSADWDRW----PSSVqtINGYGPTECCIVCT--GYTSEQD 69
Cdd:pfam00501  251 KVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFrelfGGAL--VNGYGLTETTGVVTtpLPLDEDL 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   70 FTTGTIGTSIASVSW-VVDPkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINnpawlleghggyagrqGRLYK 148
Cdd:pfam00501  329 RSLGSVGRPLPGTEVkIVDD-ETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE----------------DGWYR 391
                          170       180
                   ....*....|....*....|....*.
gi 1820002560  149 TGDLVRYDADGNLVCLGRKDSQVKLR 174
Cdd:pfam00501  392 TGDLGRRDEDGYLEIVGRKKDQIKLG 417
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
4567-5026 1.79e-34

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 141.19  E-value: 1.79e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLASa 4646
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4647 qyatlwtslgrsvvivseastsqlpvvtktadpsvNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHT 4726
Cdd:cd05907     85 -----------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4727 RVLQF--ASYTFdACIAEIITTLLCCGCICVPSDSDR-RNNLA------------------KAINAMDVNWALltpsvAR 4785
Cdd:cd05907    130 RHLSFlpLAHVF-ERRAGLYVPLLAGARIYFASSAETlLDDLSevrptvflavprvwekvyAAIKVKAVPGLK-----RK 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4786 MLDPCVVQSLKILVLGGEQVnSADWDRWPKS--IQTINAYGPTECS--ICCTTysgKQGFKSGTIGTSIvsvswvvdPEN 4861
Cdd:cd05907    204 LFDLAVGGRLRFAASGGAPL-PAELLHFFRAlgIPVYEGYGLTETSavVTLNP---PGDNRIGTVGKPL--------PGV 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4862 HNRLAPlgsIGELLVEGPILARGYLNDMEKTEAAFIDDPaWLlegygghsgrqgrlyKTGDLVRYDADGNLVYLGR-KDS 4940
Cdd:cd05907    272 EVRIAD---DGEILVRGPNVMLGYYKNPEATAEALDADG-WL---------------HTGDLGEIDEDGFLHITGRkKDL 332
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4941 QVKLRGQRVELGEVEHHVREClteakqLAVEVIVPEGEgGYAMLAAFVQLGDDTYNTLVKEKAGGDSLTVQVVFLDRVEE 5020
Cdd:cd05907    333 IITSGGKNISPEPIENALKAS------PLISQAVVIGD-GRPFLVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRA 405

                   ....*.
gi 1820002560 5021 ELAKRV 5026
Cdd:cd05907    406 EIEAAV 411
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
1946-2443 2.55e-34

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 140.29  E-value: 2.55e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1946 PAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQT 2025
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2026 GAQVVVTSAqhsarwigtnhqvvtvsagsleqfstlvnpvdlpakpENAAYVMFTSGSTGTPKGVVLEHRAVVTSClghg 2105
Cdd:cd05919     82 EARLVVTSA-------------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFA---- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2106 QAFGvTNLLRaLQFTAYTFdvCIAEIITTLVHGGCICVP--------SDSERRDNLAKAITDMQVNWGYLTSS---VARL 2174
Cdd:cd05919    121 DAMA-REALG-LTPGDRVF--SSAKMFFGYGLGNSLWFPlavgasavLNPGWPTAERVLATLARFRPTVLYGVptfYANL 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2175 LDPCLVP-----SLKVLVLGGEQVNSTDWGKWPSS--VQTINGYGPTECC-VFCTGYTGiqgfqSGNIGTSIASVSW--- 2243
Cdd:cd05919    197 LDSCAGSpdalrSLRLCVSAGEALPRGLGERWMEHfgGPILDGIGATEVGhIFLSNRPG-----AWRLGSTGRPVPGyei 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2244 -VVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFiddpawllegypghegrQGRLYKTGDLVRYSSDGNLVC 2322
Cdd:cd05919    272 rLVDEE--GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-----------------NGGWYRTGDKFCRDADGWYTH 332
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2323 LGRKDSQVKVRGQRVELGEVEhhmrkclpeanQLAVEvVPPSGErdhAMLAAFIRLDDETRNSPLIIkyAEDNSTAQIVF 2402
Cdd:cd05919    333 AGRADDMLKVGGQWVSPVEVE-----------SLIIQ-HPAVAE---AAVVAVPESTGLSRLTAFVV--LKSPAAPQESL 395
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 2403 LTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLR 2443
Cdd:cd05919    396 ARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
5648-6135 3.33e-34

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 140.30  E-value: 3.33e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQ-VVVTS 5726
Cdd:cd17654     17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSyLLQNK 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5727 AQHSARWIGTNHQVVTvsagslgQLSTlvnpvglpaiPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNl 5806
Cdd:cd17654     97 ELDNAPLSFTPEHRHF-------NIRT----------DECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5807 SRVLQFAS-YTFDACMDEIITTLMYGGCI--------CVPSDSDRRNDLVKAISTMDVSCALLTPSVARLLEP---SSVP 5874
Cdd:cd17654    159 EDILFLTSpLTFDPSVVEIFLSLSSGATLlivptsvkVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKStvlSATS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5875 TLQMLVLQGEQ----VSFADWNRWPASVQTINGYGPTECSICCNTYSGKQGFKSGIIGTSV-ASVSWVVDPENHDrlapl 5949
Cdd:cd17654    239 SLRVLALGGEPfpslVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLlGTVIEVRDQNGSE----- 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5950 gSIGELLVEGpiLARGYlndiqktaavFIDDPawllegypgHPGRQGRLYKTGDLVRYDaNGNLVCLGRKDSQVKLRGQR 6029
Cdd:cd17654    314 -GTGQVFLGG--LNRVC----------ILDDE---------VTVPKGTMRATGDFVTVK-DGELFFLGRKDSQIKRRGKR 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6030 VELGEVEHHVRECLPEarqLAVEVILpsgqKDHAMLAAFVQLEEGTqnalldkeasgedsmaqvvflASVEEELAK-RLP 6108
Cdd:cd17654    371 INLDLIQQVIESCLGV---ESCAVTL----SDQQRLIAFIVGESSS---------------------SRIHKELQLtLLS 422
                          490       500
                   ....*....|....*....|....*..
gi 1820002560 6109 EHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:cd17654    423 SHAIPDTFVQIDKLPLTSHGKVDKSEL 449
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
1948-2395 3.37e-34

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 141.20  E-value: 3.37e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1948 ICAWDG-ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHPASRHEDI---FR 2023
Cdd:cd05911      3 IDADTGkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAA---NPIYTADELahqLK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2024 QTGAQVVVTSAQH------SARWIGTNHQVVTVS-----AGSLEQFSTLVN-------PVDLPAKPENAAYVMFTSGSTG 2085
Cdd:cd05911     80 ISKPKVIFTDPDGlekvkeAAKELGPKDKIIVLDdkpdgVLSIEDLLSPTLgeededlPPPLKDGKDDTAAILYSSGTTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2086 TPKGVVLEHRAVVTSCLGHGQAFGVTNLLRALQFTAYTFD--VCIAEIITTLVHGGCICVPS--DSErrdNLAKAITDMQ 2161
Cdd:cd05911    160 LPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiYGLFTTLASLLNGATVIIMPkfDSE---LFLDLIEKYK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2162 VNWGYLTSSVARLL--DPCLV----PSLKVLVLGG--------EQVNstdwgKWPSSVQTINGYGPTECCVFCTgYTGIQ 2227
Cdd:cd05911    237 ITFLYLVPPIAAALakSPLLDkydlSSLRVILSGGaplskelqELLA-----KRFPNATIKQGYGMTETGGILT-VNPDG 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2228 GFQSGNIGTSIASVSW-VVDPENHGRLAPlGSIGELLVEGPILARGYLNDVDKTQAAFIDDpAWLlegypghegrqgrly 2306
Cdd:cd05911    311 DDKPGSVGRLLPNVEAkIVDDDGKDSLGP-NEPGEICVRGPQVMKGYYNNPEATKETFDED-GWL--------------- 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2307 KTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVP--PSGERDhamlAAFIRL-DDETR 2383
Cdd:cd05911    374 HTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLE-HPGVADAAVIGIPdeVSGELP----RAYVVRkPGEKL 448
                          490
                   ....*....|..
gi 1820002560 2384 NSPLIIKYAEDN 2395
Cdd:cd05911    449 TEKEVKDYVAKK 460
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
867-1365 3.40e-34

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 140.12  E-value: 3.40e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  867 DASAVCAWDGELTYGELDELSSKLAAHLVQLG-VKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPAsrHEeif 945
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPL--AE--- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  946 kqigAQVVLTSSQHAMLfasserhqvtvskvstsqlptvvnfakspVDPgntAYIIFTSGTTGIPKGVVLQHRAVTTSCL 1025
Cdd:cd05941     76 ----LEYVITDSEPSLV-----------------------------LDP---ALILYTSGTTGRPKGVVLTHANLAANVR 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1026 GHGEAFGYTDHARVLQ------------------FASYT------FDACIAEII-----TTLLYGgcicVPSESDRrnnL 1076
Cdd:cd05941    120 ALVDAWRWTEDDVLLHvlplhhvhglvnallcplFAGASveflpkFDPKEVAISrlmpsITVFMG----VPTIYTR---L 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1077 AKAISTMDVNCALLTPSVARLLepsavpslkRLVLQG-----EQVsFADWNRWPGsvQTI-NGYGPTECSVC-CNTYSGK 1149
Cdd:cd05941    193 LQYYEAHFTDPQFARAAAAERL---------RLMVSGsaalpVPT-LEEWEAITG--HTLlERYGMTEIGMAlSNPLDGE 260
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1150 QgfKSGIIGTSVASLSWVVDAGNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpawlleGYeghagrrgrlY 1229
Cdd:cd05941    261 R--RPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDD------GW----------F 322
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1230 KTGDLVRCDADGNLVCLGR-KDSQVKVRGQRVELGEIEHHVREcLPEARQLAVeVILPS---GQKehalLAAFIQLDKGN 1305
Cdd:cd05941    323 KTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLA-HPGVSECAV-IGVPDpdwGER----VVAVVVLRAGA 396
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1306 HNALFEEkasgedsmaqvvfltgVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd05941    397 AALSLEE----------------LKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
3480-3890 6.56e-34

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 140.43  E-value: 6.56e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3480 ICAWDG-ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHPASRHEEI---FE 3555
Cdd:cd05911      3 IDADTGkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAA---NPIYTADELahqLK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3556 QTGAQVVVASAQY-------SARWTSSScHVVTVSKALS-----SQLPAVVDSTNTSVRP-------ENAAYIIFTSGST 3616
Cdd:cd05911     80 ISKPKVIFTDPDGlekvkeaAKELGPKD-KIIVLDDKPDgvlsiEDLLSPTLGEEDEDLPpplkdgkDDTAAILYSSGTT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3617 GVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFD--ACIAEIITTLLCGGCICVPSDSDRRNSLaKAISTMDV 3694
Cdd:cd05911    159 GLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiYGLFTTLASLLNGATVIIMPKFDSELFL-DLIEKYKI 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3695 NWAFLTPSVARLL------DPGLIPSLKILAIGG----EQSSSADWNRWPGSVQKiHVYGPTECCiFCTGYTTKQGFEPS 3764
Cdd:cd05911    238 TFLYLVPPIAAALakspllDKYDLSSLRVILSGGaplsKELQELLAKRFPNATIK-QGYGMTETG-GILTVNPDGDDKPG 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3765 TIGTSVASVSW-VVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpAWLlegypghpgrqgrlyKTGDL 3843
Cdd:cd05911    316 SVGRLLPNVEAkIVDDDGKDSLGP-NEPGEICVRGPQVMKGYYNNPEATKETFDED-GWL---------------HTGDI 378
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 3844 VQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAV 3890
Cdd:cd05911    379 GYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLE-HPGVADAAV 424
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
4566-5054 1.19e-33

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 140.35  E-value: 1.19e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4566 ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRhehifrQTgaqVVLAS 4645
Cdd:cd17647     20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR------QN---IYLGV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4646 AQYATLwtslgrsvvivseastsqlpVVTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDH 4725
Cdd:cd17647     91 AKPRGL--------------------IVIRAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4726 TRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNN--LAKAINAMDVNWALLTPSVARMLDPCVVQ---SLKILVL 4800
Cdd:cd17647    151 DKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPgrLAEWMAKYGATVTHLTPAMGQLLTAQATTpfpKLHHAFF 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4801 GGEQVNSADWDRW---PKSIQTINAYGPTECS-----ICCTTYSGKQGFKSGT-----IGTSIVSVSW-VVDPENHNRLA 4866
Cdd:cd17647    231 VGDILTKRDCLRLqtlAENVRIVNMYGTTETQravsyFEVPSRSSDPTFLKNLkdvmpAGRGMLNVQLlVVNRNDRTQIC 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4867 PLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpaWLLE----GY----GGHSGRQ------GRLYKTGDLVRYDADGNL 4932
Cdd:cd17647    311 GIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNN--WFVEpdhwNYldkdNNEPWRQfwlgprDRLYRTGDLGRYLPNGDC 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4933 VYLGRKDSQVKLRGQRVELGEVEHH------VRECLT-------EAKQLaVEVIVPEGEGGYAMLAAFVQLGDDTYNTLV 4999
Cdd:cd17647    389 ECCGRADDQVKIRGFRIELGEIDTHisqhplVRENITlvrrdkdEEPTL-VSYIVPRFDKPDDESFAQEDVPKEVSTDPI 467
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 5000 kekAGGdsLTVQVVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd17647    468 ---VKG--LIGYRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
4548-5056 1.49e-33

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 139.65  E-value: 1.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4548 AEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPA 4627
Cdd:PRK07656    12 ARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4628 SRHEHIFRQTGAQVVLASAQYATLWTSLG------RSVVIVSEASTSQLPVVTKTAD------------PSVNPGNAAYA 4689
Cdd:PRK07656    92 DEAAYILARGDAKALFVLGLFLGVDYSATtrlpalEHVVICETEEDDPHTEKMKTFTdflaagdpaeraPEVDPDDVADI 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4690 IFTSGSTGIPKGVVLEHKavvtSCLGHGQAF----GITDHTRVLQ----FASYTFDACiaeIITTLLCCGCIC-VPSDSd 4760
Cdd:PRK07656   172 LFTSGTTGRPKGAMLTHR----QLLSNAADWaeylGLTEGDRYLAanpfFHVFGYKAG---VNAPLMRGATILpLPVFD- 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4761 rrnnLAKAINAMDVNWALLTPSVARM---------LDPCVVQSLKILVLGGEQVNSADWDRWPKS--IQTI-NAYGPTEC 4828
Cdd:PRK07656   244 ----PDEVFRLIETERITVLPGPPTMynsllqhpdRSAEDLSSLRLAVTGAASMPVALLERFESElgVDIVlTGYGLSEA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4829 S--ICCTTYSGKQGFKSGTIGTSIVSVSWVVDPENHNRLaPLGSIGELLVEGPILARGYLNDMEKTEAAfIDDPAWLleg 4906
Cdd:PRK07656   320 SgvTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEV-PVGEVGELLVRGPNVMKGYYDDPEATAAA-IDADGWL--- 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4907 yggHsgrqgrlykTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhhvrECLTEAKQLA-VEVI-VPE---GEGGy 4981
Cdd:PRK07656   395 ---H---------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVE----EVLYEHPAVAeAAVIgVPDerlGEVG- 457
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 4982 amlAAFVQLGDdtyntlvkekagGDSLTVQVVfLDRVEEELAK-RVPEHMmltTFftLEAMPTTTSGKIDRKRLRE 5056
Cdd:PRK07656   458 ---KAYVVLKP------------GAELTEEEL-IAYCREHLAKyKVPRSI---EF--LDELPKNATGKVLKRALRE 512
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
4551-5051 3.37e-33

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 136.97  E-value: 3.37e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 4630
Cdd:cd17631      5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4631 EHIFRQTGAQVVLAsaqyatlwtslgrsvvivseastsqlpvvtktaDPsvnpgnaAYAIFTSGSTGIPKGVVLEHKAVV 4710
Cdd:cd17631     85 AYILADSGAKVLFD---------------------------------DL-------ALLMYTSGTTGRPKGAMLTHRNLL 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4711 TSCLGHGQAFGITDHTRVLQFAS-YTFDACIAEIITTLLCCGCICVPSDSDRRNNLAkAINAMDVNWALLTPSVARMLDP 4789
Cdd:cd17631    125 WNAVNALAALDLGPDDVLLVVAPlFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLD-LIERHRVTSFFLVPTMIQALLQ 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4790 CV------VQSLKILVLGG----EQVNSADWDRWPKSIQtinAYGPTECSICCTTYSGK-QGFKSGTIGTSI--VSVSwV 4856
Cdd:cd17631    204 HPrfattdLSSLRAVIYGGapmpERLLRALQARGVKFVQ---GYGMTETSPGVTFLSPEdHRRKLGSAGRPVffVEVR-I 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4857 VDPENhnRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpaWLlegygghsgrqgrlyKTGDLVRYDADGNLVYLG 4936
Cdd:cd17631    280 VDPDG--REVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG--WF---------------HTGDLGRLDEDGYLYIVD 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4937 RKDSQVKLRGQRVELGEVEH----H--VREClteakqlAVeVIVPEGEGGYAMLAAFVqlgddtyntlvkeKAGGDSLTV 5010
Cdd:cd17631    341 RKKDMIISGGENVYPAEVEDvlyeHpaVAEV-------AV-IGVPDEKWGEAVVAVVV-------------PRPGAELDE 399
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 5011 QVVFlDRVEEELAK-RVPEHmmlttFFTLEAMPTTTSGKIDR 5051
Cdd:cd17631    400 DELI-AHCRERLARyKIPKS-----VEFVDALPRNATGKILK 435
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
5648-6107 3.64e-33

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 137.34  E-value: 3.64e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSA 5727
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5728 qhsarwigtnhqvvtvsagsLGQLSTlvnpvglpaipenavyIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLS 5807
Cdd:cd05907     86 --------------------PDDLAT----------------IIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5808 RVLQF--ASYTFDACMDEIItTLMYGGCICVPSDSDRrndLVKAISTmdVSCALLTpSVARLLEP-------SSVPTLQM 5878
Cdd:cd05907    130 RHLSFlpLAHVFERRAGLYV-PLLAGARIYFASSAET---LLDDLSE--VRPTVFL-AVPRVWEKvyaaikvKAVPGLKR 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5879 LVLQ---GEQVSFA---------DWNRWPAS--VQTINGYGPTECS--ICCNTysgKQGFKSGiigtsvaSVSWVVDPeN 5942
Cdd:cd05907    203 KLFDlavGGRLRFAasggaplpaELLHFFRAlgIPVYEGYGLTETSavVTLNP---PGDNRIG-------TVGKPLPG-V 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5943 HDRLAPlgsIGELLVEGPILARGYLNDIQKTAAVFIDDPaWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGR-KDS 6021
Cdd:cd05907    272 EVRIAD---DGEILVRGPNVMLGYYKNPEATAEALDADG-WL---------------HTGDLGEIDEDGFLHITGRkKDL 332
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6022 QVKLRGQRVELGEVEHHVREClpearqLAVEVILPSGQKDhAMLAAFVQLEEGTQNALLDKEASGEDSMAQVVFLASVEE 6101
Cdd:cd05907    333 IITSGGKNISPEPIENALKAS------PLISQAVVIGDGR-PFLVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRA 405

                   ....*.
gi 1820002560 6102 ELAKRL 6107
Cdd:cd05907    406 EIEAAV 411
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
6853-7135 5.87e-33

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 142.90  E-value: 5.87e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6853 GSIGELLVEGPILARGYLNDADKTAAAFVNDpaWLVE-----------GHGKHP---GRRGRLYKTGDLVYYNKDGNLVY 6918
Cdd:TIGR03443  619 GEVGEIYVRAGGLAEGYLGLPELNAEKFVNN--WFVDpshwidldkenNKPEREfwlGPRDRLYRTGDLGRYLPDGNVEC 696
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6919 IGRKDGQVKVRGQRVELGEIENRL-RECMPRATQMAVEvispaGAAEQAKTMVVAFLQLNDEARDALLGGNVPNDDNlSA 6997
Cdd:TIGR03443  697 CGRADDQVKIRGFRIELGEIDTHLsQHPLVRENVTLVR-----RDKDEEPTLVSYIVPQDKSDELEEFKSEVDDEES-SD 770
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6998 QVV--------FPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLreigaSF--TAQQLAEMRTSSQGPKRQP 7067
Cdd:TIGR03443  771 PVVkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL-----PFpdTAQLAAVAKNRSASAADEE 845
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 7068 STEAERTMQQLWARMLKVKADSIGLDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADVFRHPRLVDLA 7135
Cdd:TIGR03443  846 FTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKlNVELPLGLIFKSPTIKGFA 914
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
3486-3974 6.68e-33

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 138.03  E-value: 6.68e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3486 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRheeifeqtgaQVVVAS 3565
Cdd:cd17647     20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR----------QNIYLG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3566 aqysarwtssschvVTVSKALssqlpAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNL 3645
Cdd:cd17647     90 --------------VAKPRGL-----IVIRAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3646 SRVLQFASYTFDACIAEIITTLLCGGCICVPSDSD--RRNSLAKAISTMDVNWAFLTPSVARLLDPGL---IPSLKILAI 3720
Cdd:cd17647    151 DKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDigTPGRLAEWMAKYGATVTHLTPAMGQLLTAQAttpFPKLHHAFF 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3721 GGEQSSSADWNRWPG---SVQKIHVYGPTE----CCIF-CTGYTTKQGFEPST-----IGTSVASVSW-VVDPENHNRLA 3786
Cdd:cd17647    231 VGDILTKRDCLRLQTlaeNVRIVNMYGTTEtqraVSYFeVPSRSSDPTFLKNLkdvmpAGRGMLNVQLlVVNRNDRTQIC 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3787 PLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLLEgyPGH----------PGRQ------GRLYKTGDLVQYNADG 3850
Cdd:cd17647    311 GIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNN--WFVE--PDHwnyldkdnnePWRQfwlgprDRLYRTGDLGRYLPNG 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3851 NLVYLGRKDSQVKVRGQRVELGEVEHH------VRECLPEARQLA------VEVILPSGQKDHAMLAAFVQLEEGTQNal 3918
Cdd:cd17647    387 DCECCGRADDQVKIRGFRIELGEIDTHisqhplVRENITLVRRDKdeeptlVSYIVPRFDKPDDESFAQEDVPKEVST-- 464
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 3919 lDKEAGGedSMAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:cd17647    465 -DPIVKG--LIGYRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
5641-6051 1.19e-32

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 136.57  E-value: 1.19e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5641 ICAWDG-ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTG 5719
Cdd:cd05911      3 IDADTGkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5720 AQVVVTSAQH------SARWIGTNHQVVTVS-----AGSLGQLSTLVNPVGLPAIPE-------NAVYIMFTSGSTGIPK 5781
Cdd:cd05911     83 PKVIFTDPDGlekvkeAAKELGPKDKIIVLDdkpdgVLSIEDLLSPTLGEEDEDLPPplkdgkdDTAAILYSSGTTGLPK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5782 GVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFD--ACMDEIITTLMYGGCICVPS--DSDrrnDLVKAISTMDVSC 5857
Cdd:cd05911    163 GVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiYGLFTTLASLLNGATVIIMPkfDSE---LFLDLIEKYKITF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5858 ALLTPSVARLL------EPSSVPTLQMLV-----LQGEQVSF--ADWNRWPAsvqtINGYGPTECS--ICCNTYSGKqgf 5922
Cdd:cd05911    240 LYLVPPIAAALakspllDKYDLSSLRVILsggapLSKELQELlaKRFPNATI----KQGYGMTETGgiLTVNPDGDD--- 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5923 KSGIIGTSVASVSW-VVDPENHDRLAPlGSIGELLVEGPILARGYLNDIQKTAAVFIDDpAWLlegypghpgrqgrlyKT 6001
Cdd:cd05911    313 KPGSVGRLLPNVEAkIVDDDGKDSLGP-NEPGEICVRGPQVMKGYYNNPEATKETFDED-GWL---------------HT 375
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6002 GDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAV 6051
Cdd:cd05911    376 GDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLE-HPGVADAAV 424
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
1954-2442 1.30e-32

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 137.26  E-value: 1.30e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1954 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRhedifrqtgaQVVVTS 2033
Cdd:cd17647     20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR----------QNIYLG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2034 AQHSARWIGtnhqvvtvsagsLEQFSTLVNPVDLPAkpenaayVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNL 2113
Cdd:cd17647     90 VAKPRGLIV------------IRAAGVVVGPDSNPT-------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2114 LRALQFTAYTFDVCIAEIITTLVHGGCICVPS--DSERRDNLAKAITDMQVNWGYLTSSVARLLDPCLV---PSLKVLVL 2188
Cdd:cd17647    151 DKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTqdDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATtpfPKLHHAFF 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2189 GGEQVNSTDWGKWPS---SVQTINGYGPTE----CCVF-CTGYTGIQGFQSG-----NIGTSIASVSW-VVDPENHGRLA 2254
Cdd:cd17647    231 VGDILTKRDCLRLQTlaeNVRIVNMYGTTEtqraVSYFeVPSRSSDPTFLKNlkdvmPAGRGMLNVQLlVVNRNDRTQIC 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2255 PLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpaWLLEgyPGH----------------EGRQGRLYKTGDLVRYSSDG 2318
Cdd:cd17647    311 GIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNN--WFVE--PDHwnyldkdnnepwrqfwLGPRDRLYRTGDLGRYLPNG 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2319 NLVCLGRKDSQVKVRGQRVELGEVEHHM-------------RKCLPEANQLAVEVVpPSGERDHAMLAAFIRLDDETRNS 2385
Cdd:cd17647    387 DCECCGRADDQVKIRGFRIELGEIDTHIsqhplvrenitlvRRDKDEEPTLVSYIV-PRFDKPDDESFAQEDVPKEVSTD 465
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2386 PLI---IKYAEdnstaqivFLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd17647    466 PIVkglIGYRK--------LIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
854-1302 1.45e-32

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 138.31  E-value: 1.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDG----ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAF 929
Cdd:COG1022     13 LPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  930 VPLDPGHPASRHEEIFKQIGAQVVLTSSQ-HAMLFASSE------RHQVTVSKVSTSQLPTVVNFA-------------- 988
Cdd:COG1022     93 VPIYPTSSAEEVAYILNDSGAKVLFVEDQeQLDKLLEVRdelpslRHIVVLDPRGLRDDPRLLSLDellalgrevadpae 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  989 ----KSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQF--ASYTFDACIAeiITTLLYGG 1062
Cdd:COG1022    173 learRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlpLAHVFERTVS--YYALAAGA 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1063 CICVPSESDrrnNLAKAISTmdVNCALLTpSVARLLEP---------SAVPSLKR---------------LVLQGEQVSF 1118
Cdd:COG1022    251 TVAFAESPD---TLAEDLRE--VKPTFML-AVPRVWEKvyagiqakaEEAGGLKRklfrwalavgrryarARLAGKSPSL 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1119 ADWNRWP-----------------------GS---------------VQTINGYGPTECS--VCCNTYsgkQGFKSG--- 1155
Cdd:COG1022    325 LLRLKHAladklvfsklrealggrlrfavsGGaalgpelarffralgIPVLEGYGLTETSpvITVNRP---GDNRIGtvg 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1156 --IIGTSVaslswvvdagnhnRLAPlgsIGELLVEGPILARGYLNDIDKTEAAFIDDpAWLlegyeghagrrgrlyKTGD 1233
Cdd:COG1022    402 ppLPGVEV-------------KIAE---DGEILVRGPNVMKGYYKNPEATAEAFDAD-GWL---------------HTGD 449
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1234 LVRCDADGNLVCLGRKDSQVKVR-GQRVELGEIEHHVREClPEARQlAVeVIlpsGQKEHAlLAAFIQLD 1302
Cdd:COG1022    450 IGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKAS-PLIEQ-AV-VV---GDGRPF-LAALIVPD 512
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
7626-8114 2.70e-32

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 135.42  E-value: 2.70e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7626 ICAWDG-ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHPASRHEEI---FE 7701
Cdd:cd05911      3 IDADTGkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAA---NPIYTADELahqLK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7702 QTGAQVVVASAQY-------SARWTSSScHVVTVSKALS-----SQLPAVVDSTNTSVRP-------ENAAYIIFTSGST 7762
Cdd:cd05911     80 ISKPKVIFTDPDGlekvkeaAKELGPKD-KIIVLDDKPDgvlsiEDLLSPTLGEEDEDLPpplkdgkDDTAAILYSSGTT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7763 GVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFD--ACIAEIITTLLCGGCICVPSDSDRRNSLaKAISTMDV 7840
Cdd:cd05911    159 GLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiYGLFTTLASLLNGATVIIMPKFDSELFL-DLIEKYKI 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7841 NWAFLTPSVARLL------DPGLIPSLKILAIGG----EQSSSADWNRWPGSVQKiHVYGPTECCiFCTGYTTKQGFEPS 7910
Cdd:cd05911    238 TFLYLVPPIAAALakspllDKYDLSSLRVILSGGaplsKELQELLAKRFPNATIK-QGYGMTETG-GILTVNPDGDDKPG 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7911 TIGTSVASVSW-VVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpAWLlegypghpgrqgrlyKTGDL 7989
Cdd:cd05911    316 SVGRLLPNVEAkIVDDDGKDSLGP-NEPGEICVRGPQVMKGYYNNPEATKETFDED-GWL---------------HTGDI 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7990 VQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKNHAMLAVFVqlgkgthiahleeKA 8069
Cdd:cd05911    379 GYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLE-HPGVADAAV-IGIPDEVSGELPRAYVV-------------RK 443
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 8070 GGEDSmaqvvfltgTEEEL----AKRLP--KHMVPTVFFaLLHFPMTTSGK 8114
Cdd:cd05911    444 PGEKL---------TEKEVkdyvAKKVAsyKQLRGGVVF-VDEIPKSASGK 484
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
5639-6136 7.09e-32

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 133.36  E-value: 7.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5639 PAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHT 5718
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5719 GAQVVVTSAqhsarwigtnhqvvtvsagslgqlstlvnpvglpaipENAVYIMFTSGSTGIPKGVVLEHRAVVTSC--WG 5796
Cdd:cd05919     82 EARLVVTSA-------------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdaMA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5797 RgRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRNDLVKAIStmdvscALLTPSV--------ARLL 5868
Cdd:cd05919    125 R-EALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATL------ARFRPTVlygvptfyANLL 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5869 -----EPSSVPTLQMLVLQGEQVSFADWNRWPAS--VQTINGYGPTEC--SICCNTYSGKQgfksgiIGTSVASVSW--- 5936
Cdd:cd05919    198 dscagSPDALRSLRLCVSAGEALPRGLGERWMEHfgGPILDGIGATEVghIFLSNRPGAWR------LGSTGRPVPGyei 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5937 -VVDPENHDrlAPLGSIGELLVEGPILARGYLNDIQKTAAVFiddpawllegypghpgrQGRLYKTGDLVRYDANGNLVC 6015
Cdd:cd05919    272 rLVDEEGHT--IPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-----------------NGGWYRTGDKFCRDADGWYTH 332
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6016 LGRKDSQVKLRGQRVELGEVEHHVreCLPEARQLAVEVILPSgQKDHAMLAAFVQLEEGTQNalldKEASGEDSMAQvvf 6095
Cdd:cd05919    333 AGRADDMLKVGGQWVSPVEVESLI--IQHPAVAEAAVVAVPE-STGLSRLTAFVVLKSPAAP----QESLARDIHRH--- 402
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 6096 lasveeeLAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:cd05919    403 -------LLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
7632-8120 7.21e-32

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 134.95  E-value: 7.21e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7632 ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRheeifeqtgaQVVVAS 7711
Cdd:cd17647     20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR----------QNIYLG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7712 aqysarwtssschvVTVSKALssqlpAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNL 7791
Cdd:cd17647     90 --------------VAKPRGL-----IVIRAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7792 SRVLQFASYTFDACIAEIITTLLCGGCICVPSDSD--RRNSLAKAISTMDVNWAFLTPSVARLLDPGL---IPSLKILAI 7866
Cdd:cd17647    151 DKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDigTPGRLAEWMAKYGATVTHLTPAMGQLLTAQAttpFPKLHHAFF 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7867 GGEQSSSADWNRWPG---SVQKIHVYGPTE----CCIF-CTGYTTKQGFEPST-----IGTSVASVSW-VVDPENHNRLA 7932
Cdd:cd17647    231 VGDILTKRDCLRLQTlaeNVRIVNMYGTTEtqraVSYFeVPSRSSDPTFLKNLkdvmpAGRGMLNVQLlVVNRNDRTQIC 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7933 PLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLLEgyPGH----------PGRQ------GRLYKTGDLVQYNADG 7996
Cdd:cd17647    311 GIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNN--WFVE--PDHwnyldkdnnePWRQfwlgprDRLYRTGDLGRYLPNG 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7997 NLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQlavEVILPSGQKNHA------MLAVFVQLGKGTHIAHLEEKAG 8070
Cdd:cd17647    387 DCECCGRADDQVKIRGFRIELGEIDTHISQ-HPLVRE---NITLVRRDKDEEptlvsyIVPRFDKPDDESFAQEDVPKEV 462
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 8071 GEDSMAQVV-----FLTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRL 8120
Cdd:cd17647    463 STDPIVKGLigyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
9-283 8.84e-32

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 134.25  E-value: 8.84e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    9 TPSVAR--LLEPS----HIPSLRILVMGGE----QVNSADWDRWPSSVqTINGYGPTECCIVCTGY--TSE--QDFTTGT 74
Cdd:PRK04813   241 TPSFADmcLLDPSfneeHLPNLTHFLFCGEelphKTAKKLLERFPSAT-IYNTYGPTEATVAVTSIeiTDEmlDQYKRLP 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   75 IGTSIASVSWVVDPKDhGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINnpawlLEGHggyagrqgRLYKTGDLVR 154
Cdd:PRK04813   320 IGYAKPDSPLLIIDEE-GTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT-----FDGQ--------PAYHTGDAGY 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  155 YDaDGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClpeaKQLAVEVVLPLgQKNHAT--LAAFIQLDKGTHNALLKekv 232
Cdd:PRK04813   386 LE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQS----SYVESAVVVPY-NKDHKVqyLIAYVVPKEEDFEREFE--- 456
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  233 ggddsiarvvFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:PRK04813   457 ----------LTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
851-1365 1.21e-31

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 133.61  E-value: 1.21e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  851 DRCIHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVV----PLCFEksmwTVVAMLAVLKAG 926
Cdd:cd05920     14 DEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVvvqlPNVAE----FVVLFFALLRLG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  927 GAFVPLDPGHpasRHEEI---FKQIGAQVVLTSSQHAMLFasserHQVTVSKVSTSQlPTVvnfakspvdpgntAYIIFT 1003
Cdd:cd05920     90 AVPVLALPSH---RRSELsafCAHAEAVAYIVPDRHAGFD-----HRALARELAESI-PEV-------------ALFLLS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1004 SGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQF--ASYTFDACIAEIITTLLYGGCIcVPSESDRRNNLAKAIS 1081
Cdd:cd05920    148 GGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRV-VLAPDPSPDAAFPLIE 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1082 TMDVNCALLTPSVARLL------EPSAVPSLKRLVLQGEQVSFADWNRWPG----SVQTIngYGPTECSVCcntYSGKQG 1151
Cdd:cd05920    227 REGVTVTALVPALVSLWldaaasRRADLSSLRLLQVGGARLSPALARRVPPvlgcTLQQV--FGMAEGLLN---YTRLDD 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1152 FKSGIIGTSVASLS-----WVVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpawlleGYeghagrrg 1226
Cdd:cd05920    302 PDEVIIHTQGRPMSpddeiRVVDE--EGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPD------GF-------- 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1227 rlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQLAVeVILPsgqkeHALLaafiqldkgnh 1306
Cdd:cd05920    366 --YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR-HPAVHDAAV-VAMP-----DELL----------- 425
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 1307 nalfeekasGEDSMAQVVF------LTGVEEELAKR-LPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd05920    426 ---------GERSCAFVVLrdpppsAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
862-1362 1.39e-31

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 132.35  E-value: 1.39e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  862 ARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRH 941
Cdd:cd17631      5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  942 EEIFKQIGAQVVLTssqhamlfasserhqvtvskvstsqlptvvnfakspvDPgntAYIIFTSGTTGIPKGVVLQHRAVT 1021
Cdd:cd17631     85 AYILADSGAKVLFD-------------------------------------DL---ALLMYTSGTTGRPKGAMLTHRNLL 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1022 TSCLGHGEAFGYTDHARVLQFAS-YTFDACIAEIITTLLYGGCICVPSESDRRNNLAkAISTMDVNCALLTPSVARLL-- 1098
Cdd:cd17631    125 WNAVNALAALDLGPDDVLLVVAPlFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLD-LIERHRVTSFFLVPTMIQALlq 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1099 EPSA----VPSLKRLVLQGEQVSFADWNRWPG-SVQTINGYGPTECS--VCCNTYSGKQGfKSGIIGTSVASLSW-VVDA 1170
Cdd:cd17631    204 HPRFattdLSSLRAVIYGGAPMPERLLRALQArGVKFVQGYGMTETSpgVTFLSPEDHRR-KLGSAGRPVFFVEVrIVDP 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1171 gnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpaWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKD 1250
Cdd:cd17631    283 --DGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG--WF---------------HTGDLGRLDEDGYLYIVDRKK 343
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1251 SQVKVRGQRVELGEIEHHVREcLPEARQLAVeVILPSGQkehallaafiqldkgnhnalfeekaSGEDSMAQVVFLTGV- 1329
Cdd:cd17631    344 DMIISGGENVYPAEVEDVLYE-HPAVAEVAV-IGVPDEK-------------------------WGEAVVAVVVPRPGAe 396
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1820002560 1330 --EEELAKRLPEHM----VPTILFTVKAMPITTSGKIDR 1362
Cdd:cd17631    397 ldEDELIAHCRERLarykIPKSVEFVDALPRNATGKILK 435
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1932-2444 1.44e-31

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 134.12  E-value: 1.44e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1932 HDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAGGAFV 2007
Cdd:COG1021     28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVvvqlPNVAE----FVIVFFALFRAGAIPV 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2008 PLDPDHPASRHEDIFRQTGAQVVVTSAQHS------------ARWIGTNHQVVTVSAGSLEQFSTLVN-PVDLPA---KP 2071
Cdd:COG1021    104 FALPAHRRAEISHFAEQSEAVAYIIPDRHRgfdyralarelqAEVPSLRHVLVVGDAGEFTSLDALLAaPADLSEprpDP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2072 ENAAYVMFTSGSTGTPKGVVLEH-------RAVVTSC-LGHGqafgvTNLLRALQFtAYTFDVCIAEIITTLVHGGCIcV 2143
Cdd:COG1021    184 DDVAFFQLSGGTTGLPKLIPRTHddylysvRASAEICgLDAD-----TVYLAALPA-AHNFPLSSPGVLGVLYAGGTV-V 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2144 PSDSERRDNLAKAITDMQVNwgyLTSSV---------ARLLDPCLVPSLKVLVLGGeqvnstdwGKWPSSV--QTINGYG 2212
Cdd:COG1021    257 LAPDPSPDTAFPLIERERVT---VTALVpplallwldAAERSRYDLSSLRVLQVGG--------AKLSPELarRVRPALG 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2213 PTECCVFCTG-----YTGI----------QgfqsgniGTSIAS---VsWVVDPEnhGRLAPLGSIGELLVEGPILARGYL 2274
Cdd:COG1021    326 CTLQQVFGMAeglvnYTRLddpeevilttQ-------GRPISPddeV-RIVDED--GNPVPPGEVGELLTRGPYTIRGYY 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2275 NDVDKTQAAFIDDpawlleGYpghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEAN 2354
Cdd:COG1021    396 RAPEHNARAFTPD------GF----------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLA-HPAVH 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2355 QLAVEVVPPS--GERDHamlaAFIRLDDETRNSPLIIKYaednstaqivfltgieeeLSER-LPQHMVPTVFFALVHFPT 2431
Cdd:COG1021    459 DAAVVAMPDEylGERSC----AFVVPRGEPLTLAELRRF------------------LRERgLAAFKLPDRLEFVDALPL 516
                          570
                   ....*....|...
gi 1820002560 2432 TTSGKTDRKRLRE 2444
Cdd:COG1021    517 TAVGKIDKKALRA 529
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
1955-2414 1.55e-31

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 132.33  E-value: 1.55e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSa 2034
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2035 qhsarwigtnhqvvtvsagsleqfstlvNPVDLpakpenaAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLL 2114
Cdd:cd05907     85 ----------------------------DPDDL-------ATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2115 RALQF--TAYTFDVcIAEIITTLVHGGCICVPSDSER-RDNLA------------------KAITDMQVNWGyltssVAR 2173
Cdd:cd05907    130 RHLSFlpLAHVFER-RAGLYVPLLAGARIYFASSAETlLDDLSevrptvflavprvwekvyAAIKVKAVPGL-----KRK 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2174 LLDPCLVPSLKVLVLGGEQVnSTDWGKWPSS--VQTINGYGPTECCVFCTgytgIQGFQSGNIGTsiasVSWVVDPeNHG 2251
Cdd:cd05907    204 LFDLAVGGRLRFAASGGAPL-PAELLHFFRAlgIPVYEGYGLTETSAVVT----LNPPGDNRIGT----VGKPLPG-VEV 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2252 RLAPlgsIGELLVEGPILARGYLNDVDKTQAAFIDDPaWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLGR-KDSQV 2330
Cdd:cd05907    274 RIAD---DGEILVRGPNVMLGYYKNPEATAEALDADG-WL---------------HTGDLGEIDEDGFLHITGRkKDLII 334
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2331 KVRGQRVELGEVEHHMRKCLPEANQLAVevvppsGERDhAMLAAFIRLDDETRNSPLIIKYAEDNSTAQIVFLTGIEEEL 2410
Cdd:cd05907    335 TSGGKNISPEPIENALKASPLISQAVVI------GDGR-PFLVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRAEI 407

                   ....
gi 1820002560 2411 SERL 2414
Cdd:cd05907    408 EAAV 411
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
4545-4961 1.67e-31

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 134.84  E-value: 1.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4545 DQFAEQARARPDTPAICAWDG----ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVP 4620
Cdd:COG1022     15 DLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4621 LDPDHPASRHEHIFRQTGAQVVLAS--AQYATLWTSLG-----RSVVIVSEASTSQLPVVT----------KTADP---- 4679
Cdd:COG1022     95 IYPTSSAEEVAYILNDSGAKVLFVEdqEQLDKLLEVRDelpslRHIVVLDPRGLRDDPRLLsldellalgrEVADPaele 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4680 ----SVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQF--ASYTFDACIAeiiTTLLCCGC- 4752
Cdd:COG1022    175 arraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlpLAHVFERTVS---YYALAAGAt 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4753 ICVPSDSDR-RNNL-------------------AKAINAMD---------VNWALltpSVARMLDPCVVQSLKI------ 4797
Cdd:COG1022    252 VAFAESPDTlAEDLrevkptfmlavprvwekvyAGIQAKAEeagglkrklFRWAL---AVGRRYARARLAGKSPslllrl 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4798 -------LVLG------GEQVN---------SADWDRWPKS--IQTINAYGPTECS--ICCTTYsgkQGFKSGTIGTSIV 4851
Cdd:COG1022    329 khaladkLVFSklrealGGRLRfavsggaalGPELARFFRAlgIPVLEGYGLTETSpvITVNRP---GDNRIGTVGPPLP 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4852 SVSWVVDPEnhnrlaplgsiGELLVEGPILARGYLNDMEKTEAAFIDDpAWLlegygghsgrqgrlyKTGDLVRYDADGN 4931
Cdd:COG1022    406 GVEVKIAED-----------GEILVRGPNVMKGYYKNPEATAEAFDAD-GWL---------------HTGDIGELDEDGF 458
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1820002560 4932 LVYLGRKDSQVKLR-GQRVELGEVEHHVREC 4961
Cdd:COG1022    459 LRITGRKKDLIVTSgGKNVAPQPIENALKAS 489
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
4556-5056 1.81e-31

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 132.03  E-value: 1.81e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4556 DTPAICAWDGELTYGELDTLSSKLASHLVQLG-VKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIF 4634
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4635 RQTGAQVVLasaqyatlwtslgrsvvivseastsqlpvvtktadpsvnpgNAAYAIFTSGSTGIPKGVVLEHKAVVTSCL 4714
Cdd:cd05941     81 TDSEPSLVL-----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVR 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4715 GHGQAFGITDHTRVLQ------------------FASYT------FDACIAEII-----TTLLccgcICVPSDSDRrnnL 4765
Cdd:cd05941    120 ALVDAWRWTEDDVLLHvlplhhvhglvnallcplFAGASveflpkFDPKEVAISrlmpsITVF----MGVPTIYTR---L 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4766 AKAINAMDVNWALLTPSVARmldpcvvqSLKILVLGGEQVNSADWDRWpKSI--QTI-NAYGPTECSICCTT-YSGKQgf 4841
Cdd:cd05941    193 LQYYEAHFTDPQFARAAAAE--------RLRLMVSGSAALPVPTLEEW-EAItgHTLlERYGMTEIGMALSNpLDGER-- 261
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4842 KSGTIGTSIVSVSWVVDPENHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpawlleGYgghsgrqgrlYKTG 4921
Cdd:cd05941    262 RPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDD------GW----------FKTG 325
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4922 DLVRYDADGNLVYLGR-KDSQVKLRGQRVELGEVEHH------VREClteakqlAVeVIVPEGEGGYAMLAAfvqlgddt 4994
Cdd:cd05941    326 DLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVllahpgVSEC-------AV-IGVPDPDWGERVVAV-------- 389
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 4995 yntlVKEKAGGDSLTVQvVFLDRVEEELAK-RVPEHMMLttfftLEAMPTTTSGKIDRKRLRE 5056
Cdd:cd05941    390 ----VVLRAGAAALSLE-ELKEWAKQRLAPyKRPRRLIL-----VDELPRNAMGKVNKKELRK 442
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
4544-5056 3.39e-31

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 132.96  E-value: 3.39e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4544 HDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMV----PLCFEksmwTVVAMLAVLKAGGAFV 4619
Cdd:COG1021     28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVvvqlPNVAE----FVIVFFALFRAGAIPV 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4620 PLDPDHPASRHEHIFRQTGAQVVLASAQ-----YATLWTSLG------RSVVIVSEAS--TSQLPVVTKTAD---PSVNP 4683
Cdd:COG1021    104 FALPAHRRAEISHFAEQSEAVAYIIPDRhrgfdYRALARELQaevpslRHVLVVGDAGefTSLDALLAAPADlsePRPDP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4684 GNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQF--ASYTFDACIAEIITTLLCCGCIcVPSDSDR 4761
Cdd:COG1021    184 DDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAAlpAAHNFPLSSPGVLGVLYAGGTV-VLAPDPS 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4762 RNNLAKAINAMDVNWALLTPSVA-RMLDPCV-----VQSLKILVLGGEQVNSADWDRWPKSI--QTINAYGPTECSICCT 4833
Cdd:COG1021    263 PDTAFPLIERERVTVTALVPPLAlLWLDAAErsrydLSSLRVLQVGGAKLSPELARRVRPALgcTLQQVFGMAEGLVNYT 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4834 --------TYSgkqgfksgTIGTSIvsvS-----WVVDPEnhNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDp 4900
Cdd:COG1021    343 rlddpeevILT--------TQGRPI---SpddevRIVDED--GNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPD- 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4901 awlleGYgghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVreclteakqLAVEVIVPegegg 4980
Cdd:COG1021    409 -----GF----------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLL---------LAHPAVHD----- 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4981 yamlAAFVQLGDDtyntLVKEKAG------GDSLTVQVV--FLDrvEEELAK-RVPEHMMLttfftLEAMPTTTSGKIDR 5051
Cdd:COG1021    460 ----AAVVAMPDE----YLGERSCafvvprGEPLTLAELrrFLR--ERGLAAfKLPDRLEF-----VDALPLTAVGKIDK 524

                   ....*
gi 1820002560 5052 KRLRE 5056
Cdd:COG1021    525 KALRA 529
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
3478-3975 3.88e-31

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 131.04  E-value: 3.88e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3478 PAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQT 3557
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3558 GAQVVVASAqysarwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHG 3637
Cdd:cd05919     82 EARLVVTSA-------------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3638 R-AFGITNLSRVLQFASYTFDACIA-EIITTLLCGG-CICVPSDSDRRNSLAKAistmdvnwAFLTPSV--------ARL 3706
Cdd:cd05919    125 ReALGLTPGDRVFSSAKMFFGYGLGnSLWFPLAVGAsAVLNPGWPTAERVLATL--------ARFRPTVlygvptfyANL 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3707 LDPGLIP-----SLKILAIGGEQSSSADWNRWP--GSVQKIHVYGPTEccIFCTGYTTKQGfePSTIGTSVASVSW---- 3775
Cdd:cd05919    197 LDSCAGSpdalrSLRLCVSAGEALPRGLGERWMehFGGPILDGIGATE--VGHIFLSNRPG--AWRLGSTGRPVPGyeir 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3776 VVDPENHNrlAPLGSMGELLMEGPILARGYLNDVDKTEAAFiddpawllegypghpgrQGRLYKTGDLVQYNADGNLVYL 3855
Cdd:cd05919    273 LVDEEGHT--IPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-----------------NGGWYRTGDKFCRDADGWYTHA 333
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3856 GRKDSQVKVRGQRVELGEVEHHVreCLPEARQLAVEVILPSgQKDHAMLAAFVQLEEGTQNalldkeaggedsmaQVVFL 3935
Cdd:cd05919    334 GRADDMLKVGGQWVSPVEVESLI--IQHPAVAEAAVVAVPE-STGLSRLTAFVVLKSPAAP--------------QESLA 396
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 3936 ASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd05919    397 RDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
3476-3976 5.12e-31

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 130.87  E-value: 5.12e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3476 HAPAICAWDGELTYGELDALSSKLASHLVQLG-VNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 3554
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsvrpeNAAYIIFTSGSTGVPKGVVLEHRAVATSCL 3634
Cdd:cd05941     81 TDSEPSLVL-----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVR 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3635 GHGRAFGITNLSRVLQ------------------FASYT------FDACIAEII-----TTLLCGgcicVPSDSDRrnsL 3685
Cdd:cd05941    120 ALVDAWRWTEDDVLLHvlplhhvhglvnallcplFAGASveflpkFDPKEVAISrlmpsITVFMG----VPTIYTR---L 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3686 AKAISTMDVNWAFLTPSVARLLDpglipslkiLAIGGeqsSSA----DWNRWpgsvQKI--HV----YGPTEccifcTGY 3755
Cdd:cd05941    193 LQYYEAHFTDPQFARAAAAERLR---------LMVSG---SAAlpvpTLEEW----EAItgHTllerYGMTE-----IGM 251
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3756 TTKQGFE----PSTIGTSVASVSWVVDPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawlleGYpghp 3831
Cdd:cd05941    252 ALSNPLDgerrPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDD------GW---- 321
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3832 grqgrlYKTGDLVQYNADGNLVYLGR-KDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPS---GQKdhamLAAF 3907
Cdd:cd05941    322 ------FKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLA-HPGVSECAV-IGVPDpdwGER----VVAV 389
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 3908 VQLEEGTQNalldkeaggedsmaqvVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:cd05941    390 VVLRAGAAA----------------LSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
3487-3946 6.99e-31

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 130.41  E-value: 6.99e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASA 3566
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3567 qysarwtssschvvtvskalssqlpavvdstntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLS 3646
Cdd:cd05907     86 ------------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3647 RVLQF--ASYTFdACIAEIITTLLCGGCICVPSDSDRrnsLAKAISTMDVNWAFLTPSV-----------------ARLL 3707
Cdd:cd05907    130 RHLSFlpLAHVF-ERRAGLYVPLLAGARIYFASSAET---LLDDLSEVRPTVFLAVPRVwekvyaaikvkavpglkRKLF 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3708 DPGLIPSLKILAIGGeQSSSADWNRWpgsVQKIHV-----YGPTECCIFCTgYTTKQGFEPSTIGTSVasvswvvdPENH 3782
Cdd:cd05907    206 DLAVGGRLRFAASGG-APLPAELLHF---FRALGIpvyegYGLTETSAVVT-LNPPGDNRIGTVGKPL--------PGVE 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3783 NRLAPlgsMGELLMEGPILARGYLNDVDKTEAAFIDDPaWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGR-KDSQ 3861
Cdd:cd05907    273 VRIAD---DGEILVRGPNVMLGYYKNPEATAEALDADG-WL---------------HTGDLGEIDEDGFLHITGRkKDLI 333
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3862 VKVRGQRVELGEVEHHVREClpearqLAVEVILPSGQKDhAMLAAFVQLEEGTQNALLDKEAGGEDSMAQVVFLASVEEE 3941
Cdd:cd05907    334 ITSGGKNISPEPIENALKAS------PLISQAVVIGDGR-PFLVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRAE 406

                   ....*
gi 1820002560 3942 LAKRL 3946
Cdd:cd05907    407 IEAAV 411
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
6716-7041 1.03e-30

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 130.67  E-value: 1.03e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6716 PNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIL 6795
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6796 RQTGAQVILASAQNTTLF---------------QSSNQTVVTVNRSSYIL------------------------------ 6830
Cdd:cd17656     82 LDSGVRVVLTQRHLKSKLsfnkstilledpsisQEDTSNIDYINNSDDLLyiiytsgttgkpkgvqlehknmvnllhfer 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560      --------------------------------------------------------------------------------
Cdd:cd17656    162 ektninfsdkvlqfatcsfdvcyqeifstllsggtlyiireetkrdveqlfdlvkrhnievvflpvaflkfifserefin 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6831 -FPDENREAY----------PFVR--------------PS------------------------------------NAAL 6849
Cdd:cd17656    242 rFPTCVKHIItageqlvitnEFKEmlhehnvhlhnhygPSethvvttytinpeaeipelppigkpisntwiyildqEQQL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6850 APLGSIGELLVEGPILARGYLNDADKTAAAFVNDPAWLVEghgkhpgrrgRLYKTGDLVYYNKDGNLVYIGRKDGQVKVR 6929
Cdd:cd17656    322 QPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNE----------RMYRTGDLARYLPDGNIEFLGRADHQVKIR 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6930 GQRVELGEIENRLRECmPRATQMAVEVISPAGAAEQAKTMVVAFLQLNDEardallggnvpnddnlsaqvvfpaKVDEKL 7009
Cdd:cd17656    392 GYRIELGEIEAQLLNH-PGVSEAVVLDKADDKGEKYLCAYFVMEQELNIS------------------------QLREYL 446
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1820002560 7010 SNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd17656    447 AKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
3463-3976 1.34e-30

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 131.08  E-value: 1.34e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3463 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP-- 3540
Cdd:PRK06187     8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPin 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3541 --LDPdhpasrhEEIF---EQTGAQVVVASAQYS------ARWTSSSCHVVTVSKALSSQLP-------AVVDSTNTS-- 3600
Cdd:PRK06187    88 irLKP-------EEIAyilNDAEDRVVLVDSEFVpllaaiLPQLPTVRTVIVEGDGPAAPLApevgeyeELLAAASDTfd 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3601 ---VRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVL----QFASYTFDACIAeiitTLLCGGCI 3673
Cdd:PRK06187   161 fpdIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHAWGLPYL----ALMAGAKQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3674 CVPSDSDRRNsLAKAISTMDVNWAFLTPSVARLLDPGLIP------SLKILAIGGeqssSA-------DWNRWPGsVQKI 3740
Cdd:PRK06187   237 VIPRRFDPEN-LLDLIETERVTFFFAVPTIWQMLLKAPRAyfvdfsSLRLVIYGG----AAlppallrEFKEKFG-IDLV 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3741 HVYGPTECC-IFCTGYTTKQGFEPSTI----GTSVASVSW-VVDPENhNRLAP-LGSMGELLMEGPILARGYLNDVDKTE 3813
Cdd:PRK06187   311 QGYGMTETSpVVSVLPPEDQLPGQWTKrrsaGRPLPGVEArIVDDDG-DELPPdGGEVGEIIVRGPWLMQGYWNRPEATA 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3814 AAFIDDpaWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE----HH--VREClpearq 3887
Cdd:PRK06187   390 ETIDGG--WL---------------HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEdalyGHpaVAEV------ 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3888 lAVeVILP---SGQKDHamlaAFVQLEEGTQnalLDkeaggEDSMAQvvFLAsveEELAK-RLPEHM--VPTVffsllhf 3961
Cdd:PRK06187   447 -AV-IGVPdekWGERPV----AVVVLKPGAT---LD-----AKELRA--FLR---GRLAKfKLPKRIafVDEL------- 500
                          570
                   ....*....|....*
gi 1820002560 3962 PTTTSGKTDRKRLRE 3976
Cdd:PRK06187   501 PRTSVGKILKRVLRE 515
PRK09088 PRK09088
acyl-CoA synthetase; Validated
4548-5060 1.76e-30

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 129.93  E-value: 1.76e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4548 AEQARARPDTPAI--CAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 4625
Cdd:PRK09088     2 AFHARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4626 PASRHEHIFRQTGAQVVLASAQYATlwtslGRSVVIVSEASTSQLPVVTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLE 4705
Cdd:PRK09088    82 SASELDALLQDAEPRLLLGDDAVAA-----GRTDVEDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4706 HKAVVTSCLGhgqaFGITdhTRVLQFASYTFDACIAEII-------TTLLCCGCICVPSDSDRRNNLAKAIN-AMDVNWA 4777
Cdd:PRK09088   157 ERNLQQTAHN----FGVL--GRVDAHSSFLCDAPMFHIIglitsvrPVLAVGGSILVSNGFEPKRTLGRLGDpALGITHY 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4778 LLTPSVARML------DPCVVQSLKILVLGGEQVNSADWDRW-PKSIQTINAYGPTEC------SICCTTYSGK---QGF 4841
Cdd:PRK09088   231 FCVPQMAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWlDDGIPMVDGFGMSEAgtvfgmSVDCDVIRAKagaAGI 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4842 KSGTIGTSIVsvswvvdpENHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpAWllegygghsgrqgrlYKTG 4921
Cdd:PRK09088   311 PTPTVQTRVV--------DDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGD-GW---------------FRTG 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4922 DLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE-----H-HVREClteakqlAVeVIVPE---GEGGYamLAAFVQLGD 4992
Cdd:PRK09088   367 DIARRDADGFFWVVDRKKDMFISGGENVYPAEIEavladHpGIREC-------AV-VGMADaqwGEVGY--LAIVPADGA 436
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 4993 DTYNTLVkekaggdsltvqvvfLDRVEEELAK-RVPEHMMLTtfftlEAMPTTTSGKIDRKRLREIGAS 5060
Cdd:PRK09088   437 PLDLERI---------------RSHLSTRLAKyKVPKHLRLV-----DALPRTASGKLQKARLRDALAA 485
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
2-279 2.71e-30

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 125.86  E-value: 2.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL------EPSHIPSLRILVMGGEQVNSADWDRWPSS--VQTINGYGPTECCIVCTGYTSEQDFT-T 72
Cdd:cd04433     88 KVTILLGVPTLLARLlkapesAGYDLSSLRALVSGGAPLPPELLERFEEApgIKLVNGYGLTETGGTVATGPPDDDARkP 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   73 GTIGTSIASVSW-VVDPkdHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinnpawllegHGGYagrqgrlYKTGD 151
Cdd:cd04433    168 GSVGRPVPGVEVrIVDP--DGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD----------EDGW-------YRTGD 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  152 LVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAVeVVLPLGQKNHAtLAAFIQLDKGtHNALLKEk 231
Cdd:cd04433    229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGH-PGVAEAAV-VGVPDPEWGER-VVAVVVLRPG-ADLDAEE- 303
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560  232 vggddsiarvvflagVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTD 279
Cdd:cd04433    304 ---------------LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
4548-5054 3.25e-30

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 128.98  E-value: 3.25e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4548 AEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMV----PLCFEksmwTVVAMLAVLKAGGAFVPLDP 4623
Cdd:cd05920     22 ARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVvvqlPNVAE----FVVLFFALLRLGAVPVLALP 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4624 DHPASRHEHIFRQTGAQVVLASAQYATL-WTSLGRSVVivseastsqlpvvTKTADPsvnpgnaAYAIFTSGSTGIPKGV 4702
Cdd:cd05920     98 SHRRSELSAFCAHAEAVAYIVPDRHAGFdHRALARELA-------------ESIPEV-------ALFLLSGGTTGTPKLI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4703 VLEHKAVVTSCLGHGQAFGITDHTRVLQF--ASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLAkAINAMDVNWALLT 4780
Cdd:cd05920    158 PRTHNDYAYNVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFP-LIEREGVTVTALV 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4781 PSVARM-LDPCV-----VQSLKILVLGGEQVNSADWDRWPKSI--QTINAYGPTECSICCTTYSGKQGFKSGTIGTSIVS 4852
Cdd:cd05920    237 PALVSLwLDAAAsrradLSSLRLLQVGGARLSPALARRVPPVLgcTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRPMSP 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4853 V--SWVVDPENhNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAFIDDpawlleGYgghsgrqgrlYKTGDLVRYDADG 4930
Cdd:cd05920    317 DdeIRVVDEEG-NPVPP-GEEGELLTRGPYTIRGYYRAPEHNARAFTPD------GF----------YRTGDLVRRTPDG 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4931 NLVYLGRKDSQVKLRGQRVELGEVEHHVREcLTEAKQLAVeVIVPEGEggyamlaafvqLGDDTYNTLVKEkagGDSLTV 5010
Cdd:cd05920    379 YLVVEGRIKDQINRGGEKIAAEEVENLLLR-HPAVHDAAV-VAMPDEL-----------LGERSCAFVVLR---DPPPSA 442
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 5011 QVV--FLDrvEEELAK-RVPEHMMLttfftLEAMPTTTSGKIDRKRL 5054
Cdd:cd05920    443 AQLrrFLR--ERGLAAyKLPDRIEF-----VDSLPLTAVGKIDKKAL 482
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
875-1366 4.59e-30

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 127.41  E-value: 4.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  875 DGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVL 954
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  955 TSsqhamlfasserhqvtvskvstsqlptvvnfakspvdpgnTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYT 1034
Cdd:cd05934     81 VD----------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1035 DHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNNLAKAISTMDVNCALLTPSVARLL---EPSAVPSLKRL-V 1110
Cdd:cd05934    121 EDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLlaqPPSPDDRAHRLrA 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1111 LQGEQVSFADW----NRWpgSVQTINGYGPTECSVC-CNTYSGKQGFKS-GIIGTSVASLswVVDAgnHNRLAPLGSIGE 1184
Cdd:cd05934    201 AYGAPNPPELHeefeERF--GVRLLEGYGMTETIVGvIGPRDEPRRPGSiGRPAPGYEVR--IVDD--DGQELPAGEPGE 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1185 LLV---EGPILARGYLNDIDKTEAAFiddpawllegyeghagrRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVE 1261
Cdd:cd05934    275 LVIrglRGWGFFKGYYNMPEATAEAM-----------------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1262 LGEIE-----HhvreclPEARQLAVeVILPSGQKEHAlLAAFIQLDKGnhnalfeEKASGEDsmaqvvfltgVEEELAKR 1336
Cdd:cd05934    338 SAEVErailrH------PAVREAAV-VAVPDEVGEDE-VKAVVVLRPG-------ETLDPEE----------LFAFCEGQ 392
                          490       500       510
                   ....*....|....*....|....*....|
gi 1820002560 1337 LPEHMVPTILFTVKAMPITTSGKIDRKRLQ 1366
Cdd:cd05934    393 LAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
6277-6666 5.47e-30

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 127.43  E-value: 5.47e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6277 MYPCSPLQEGLM--SLTAKRAGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVEE------ 6348
Cdd:cd19547      1 VYPLAPMQEGMLfrGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDlappwa 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6349 KIQWTE------SKRLEEYLREDKAVSMGLGD-PLARYAIIKEAwGGKRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAV 6421
Cdd:cd19547     81 LLDWSGedpdrrAELLERLLADDRAAGLSLADcPLYRLTLVRLG-GGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6422 LETQPS------FNAFIQYLSQQDL--EATAAYWQTALADCEATLFPPLPSSVKQLVadTTVEHQCPLPSRSTSDTTTS- 6492
Cdd:cd19547    160 HGREPQlspcrpYRDYVRWIRARTAqsEESERFWREYLRDLTPSPFSTAPADREGEF--DTVVHEFPEQLTRLVNEAARg 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6493 ------TLIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEMI 6566
Cdd:cd19547    238 ygvttnAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6567 AYEQTGLQQIAKMGPDPQHACG--FQTLLVVQ--PAGDVLGSDDTLGKWRGYSglQDFMTYALGVrCTLSAEGVKITASF 6642
Cdd:cd19547    318 AHGHVPLAQIKSWASGERLSGGrvFDNLVAFEnyPEDNLPGDDLSIQIIDLHA--QEKTEYPIGL-IVLPLQKLAFHFNY 394
                          410       420
                   ....*....|....*....|....
gi 1820002560 6643 DARVIEHWVVEKMLGQFSFAMQQL 6666
Cdd:cd19547    395 DTTHFTRAQVDRFIEVFRLLTEQL 418
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7641-8121 8.56e-30

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 127.56  E-value: 8.56e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7641 LSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGA----FVPLDPDHPASRHEEIFEQTGAQVVVASAQYSA 7716
Cdd:cd05922      2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7717 RWT--SSSCHVVTVS------KALSSQLPAVVdstntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGI 7788
Cdd:cd05922     82 RLRdaLPASPDPGTVldadgiRAARASAPAHE------VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7789 TNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFLTPSVARLL-----DPGLIPSLKI 7863
Cdd:cd05922    156 TADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLtrlgfDPAKLPSLRY 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7864 LAIGGEQSSSADWNRW----PGSvqKIHV-YGPTECCIFCTGYTTKQGFE-PSTIGTSVASVSWVVDPENHNRLAPlGSM 7937
Cdd:cd05922    236 LTQAGGRLPQETIARLrellPGA--QVYVmYGQTEATRRMTYLPPERILEkPGSIGLAIPGGEFEILDDDGTPTPP-GEP 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7938 GELLMEGPILARGYLNDvdkteaafiddpawllEGYPGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVEL 8017
Cdd:cd05922    313 GEIVHRGPNVMKGYWND----------------PPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISP 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8018 GEVEHHVRECLPEARQLAVEVILPSGQKnhamLAVFVqlgkgthiahlEEKAGGEDSMAQVVfltgteeeLAKRLPKHMV 8097
Cdd:cd05922    377 TEIEAAARSIGLIIEAAAVGLPDPLGEK----LALFV-----------TAPDKIDPKDVLRS--------LAERLPPYKV 433
                          490       500
                   ....*....|....*....|....
gi 1820002560 8098 PTVFFALLHFPMTTSGKADRKRLR 8121
Cdd:cd05922    434 PATVRVVDELPLTASGKVDYAALR 457
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4574-5055 1.10e-29

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 127.17  E-value: 1.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4574 TLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGA----FVPLDPDHPASRHEHIFRQTGAQVVLASAQYA 4649
Cdd:cd05922      1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4650 TLWtslgRSVVIVSEASTSQLPVVTKTADPSVNPG------NAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGIT 4723
Cdd:cd05922     81 DRL----RDALPASPDPGTVLDADGIRAARASAPAhevsheDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4724 DHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLAKAINAMDVNWALLTPSVARML-----DPCVVQSLKIL 4798
Cdd:cd05922    157 ADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLtrlgfDPAKLPSLRYL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4799 VLGGEQVNSADWDRWPKSI---QTINAYGPTECSICCTTYSGKQ-GFKSGTIGTSIVSVSWVVDPENHNRLAPlGSIGEL 4874
Cdd:cd05922    237 TQAGGRLPQETIARLRELLpgaQVYVMYGQTEATRRMTYLPPERiLEKPGSIGLAIPGGEFEILDDDGTPTPP-GEPGEI 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4875 LVEGPILARGYLNDmekteaafiddPAWLLEGYGGhsgrQGRLYkTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEV 4954
Cdd:cd05922    316 VHRGPNVMKGYWND-----------PPYRRKEGRG----GGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEI 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4955 EHHVRECLTEAKQLAVEVIVPEGEGgyamLAAFVQLGDDtyntlvkekaggdsltvqvVFLDRVEEELAKRVPEHMMLTT 5034
Cdd:cd05922    380 EAAARSIGLIIEAAAVGLPDPLGEK----LALFVTAPDK-------------------IDPKDVLRSLAERLPPYKVPAT 436
                          490       500
                   ....*....|....*....|.
gi 1820002560 5035 FFTLEAMPTTTSGKIDRKRLR 5055
Cdd:cd05922    437 VRVVDELPLTASGKVDYAALR 457
PRK06145 PRK06145
acyl-CoA synthetase; Validated
4545-5056 1.47e-29

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 127.31  E-value: 1.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4545 DQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 4624
Cdd:PRK06145     6 ASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4625 HPASRHEHIFRQTGAQVVLASAQYATLwTSLGRSVVIVSEASTSQLPVVTKTADP-----SVNPGNAAYAIFTSGSTGIP 4699
Cdd:PRK06145    86 LAADEVAYILGDAGAKLLLVDEEFDAI-VALETPKIVIDAAAQADSRRLAQGGLEippqaAVAPTDLVRLMYTSGTTDRP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4700 KGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFAS-YTFDACIAEIITTLLCCGCICVPSDSDRRNNLAkAINAMDVNWAL 4778
Cdd:PRK06145   165 KGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPlYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA-AIERHRLTCAW 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4779 LTP-SVARML-----DPCVVQSLKILVLGGEQVNSA---DWDRWPKSIQTINAYGPTE-CSICCTTYSGKQGFKSGTIGT 4848
Cdd:PRK06145   244 MAPvMLSRVLtvpdrDRFDLDSLAWCIGGGEKTPESrirDFTRVFTRARYIDAYGLTEtCSGDTLMEAGREIEKIGSTGR 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4849 SIVSVSWVVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAFIDDpaWLlegygghsgrqgrlyKTGDLVRYDA 4928
Cdd:PRK06145   324 ALAHVEIRIADGAGRWLPP-NMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--WF---------------RSGDVGYLDE 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4929 DGNLVYLGRKDSQVKLRGQRVELGEVEHHVREcLTEAKQLAVeVIVPEGEGGYAMLAAFVQlgddtyntlvkekAGGDSL 5008
Cdd:PRK06145   386 EGFLYLTDRKKDMIISGGENIASSEVERVIYE-LPEVAEAAV-IGVHDDRWGERITAVVVL-------------NPGATL 450
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5009 TVQVvfLDR-VEEELAK-RVPEHMMLTtfftlEAMPTTTSGKIDRKRLRE 5056
Cdd:PRK06145   451 TLEA--LDRhCRQRLASfKVPRQLKVR-----DELPRNPSGKVLKRVLRD 493
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
4551-5054 2.35e-29

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 126.97  E-value: 2.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPA-ICAWDG-ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 4628
Cdd:cd05904     15 ASAHPSRPAlIDAATGrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4629 RHEHIFRQTGAQVVLASAQYATLWTSLGRSVVIVSEA-----STSQLPVVTKTADPS---VNPGNAAYAIFTSGSTGIPK 4700
Cdd:cd05904     95 EIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAefdslSFSDLLFEADEAEPPvvvIKQDDVAALLYSSGTTGRSK 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4701 GVVLEHKAVVTSCLGH--GQAFGITDHTRVL----QFASYTFDAciaeIITTLLCCG-CICVPSDSDRRNNLAkAINAMD 4773
Cdd:cd05904    175 GVMLTHRNLIAMVAQFvaGEGSNSDSEDVFLcvlpMFHIYGLSS----FALGLLRLGaTVVVMPRFDLEELLA-AIERYK 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4774 VNWALLTPSV------ARMLDPCVVQSLKILVLG----GEQVNSADWDRWPkSIQTINAYGPTECSICCTTYSG--KQGF 4841
Cdd:cd05904    250 VTHLPVVPPIvlalvkSPIVDKYDLSSLRQIMSGaaplGKELIEAFRAKFP-NVDLGQGYGMTESTGVVAMCFApeKDRA 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4842 KSGTIGTSIVSV-SWVVDPENhNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAfIDDPAWLlegygghsgrqgrlyKT 4920
Cdd:cd05904    329 KYGSVGRLVPNVeAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLNNPEATAAT-IDKEGWL---------------HT 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4921 GDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVrecLTEAKQLAVEVI-VPEGEGG-YAMlaAFVqlgddtyntl 4998
Cdd:cd05904    392 GDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALL---LSHPEILDAAVIpYPDEEAGeVPM--AFV---------- 456
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 4999 VkeKAGGDSLTVQVVfLDRVEEELA--KRVPEhmmltTFFTlEAMPTTTSGKIDRKRL 5054
Cdd:cd05904    457 V--RKPGSSLTEDEI-MDFVAKQVApyKKVRK-----VAFV-DAIPKSPSGKILRKEL 505
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3494-3975 2.64e-29

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 126.02  E-value: 2.64e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3494 ALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGA----FVPLDPDHPASRHEEIFEQTGAQVVVASAQYS 3569
Cdd:cd05922      1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3570 ARWT--SSSCHVVTVS------KALSSQLPAVVdstntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFG 3641
Cdd:cd05922     81 DRLRdaLPASPDPGTVldadgiRAARASAPAHE------VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3642 ITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFLTPSVARLL-----DPGLIPSLK 3716
Cdd:cd05922    155 ITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLtrlgfDPAKLPSLR 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3717 ILAIGGEQSSSADWNRW----PGSvqKIHV-YGPTECCIFCTGYTTKQGFE-PSTIGTSVASVSWVVDPENHNRLAPlGS 3790
Cdd:cd05922    235 YLTQAGGRLPQETIARLrellPGA--QVYVmYGQTEATRRMTYLPPERILEkPGSIGLAIPGGEFEILDDDGTPTPP-GE 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3791 MGELLMEGPILARGYLNDvdkteaafiddpawllEGYPGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVE 3870
Cdd:cd05922    312 PGEIVHRGPNVMKGYWND----------------PPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRIS 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3871 LGEVEHHVRECLPEARQLAVEVILPSGQKdhamLAAFVQLEEGtqnalldkeaggedsmaqvVFLASVEEELAKRLPEHM 3950
Cdd:cd05922    376 PTEIEAAARSIGLIIEAAAVGLPDPLGEK----LALFVTAPDK-------------------IDPKDVLRSLAERLPPYK 432
                          490       500
                   ....*....|....*....|....*
gi 1820002560 3951 VPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd05922    433 VPATVRVVDELPLTASGKVDYAALR 457
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4566-5055 3.76e-29

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 125.24  E-value: 3.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4566 ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPdhpasrhehIFRQTGAQVVLAS 4645
Cdd:cd05971      6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFA---------LFGPEALEYRLSN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4646 aqyatlwtslgrsvvivSEASTsqlpVVTKTADpsvnpgNAAYAIFTSGSTGIPKGVVLEHKAVvtscLGHGQAFGITdh 4725
Cdd:cd05971     77 -----------------SGASA----LVTDGSD------DPALIIYTSGTTGPPKGALHAHRVL----LGHLPGVQFP-- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4726 trvLQFASYTFD--------ACIAEIITTLLCCGCICVPSDSDRRNNL-AKAINAM----DVNWALLTPSVARMLDPCVV 4792
Cdd:cd05971    124 ---FNLFPRDGDlywtpadwAWIGGLLDVLLPSLYFGVPVLAHRMTKFdPKAALDLmsryGVTTAFLPPTALKMMRQQGE 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4793 Q------SLKILVLGGEQV--NSADWDRWPKSIQTINAYGPTECSICCTTYSGKQGFKSGTIGT----SIVSVswvVDpE 4860
Cdd:cd05971    201 QlkhaqvKLRAIATGGESLgeELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKpipgHRVAI---VD-D 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4861 NHNRLAPlGSIGELLVE--GPILARGYLNDMEKTEAAFIDDpaWLLegygghsgrqgrlykTGDLVRYDADGNLVYLGRK 4938
Cdd:cd05971    277 NGTPLPP-GEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD--WLL---------------TGDLGRKDSDGYFWYVGRD 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4939 DSQVKLRGQRVELGEVEhhvrECLTEAKQ-LAVEVI-VPEGEGGyAMLAAFVQL--GDDTYNTLVKEkaggdsltvqvvf 5014
Cdd:cd05971    339 DDVITSSGYRIGPAEIE----ECLLKHPAvLMAAVVgIPDPIRG-EIVKAFVVLnpGETPSDALARE------------- 400
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 5015 ldrVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLR 5055
Cdd:cd05971    401 ---IQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
50-283 4.10e-29

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 125.66  E-value: 4.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   50 NGYGPTECCIVCTGYTSEQDFTT--GTIGTSIASVsWVVDPKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFIN 127
Cdd:cd17656    276 NHYGPSETHVVTTYTINPEAEIPelPPIGKPISNT-WIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFP 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  128 NPAwlleghggyaGRQGRLYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAVevvlplgq 207
Cdd:cd17656    355 DPF----------DPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNH-PGVSEAVV-------- 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  208 knhatlaafiqLDKGTHNallkekvGGDDSIARVVFLAGV-----EEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKR 282
Cdd:cd17656    416 -----------LDKADDK-------GEKYLCAYFVMEQELnisqlREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKA 477

                   .
gi 1820002560  283 L 283
Cdd:cd17656    478 L 478
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
7611-8120 4.31e-29

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 125.90  E-value: 4.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAGGAFVP 7686
Cdd:cd05920     19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVvvqlPNVAE----FVVLFFALLRLGAVPVL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7687 LDPDHpasRHEEI---FEQTGAQVVVASAQYSarwtsSSCHVVTVSKALSSQlPAVvdstntsvrpenaAYIIFTSGSTG 7763
Cdd:cd05920     95 ALPSH---RRSELsafCAHAEAVAYIVPDRHA-----GFDHRALARELAESI-PEV-------------ALFLLSGGTTG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7764 VPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQF--ASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAkAISTMDVN 7841
Cdd:cd05920    153 TPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFP-LIEREGVT 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7842 WAFLTPSVARL-LDPGL-----IPSLKILAIGGEQSSSADWNRWPG----SVQKihVYGPTECCIfctGYTTKQGFEPST 7911
Cdd:cd05920    232 VTALVPALVSLwLDAAAsrradLSSLRLLQVGGARLSPALARRVPPvlgcTLQQ--VFGMAEGLL---NYTRLDDPDEVI 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7912 IGTSVASVS-----WVVDPENhNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawlleGYpghpgrqgrlYKT 7986
Cdd:cd05920    307 IHTQGRPMSpddeiRVVDEEG-NPVPP-GEEGELLTRGPYTIRGYYRAPEHNARAFTPD------GF----------YRT 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7987 GDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPS---GQKNHAMLAVfvqlgKGTHIA 8063
Cdd:cd05920    369 GDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR-HPAVHDAAV-VAMPDellGERSCAFVVL-----RDPPPS 441
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 8064 HLEEKAggedsmaqvvFLtgTEEELAK-RLPKHMVPtvffaLLHFPMTTSGKADRKRL 8120
Cdd:cd05920    442 AAQLRR----------FL--RERGLAAyKLPDRIEF-----VDSLPLTAVGKIDKKAL 482
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
7623-8122 4.47e-29

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 125.09  E-value: 4.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7623 APAICAWDGELTYGELDVLSSNLAGHLVQLG-VNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFE 7701
Cdd:cd05941      2 RIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7702 QTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsvrpeNAAYIIFTSGSTGVPKGVVLEHRAVATSCLG 7781
Cdd:cd05941     82 DSEPSLVL-----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRA 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7782 HGRAFGITNLSRVLQ------------------FASYT------FDACIAEII-----TTLLCGgcicVPSDSDRrnsLA 7832
Cdd:cd05941    121 LVDAWRWTEDDVLLHvlplhhvhglvnallcplFAGASveflpkFDPKEVAISrlmpsITVFMG----VPTIYTR---LL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7833 KAISTMDVNWAFLTPSVARLLDpglipslkiLAIGGeqsSSA----DWNRWpgsvQKI--HV----YGPTEccifcTGYT 7902
Cdd:cd05941    194 QYYEAHFTDPQFARAAAAERLR---------LMVSG---SAAlpvpTLEEW----EAItgHTllerYGMTE-----IGMA 252
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7903 TKQGFE----PSTIGTSVASVSWVVDPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawlleGYpghpg 7978
Cdd:cd05941    253 LSNPLDgerrPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDD------GW----- 321
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7979 rqgrlYKTGDLVQYNADGNLVYLGR-KDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKNHAMLAVFVQlg 8057
Cdd:cd05941    322 -----FKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLA-HPGVSECAV-IGVPDPDWGERVVAVVVL-- 392
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 8058 kgthiahleekaggeDSMAQVVFLTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:cd05941    393 ---------------RAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
1507-1895 4.64e-29

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 124.44  E-value: 4.64e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1507 YPCSPLQEGlMSLTAKRAGD---YIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSElGLLQVVIE------- 1576
Cdd:cd19066      2 IPLSPMQRG-MWFLKKLATDpsaFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAG-RYEQVVLDktvrfri 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1577 ENIQWTEPKSLEEYLSE--DKAVSVGL---GDPLARYAFVKEACGGKRWfVWTIHHAVYDGWSLPLILHAVKQVYSGGVL 1651
Cdd:cd19066     80 EIIDLRNLADPEARLLEliDQIQQTIYdleRGPLVRVALFRLADERDVL-VVAIHHIIVDGGSFQILFEDISSVYDAAER 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1652 Q---WQPSFNAFI-------QYLGQQDLEATVAYWQTALADCEAVL-FPTLPPTVTQPVADATVEYQCPPLSKA------ 1714
Cdd:cd19066    159 QkptLPPPVGSYAdyaawleKQLESEAAQADLAYWTSYLHGLPPPLpLPKAKRPSQVASYEVLTLEFFLRSEETkrlrev 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1715 --TSDTTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNTPvtGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQAT 1792
Cdd:cd19066    239 arESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1793 DMIAHEQTGLQRI----AKMGQGPQHAcSFQTLLVVQPVDDVLDNTLGEWRDHSELQEFTTYTLMLQCMLAAE---GVQI 1865
Cdd:cd19066    317 EAIEHQRVPFIELvrhlGVVPEAPKHP-LFEPVFTFKNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEDpdgDLLL 395
                          410       420       430
                   ....*....|....*....|....*....|
gi 1820002560 1866 TASFDTRVIEKWVVEKMLRQFSFIMQQLAE 1895
Cdd:cd19066    396 RLEYSRGVYDERTIDRFAERYMTALRQLIE 425
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
854-1367 5.27e-29

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 126.17  E-value: 5.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 933
Cdd:PRK07656     7 LPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLN 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 PGHPASRHEEIFKQIGAQVVLTSSQ----------------HAMLFASSERHQVTVSKVSTSQL--PTVVNFAKSPVDPG 995
Cdd:PRK07656    87 TRYTADEAAYILARGDAKALFVLGLflgvdysattrlpaleHVVICETEEDDPHTEKMKTFTDFlaAGDPAERAPEVDPD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  996 NTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQ----FASYTFDACiaeIITTLLYGGCIcVPsesd 1071
Cdd:PRK07656   167 DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAanpfFHVFGYKAG---VNAPLMRGATI-LP---- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1072 rrnnlakaistmdvncaLLTPSVARLLEPSA---------VPSLKRLVLQGEQVSFADW--------------------- 1121
Cdd:PRK07656   239 -----------------LPVFDPDEVFRLIEteritvlpgPPTMYNSLLQHPDRSAEDLsslrlavtgaasmpvallerf 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1122 -NRWPgsVQTI-NGYGPTECS--VCCNTYSGKQGFKSGIIGTSVASLSWVVdAGNHNRLAPLGSIGELLVEGPILARGYL 1197
Cdd:PRK07656   302 eSELG--VDIVlTGYGLSEASgvTTFNRLDDDRKTVAGTIGTAIAGVENKI-VNELGEEVPVGEVGELLVRGPNVMKGYY 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1198 NDIDKTEAAfIDDPAWLlegyegHagrrgrlykTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhhvrECL---P 1274
Cdd:PRK07656   379 DDPEATAAA-IDADGWL------H---------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVE----EVLyehP 438
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1275 EARQLAVeVILP---SGQKEHallaAFIQLDKGNHnalfeekasgedsmaqvvfLTgvEEELAKRLPEHM----VP-TIL 1346
Cdd:PRK07656   439 AVAEAAV-IGVPderLGEVGK----AYVVLKPGAE-------------------LT--EEELIAYCREHLakykVPrSIE 492
                          570       580
                   ....*....|....*....|.
gi 1820002560 1347 FtVKAMPITTSGKIDRKRLQD 1367
Cdd:PRK07656   493 F-LDELPKNATGKVLKRALRE 512
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
5632-6132 6.46e-29

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 124.26  E-value: 6.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 5711
Cdd:cd17631      5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5712 EDTFRHTGAQVVVtsaqhsarwigtnhqvvtvsagslgqlstlvnpvglpaipENAVYIMFTSGSTGIPKGVVLEHRAVV 5791
Cdd:cd17631     85 AYILADSGAKVLF----------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLL 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5792 TSCWGRGRAFGITNLSRVLQFASYTFDACMD-EIITTLMYGGCICVPsdsdRRNDLVKAISTMD---VSCALLTPSVARL 5867
Cdd:cd17631    125 WNAVNALAALDLGPDDVLLVVAPLFHIGGLGvFTLPTLLRGGTVVIL----RKFDPETVLDLIErhrVTSFFLVPTMIQA 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5868 L--EPSS----VPTLQMLVLQGEQVSFADWNRWPA-SVQTINGYGPTECS--ICCNTYSGKQGfKSGIIGTSVASVSW-V 5937
Cdd:cd17631    201 LlqHPRFattdLSSLRAVIYGGAPMPERLLRALQArGVKFVQGYGMTETSpgVTFLSPEDHRR-KLGSAGRPVFFVEVrI 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5938 VDPEnhDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpaWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLG 6017
Cdd:cd17631    280 VDPD--GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG--WF---------------HTGDLGRLDEDGYLYIVD 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6018 RKDSQVKLRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHAMlAAFVQLEEGTQnalLDKEAsgedsmaqvvFLA 6097
Cdd:cd17631    341 RKKDMIISGGENVYPAEVEDVLYE-HPAVAEVAV-IGVPDEKWGEAV-VAVVVPRPGAE---LDEDE----------LIA 404
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 6098 SVEEELAK-RLPEHmvptVFF--SLlhfPTTTSGKTDR 6132
Cdd:cd17631    405 HCRERLARyKIPKS----VEFvdAL---PRNATGKILK 435
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
4551-5056 7.56e-29

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 126.20  E-value: 7.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAICAWDGE------LTYGELDTLSSKLASHLVQLGvKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 4624
Cdd:cd05931      3 AAARPDRPAYTFLDDEggreetLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4625 HPASRHEH---IFRQTGAQVVLASAQYATLWTSLGRSVvivSEASTSQLPVVTKTAD--------PSVNPGNAAYAIFTS 4693
Cdd:cd05931     82 TPGRHAERlaaILADAGPRVVLTTAAALAAVRAFAASR---PAAGTPRLLVVDLLPDtsaadwppPSPDPDDIAYLQYTS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4694 GSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFD-ACIAEIITTLLcCGCICV---PSD----------- 4758
Cdd:cd05931    159 GSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmGLIGGLLTPLY-SGGPSVlmsPAAflrrplrwlrl 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4759 -SDRRNNLAKAIN-AMD--VNWAllTPSVARMLDpcvVQSLKILVLGGEQVNSADWDRW----------PKSIQTinAYG 4824
Cdd:cd05931    238 iSRYRATISAAPNfAYDlcVRRV--RDEDLEGLD---LSSWRVALNGAEPVRPATLRRFaeafapfgfrPEAFRP--SYG 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4825 PTECSICCTTYSGKQGFKS------------------GTIGTSIVSVSWV--------VDPENHNRLAPlGSIGELLVEG 4878
Cdd:cd05931    311 LAEATLFVSGGPPGTGPVVlrvdrdalagravavaadDPAARELVSCGRPlpdqevriVDPETGRELPD-GEVGEIWVRG 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4879 PILARGYLNDMEKTEAAF-----IDDPAWLlegygghsgrqgrlyKTGDLVRYdADGNLVYLGRKDSQVKLRGQRVELGE 4953
Cdd:cd05931    390 PSVASGYWGRPEATAETFgalaaTDEGGWL---------------RTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQD 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4954 VEHhvreclteakqlAVEVIVPEGEGGYAmlAAFVQLGDDTYNTLV--KEKAGGDSLTvqvvfLDRVEEELAKRVP-EH- 5029
Cdd:cd05931    454 IEA------------TAEEAHPALRPGCV--AAFSVPDDGEERLVVvaEVERGADPAD-----LAAIAAAIRAAVArEHg 514
                          570       580
                   ....*....|....*....|....*....
gi 1820002560 5030 MMLTTFFTLE--AMPTTTSGKIDRKRLRE 5056
Cdd:cd05931    515 VAPADVVLVRpgSIPRTSSGKIQRRACRA 543
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
5637-6137 7.78e-29

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 124.32  E-value: 7.78e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5637 HAPAICAWDGELTYGELDALSSKLAGHLTQLG-VKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPasrhedtf 5715
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYP-------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5716 rhtgaqvvvtsaQHSARWIGTNHQVvtvsagslgqlSTLVNPvglpaipenAVyIMFTSGSTGIPKGVVLEHRAVVTSCW 5795
Cdd:cd05941     73 ------------LAELEYVITDSEP-----------SLVLDP---------AL-ILYTSGTTGRPKGVVLTHANLAANVR 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5796 GRGRAFGITNLSRVLQ------------------FASYT------FDACMDEI------ITTLMyggciCVPSDSDRrnd 5845
Cdd:cd05941    120 ALVDAWRWTEDDVLLHvlplhhvhglvnallcplFAGASveflpkFDPKEVAIsrlmpsITVFM-----GVPTIYTR--- 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5846 LVKAISTMDVSCALLT---PSVARLL----EPSSVPTLqmlvlqgeqvsfadwNRWPA-SVQTI-NGYGPTECSIC-CNT 5915
Cdd:cd05941    192 LLQYYEAHFTDPQFARaaaAERLRLMvsgsAALPVPTL---------------EEWEAiTGHTLlERYGMTEIGMAlSNP 256
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5916 YSGKQgfKSGIIGTSVASVS-WVVDPENHDRLAPlGSIGELLVEGPILARGYLNDIQKTAAVFIDDpawlleGYpghpgr 5994
Cdd:cd05941    257 LDGER--RPGTVGMPLPGVQaRIVDEETGEPLPR-GEVGEIQVRGPSVFKEYWNKPEATKEEFTDD------GW------ 321
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5995 qgrlYKTGDLVRYDANGNLVCLGR-KDSQVKLRGQRVELGEVEHHVREcLPEARQLAVeVILPS---GQKdhamLAAFVQ 6070
Cdd:cd05941    322 ----FKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLA-HPGVSECAV-IGVPDpdwGER----VVAVVV 391
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 6071 LEEGTQNalldkeasgedsmaqvVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:cd05941    392 LRAGAAA----------------LSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
7609-8122 7.82e-29

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 125.68  E-value: 7.82e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7609 VHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP-- 7686
Cdd:PRK06187     8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPin 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7687 --LDPdhpasrhEEIF---EQTGAQVVVASAQYS------ARWTSSSCHVVTVSKALSSQLP-------AVVDSTNTS-- 7746
Cdd:PRK06187    88 irLKP-------EEIAyilNDAEDRVVLVDSEFVpllaaiLPQLPTVRTVIVEGDGPAAPLApevgeyeELLAAASDTfd 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7747 ---VRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVL----QFASYTFDACIAeiitTLLCGGCI 7819
Cdd:PRK06187   161 fpdIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHAWGLPYL----ALMAGAKQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7820 CVPSDSDRRNsLAKAISTMDVNWAFLTPSVARLLDPGLIP------SLKILAIGGeqssSA-------DWNRWPGsVQKI 7886
Cdd:PRK06187   237 VIPRRFDPEN-LLDLIETERVTFFFAVPTIWQMLLKAPRAyfvdfsSLRLVIYGG----AAlppallrEFKEKFG-IDLV 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7887 HVYGPTECC-IFCTGYTTKQGFEPSTI----GTSVASVSW-VVDPENhNRLAP-LGSMGELLMEGPILARGYLNDVDKTE 7959
Cdd:PRK06187   311 QGYGMTETSpVVSVLPPEDQLPGQWTKrrsaGRPLPGVEArIVDDDG-DELPPdGGEVGEIIVRGPWLMQGYWNRPEATA 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7960 AAFIDDpaWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE----HH--VREClpearq 8033
Cdd:PRK06187   390 ETIDGG--WL---------------HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEdalyGHpaVAEV------ 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8034 lAVeVILP---SGQKNHAmlavFVQLGKGTHI------AHLEEKaggedsmaqvvfltgteeeLAK-RLPKHM--VPTVf 8101
Cdd:PRK06187   447 -AV-IGVPdekWGERPVA----VVVLKPGATLdakelrAFLRGR-------------------LAKfKLPKRIafVDEL- 500
                          570       580
                   ....*....|....*....|.
gi 1820002560 8102 fallhfPMTTSGKADRKRLRE 8122
Cdd:PRK06187   501 ------PRTSVGKILKRVLRE 515
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
3465-3974 8.26e-29

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 124.75  E-value: 8.26e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAGGAFVP 3540
Cdd:cd05920     19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVvvqlPNVAE----FVVLFFALLRLGAVPVL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3541 LDPDHpasRHEEI---FEQTGAQVVVASAQYSarwtsSSCHVVTVSKALSSQlPAVvdstntsvrpenaAYIIFTSGSTG 3617
Cdd:cd05920     95 ALPSH---RRSELsafCAHAEAVAYIVPDRHA-----GFDHRALARELAESI-PEV-------------ALFLLSGGTTG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3618 VPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQF--ASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAkAISTMDVN 3695
Cdd:cd05920    153 TPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFP-LIEREGVT 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3696 WAFLTPSVARL-LDPGL-----IPSLKILAIGGEQSSSADWNRWPG----SVQKihVYGPTECCIfctGYTTKQGFEPST 3765
Cdd:cd05920    232 VTALVPALVSLwLDAAAsrradLSSLRLLQVGGARLSPALARRVPPvlgcTLQQ--VFGMAEGLL---NYTRLDDPDEVI 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3766 IGTSVASVS-----WVVDPENhNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawlleGYpghpgrqgrlYKT 3840
Cdd:cd05920    307 IHTQGRPMSpddeiRVVDEEG-NPVPP-GEEGELLTRGPYTIRGYYRAPEHNARAFTPD------GF----------YRT 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3841 GDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPS---GQKdhamLAAFVQLEEGTQNA 3917
Cdd:cd05920    369 GDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR-HPAVHDAAV-VAMPDellGER----SCAFVVLRDPPPSA 442
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 3918 LLDKEaggedsmaqvvFLAsvEEELAK-RLPEHMVPtvffsLLHFPTTTSGKTDRKRL 3974
Cdd:cd05920    443 AQLRR-----------FLR--ERGLAAyKLPDRIEF-----VDSLPLTAVGKIDKKAL 482
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
4551-5055 9.98e-29

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 125.17  E-value: 9.98e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 4630
Cdd:cd05959     14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4631 EHIFRQTGAQVVLASAQYATLWTSLGRS------VVIVSEASTSQLPVVTKTAD-----PSVNPGNA-----AYAIFTSG 4694
Cdd:cd05959     94 AYYLEDSRARVVVVSGELAPVLAAALTKsehtlvVLIVSGGAGPEAGALLLAELvaaeaEQLKPAAThaddpAFWLYSSG 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4695 STGIPKGVVLEHKAVVTSCLGHGQ-AFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICV-----PSdsdrrnnlAKA 4768
Cdd:cd05959    174 STGRPKGVVHLHADIYWTAELYARnVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVlmperPT--------PAA 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4769 INAMdvnWALLTPSV--------ARML-DPCVVQ----SLKILVLGGEQVNSADWDRWPK--SIQTINAYGPTEC-SICC 4832
Cdd:cd05959    246 VFKR---IRRYRPTVffgvptlyAAMLaAPNLPSrdlsSLRLCVSAGEALPAEVGERWKArfGLDILDGIGSTEMlHIFL 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4833 TTYSGKqgFKSGTIGTSIVSVSW-VVDPENHNrlAPLGSIGELLVEGPILARGYLNDMEKTEAAFiddpawllegygghs 4911
Cdd:cd05959    323 SNRPGR--VRYGTTGKPVPGYEVeLRDEDGGD--VADGEPGELYVRGPSSATMYWNNRDKTRDTF--------------- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4912 grQGRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhhvrECL-TEAKQLAVEVIVPEGEGGYAMLAAFVQL 4990
Cdd:cd05959    384 --QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVE----SALvQHPAVLEAAVVGVEDEDGLTKPKAFVVL 457
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 4991 GDDTYNT---------LVKEKAGGDSLTVQVVFLDrveeELakrvpehmmlttfftleamPTTTSGKIDRKRLR 5055
Cdd:cd05959    458 RPGYEDSealeeelkeFVKDRLAPYKYPRWIVFVD----EL-------------------PKTATGKIQRFKLR 508
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5655-6136 1.39e-28

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 123.70  E-value: 1.39e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5655 ALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGA----FVPLDPDHPAS--RHEDTFRhtGAQVVVTSAQ 5728
Cdd:cd05922      1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESvlRYLVADA--GGRIVLADAG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5729 HSARWigTNHQVVTVSAGSLGQLSTLV----NPVGLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGIT 5804
Cdd:cd05922     79 AADRL--RDALPASPDPGTVLDADGIRaaraSAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5805 NLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRNDLVKAISTMDVSCALLTPSVARLL-----EPSSVPTLQML 5879
Cdd:cd05922    157 ADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLtrlgfDPAKLPSLRYL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5880 VLQG---EQVSFADWNRWPASVQTINGYGPTECSICCNTYSGKQ-GFKSGIIGTSVASVSWVVDPENHDRLAPlGSIGEL 5955
Cdd:cd05922    237 TQAGgrlPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERiLEKPGSIGLAIPGGEFEILDDDGTPTPP-GEPGEI 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5956 LVEGPILARGYLNDIQktaavfiddpawllegYPGHPGRQGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEV 6035
Cdd:cd05922    316 VHRGPNVMKGYWNDPP----------------YRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEI 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6036 EHHVRECLPEARQLAVEVILPSGQKdhamLAAFVqleegtqnalldkEASGEDSmaqvvfLASVEEELAKRLPEHMVPTV 6115
Cdd:cd05922    380 EAAARSIGLIIEAAAVGLPDPLGEK----LALFV-------------TAPDKID------PKDVLRSLAERLPPYKVPAT 436
                          490       500
                   ....*....|....*....|.
gi 1820002560 6116 FFSLLHFPTTTSGKTDRKRLR 6136
Cdd:cd05922    437 VRVVDELPLTASGKVDYAALR 457
PRK09088 PRK09088
acyl-CoA synthetase; Validated
859-1371 1.58e-28

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 124.15  E-value: 1.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  859 AEQARARPDASAV--CAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGH 936
Cdd:PRK09088     2 AFHARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  937 PASRHEEIFKQIGAQVVLTSSQHAMLFASSERHQVTVSKVSTSQLPTvvnfaKSPVDPGNTAYIIFTSGTTGIPKGVVL- 1015
Cdd:PRK09088    82 SASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADALEPAD-----TPSIPPERVSLILFTSGTSGQPKGVMLs 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1016 ----QHRAVTTSCLGHGEAfgytdHARVLQFAS-YTFDACIAEIITTLLYGGCICVPSESDRRNNLAK-AISTMDVNCAL 1089
Cdd:PRK09088   157 ernlQQTAHNFGVLGRVDA-----HSSFLCDAPmFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRlGDPALGITHYF 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1090 LTPSVARLL------EPSAVPSLKRLVLQGEQVSFADWNRW-PGSVQTINGYGPTEC------SVCCNTYSGKQGfKSGI 1156
Cdd:PRK09088   232 CVPQMAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWlDDGIPMVDGFGMSEAgtvfgmSVDCDVIRAKAG-AAGI 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1157 IGTSVASLswVVDagNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpAWllegyeghagrrgrlYKTGDLVR 1236
Cdd:PRK09088   311 PTPTVQTR--VVD--DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGD-GW---------------FRTGDIAR 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1237 CDADGNLVCLGRKDSQVKVRGQRVELGEIE-----H-HVREC----LPEARQLAVEVILPSGQKEHALLAAfiqldkgnh 1306
Cdd:PRK09088   371 RDADGFFWVVDRKKDMFISGGENVYPAEIEavladHpGIRECavvgMADAQWGEVGYLAIVPADGAPLDLE--------- 441
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 1307 nalfeekasgedsmaqvvfltGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDIGAS 1371
Cdd:PRK09088   442 ---------------------RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
PRK06145 PRK06145
acyl-CoA synthetase; Validated
856-1367 1.87e-28

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 124.23  E-value: 1.87e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  856 DLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPG 935
Cdd:PRK06145     6 ASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  936 HPASRHEEIFKQIGAQVVLTSSQHAMLFA-------SSERHQVTVSKVSTSQLPTVVNFAKSPVDpgnTAYIIFTSGTTG 1008
Cdd:PRK06145    86 LAADEVAYILGDAGAKLLLVDEEFDAIVAletpkivIDAAAQADSRRLAQGGLEIPPQAAVAPTD---LVRLMYTSGTTD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1009 IPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQFAS-YTFDACIAEIITTLLYGGCICVPSESDRRNNLAkAISTMDVNC 1087
Cdd:PRK06145   163 RPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPlYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA-AIERHRLTC 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1088 ALLTP-SVARLLepsAVP--------SLKRLVLQGE---QVSFADWNRWPGSVQTINGYGPTE-CSVCCNTYSGKQGFKS 1154
Cdd:PRK06145   242 AWMAPvMLSRVL---TVPdrdrfdldSLAWCIGGGEktpESRIRDFTRVFTRARYIDAYGLTEtCSGDTLMEAGREIEKI 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1155 GIIGTSVASLSWVVDAGNHNRLAPlGSIGELLVEGPILARGYLNDIDKTEAAFIDDpaWLlegyeghagrrgrlyKTGDL 1234
Cdd:PRK06145   319 GSTGRALAHVEIRIADGAGRWLPP-NMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--WF---------------RSGDV 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1235 VRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQLAVevilpsgqkehallaafiqldKGNHNALFeeka 1314
Cdd:PRK06145   381 GYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYE-LPEVAEAAV---------------------IGVHDDRW---- 434
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1315 sGEDSMAQVVFLTGVEEELA-------KRLPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:PRK06145   435 -GERITAVVVLNPGATLTLEaldrhcrQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
877-1367 2.79e-28

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 122.54  E-value: 2.79e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP--GHPASRHEeiFKQIGAQVVL 954
Cdd:cd05971      6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFAlfGPEALEYR--LSNSGASALV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  955 TSSqhamlfasserhqvtvskvstsqlptvvnfaksPVDPgntAYIIFTSGTTGIPKGVVLQHRAVttscLGHgeafgyt 1034
Cdd:cd05971     84 TDG---------------------------------SDDP---ALIIYTSGTTGPPKGALHAHRVL----LGH------- 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1035 dhARVLQFASYTFD------------ACIAEIITTLL---YGGcicVPSESDRRNNL-AKAISTM----DVNCALLTPSV 1094
Cdd:cd05971    117 --LPGVQFPFNLFPrdgdlywtpadwAWIGGLLDVLLpslYFG---VPVLAHRMTKFdPKAALDLmsryGVTTAFLPPTA 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1095 ARLLEPSAVP------SLKRLVLQGEQV--SFADWNRWPGSVQTINGYGPTECSV----CCNTYSGKQG-FKSGIIGTSV 1161
Cdd:cd05971    192 LKMMRQQGEQlkhaqvKLRAIATGGESLgeELLGWAREQFGVEVNEFYGQTECNLvignCSALFPIKPGsMGKPIPGHRV 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1162 ASLSwvvDAGNHnrlAPLGSIGELLVE--GPILARGYLNDIDKTEAAFIDDpaWLLegyeghagrrgrlykTGDLVRCDA 1239
Cdd:cd05971    272 AIVD---DNGTP---LPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD--WLL---------------TGDLGRKDS 328
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1240 DGNLVCLGRKDSQVKVRGQRVELGEIEhhvrECL---PEARQLAVeVILP---SGQkehaLLAAFIQLDKGnhnalfeek 1313
Cdd:cd05971    329 DGYFWYVGRDDDVITSSGYRIGPAEIE----ECLlkhPAVLMAAV-VGIPdpiRGE----IVKAFVVLNPG--------- 390
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 1314 ASGEDSMAQvvfltGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:cd05971    391 ETPSDALAR-----EIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
876-1367 2.87e-28

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 123.60  E-value: 2.87e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  876 GELTYGELdELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGgaFVPLDPGHPASRHEEI--FKQIGAQVV 953
Cdd:cd05909      6 TSLTYRKL-LTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAGLRELRacIKLAGIKTV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  954 LTSSQ------HAMLFASSE----------RHQVTVS-KVST------SQLPTVVNFAKSPVDPGNTAYIIFTSGTTGIP 1010
Cdd:cd05909     83 LTSKQfieklkLHHLFDVEYdarivyledlRAKISKAdKCKAflagkfPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1011 KGVVLQHRAVTTSCLGHGEAFGYTDHARVLQ----FASYTFDACiaeIITTLLYGGCI-CVPSESDRRnNLAKAISTMDV 1085
Cdd:cd05909    163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGC---LWLPLLSGIKVvFHPNPLDYK-KIPELIYDKKA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1086 NCALLTPS----VARLLEPSAVPSLKRLVLQGEQVSFADWNRWPGS--VQTINGYGPTECS--VCCNTysGKQGFKSGII 1157
Cdd:cd05909    239 TILLGTPTflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSpvISVNT--PQSPNKEGTV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1158 GTSVASLSWVVDAGNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDdpAWllegyeghagrrgrlYKTGDLVRC 1237
Cdd:cd05909    317 GRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD--GW---------------YDTGDIGKI 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1238 DADGNLVCLGRKDSQVKVRGQRVELGEIEHHVRECLPEARQLAVeVILPSGQKEHA--LLAAFIQLDKGNHNALFeeKAS 1315
Cdd:cd05909    380 DGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAV-VSVPDGRKGEKivLLTTTTDTDPSSLNDIL--KNA 456
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 1316 GedsmaqvvfltgveeelakrLPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:cd05909    457 G--------------------ISNLAKPSYIHQVEEIPLLGTGKPDYVTLKA 488
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
3464-3976 2.99e-28

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 124.10  E-value: 2.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3464 HDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAGgaFV 3539
Cdd:COG1021     28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVvvqlPNVAE----FVIVFFALFRAG--AI 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3540 P---LdpdhPASRHEEI---FEQTGAQVVVASAQYS-------ARWTSSSC----HVVTVSKA-----LSSQLPAVVDST 3597
Cdd:COG1021    102 PvfaL----PAHRRAEIshfAEQSEAVAYIIPDRHRgfdyralARELQAEVpslrHVLVVGDAgeftsLDALLAAPADLS 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3598 NTSVRPENAAYIIFTSGSTGVPKGVVLEH-------RAVATSClghgrafGITNLSRVLQF--ASYTFDACIAEIITTLL 3668
Cdd:COG1021    178 EPRPDPDDVAFFQLSGGTTGLPKLIPRTHddylysvRASAEIC-------GLDADTVYLAAlpAAHNFPLSSPGVLGVLY 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3669 CGGCIcVPSDSDRRNSLAKAISTMDVNWAFLTPSVARL------LDPGLIPSLKILAIGGEQSSSADWNR----WPGSVQ 3738
Cdd:COG1021    251 AGGTV-VLAPDPSPDTAFPLIERERVTVTALVPPLALLwldaaeRSRYDLSSLRVLQVGGAKLSPELARRvrpaLGCTLQ 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3739 kiHVYGPTE--CCifctgYT----------TKQGfEPstigtsvasVS-----WVVDPEnhNRLAPLGSMGELLMEGPIL 3801
Cdd:COG1021    330 --QVFGMAEglVN-----YTrlddpeevilTTQG-RP---------ISpddevRIVDED--GNPVPPGEVGELLTRGPYT 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3802 ARGYLNDVDKTEAAFIDDpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREc 3881
Cdd:COG1021    391 IRGYYRAPEHNARAFTPD------GF----------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLA- 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3882 LPEARQLAVeVILPsgqkDHAMlaafvqleegtqnalldkeagGEDSMAQVVF------LASVEEELAKR-LPEHMVPTV 3954
Cdd:COG1021    454 HPAVHDAAV-VAMP----DEYL---------------------GERSCAFVVPrgepltLAELRRFLRERgLAAFKLPDR 507
                          570       580
                   ....*....|....*....|..
gi 1820002560 3955 FFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:COG1021    508 LEFVDALPLTAVGKIDKKALRA 529
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
3471-3971 3.96e-28

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 121.95  E-value: 3.96e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 3550
Cdd:cd17631      5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3551 EEIFEQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVLEHRAVA 3630
Cdd:cd17631     85 AYILADSGAKVLF----------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLL 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3631 TSCLGHGRAFGITNLSRVLQFAS-YTFDACIAEIITTLLCGGCICVPSDSDRRNSLAkAISTMDVNWAFLTPS-VARLLD 3708
Cdd:cd17631    125 WNAVNALAALDLGPDDVLLVVAPlFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLD-LIERHRVTSFFLVPTmIQALLQ 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3709 -PGL----IPSLKILAIGGEQSSSADWNRWPGSVQKIH-VYGPTECCIFCTGYTTKQGFE-PSTIGTSVASVSW-VVDPE 3780
Cdd:cd17631    204 hPRFattdLSSLRAVIYGGAPMPERLLRALQARGVKFVqGYGMTETSPGVTFLSPEDHRRkLGSAGRPVFFVEVrIVDPD 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3781 nhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDS 3860
Cdd:cd17631    284 --GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG--WF---------------HTGDLGRLDEDGYLYIVDRKKD 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3861 QVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHAMlAAFVQLEEGTQnalLDKEAggedsmaqvvFLASVEE 3940
Cdd:cd17631    345 MIISGGENVYPAEVEDVLYE-HPAVAEVAV-IGVPDEKWGEAV-VAVVVPRPGAE---LDEDE----------LIAHCRE 408
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 3941 ELAK-RLPEHmvptVFF--SLlhfPTTTSGKTDR 3971
Cdd:cd17631    409 RLARyKIPKS----VEFvdAL---PRNATGKILK 435
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
1931-2444 3.96e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 123.37  E-value: 3.96e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1931 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 2010
Cdd:PRK06187     8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2011 PDHPASRHEDIFRQTGAQVVVTSAQHS------ARWIGTNHQVVTVSAGSLEQ-------FSTLVN--PVDLPAKP--EN 2073
Cdd:PRK06187    88 IRLKPEEIAYILNDAEDRVVLVDSEFVpllaaiLPQLPTVRTVIVEGDGPAAPlapevgeYEELLAaaSDTFDFPDidEN 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2074 AAYVMF-TSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLRAL----QFTAYTFDVCIAeiitTLVHGGCICVPsdse 2148
Cdd:PRK06187   168 DAAAMLyTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHAWGLPYL----ALMAGAKQVIP---- 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2149 RR---DNLAKAITDMQVN--------W-GYLTSSVARLLDpclVPSLKVLVLGGEQVNstdwgkwPS---------SVQT 2207
Cdd:PRK06187   240 RRfdpENLLDLIETERVTfffavptiWqMLLKAPRAYFVD---FSSLRLVIYGGAALP-------PAllrefkekfGIDL 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2208 INGYGPTECC-VFCTGY----TGIQGFQSGNIGTSIASVSW-VVDPEnhGRLAP--LGSIGELLVEGPILARGYLNDVDK 2279
Cdd:PRK06187   310 VQGYGMTETSpVVSVLPpedqLPGQWTKRRSAGRPLPGVEArIVDDD--GDELPpdGGEVGEIIVRGPWLMQGYWNRPEA 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2280 TQAAFIDDpaWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVE----HHmrkclPEANQ 2355
Cdd:PRK06187   388 TAETIDGG--WL---------------HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEdalyGH-----PAVAE 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2356 LAVEVVP--PSGERDHamlaAFIRLDDETRNSPliikyaednstaqivflTGIEEELSERLPQHMVPtvffALVHF---- 2429
Cdd:PRK06187   446 VAVIGVPdeKWGERPV----AVVVLKPGATLDA-----------------KELRAFLRGRLAKFKLP----KRIAFvdel 500
                          570
                   ....*....|....*
gi 1820002560 2430 PTTTSGKTDRKRLRE 2444
Cdd:PRK06187   501 PRTSVGKILKRVLRE 515
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
857-1365 4.61e-28

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 123.11  E-value: 4.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  857 LFAEQARARP---DASAVCAwdgeLTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLd 933
Cdd:cd05904     13 LFASAHPSRPaliDAATGRA----LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 pgHPASRHEEIFKQI---GAQVVLTSSQhamlfasserhqvTVSKVSTSQLPTVV---------------------NFAK 989
Cdd:cd05904     88 --NPLSTPAEIAKQVkdsGAKLAFTTAE-------------LAEKLASLALPVVLldsaefdslsfsdllfeadeaEPPV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  990 SPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGH--GEAFGYTDHARVL----QFASYTFDACiaeIITTLLYGGC 1063
Cdd:cd05904    153 VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFvaGEGSNSDSEDVFLcvlpMFHIYGLSSF---ALGLLRLGAT 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1064 ICVPSESDRRNNLAkAISTMDVNCALLTPSV------ARLLEPSAVPSLKRLV-----LQGE-QVSFADwnRWPgSVQTI 1131
Cdd:cd05904    230 VVVMPRFDLEELLA-AIERYKVTHLPVVPPIvlalvkSPIVDKYDLSSLRQIMsgaapLGKElIEAFRA--KFP-NVDLG 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1132 NGYGPTE----CSVCCNTysGKQGFKSGIIGTSVASL-SWVVDAgNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAA 1206
Cdd:cd05904    306 QGYGMTEstgvVAMCFAP--EKDRAKYGSVGRLVPNVeAKIVDP-ETGESLPPNQTGELWIRGPSIMKGYLNNPEATAAT 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1207 fIDDPAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhhvreclpearqlAVEVILP 1286
Cdd:cd05904    383 -IDKEGWL---------------HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELE-------------ALLLSHP 433
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1287 SgqkehALLAAFIQldkgnhnalFEEKASGEDSMAQVV-----FLTGVE--EELAKRL-PEHMVPTILFtVKAMPITTSG 1358
Cdd:cd05904    434 E-----ILDAAVIP---------YPDEEAGEVPMAFVVrkpgsSLTEDEimDFVAKQVaPYKKVRKVAF-VDAIPKSPSG 498

                   ....*..
gi 1820002560 1359 KIDRKRL 1365
Cdd:cd05904    499 KILRKEL 505
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
4545-5056 5.36e-28

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 123.32  E-value: 5.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4545 DQFAEQARARPDTPAICAWDG-ELTYGELDTLSSKLASHLVQLGVKPEDMVplCFEKSMWT--VVAMLAVLKAGGAFVPL 4621
Cdd:PRK06087    27 DYWQQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRV--AFQLPGWCefTIIYLACLKVGAVSVPL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4622 DPDHPASRHEHIFRQTGAQVVLASAQYATL------------WTSLGRSVVIVSEASTSQLPVVTK--------TADPSV 4681
Cdd:PRK06087   105 LPSWREAELVWVLNKCQAKMFFAPTLFKQTrpvdlilplqnqLPQLQQIVGVDKLAPATSSLSLSQiiadyeplTTAITT 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4682 NPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRV-----LQFASYTFDACIAEIITtllccGCICVP 4756
Cdd:PRK06087   185 HGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFmmpapLGHATGFLHGVTAPFLI-----GARSVL 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4757 SDSDRRNNLAKAINAMDVNWAL-LTPSVARML-----DPCVVQSLKILVLGGEQVNS-ADWDRWPKSIQTINAYGPTECS 4829
Cdd:PRK06087   260 LDIFTPDACLALLEQQRCTCMLgATPFIYDLLnllekQPADLSALRFFLCGGTTIPKkVARECQQRGIKLLSVYGSTESS 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4830 IC-------CTTYSGkqgfksGTIGTSIVSVSW-VVDpENHNRLaPLGSIGELLVEGPILARGYLNDMEKTEAAfIDDPA 4901
Cdd:PRK06087   340 PHavvnlddPLSRFM------HTDGYAAAGVEIkVVD-EARKTL-PPGCEGEEASRGPNVFMGYLDEPELTARA-LDEEG 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4902 WllegygghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREClTEAKQLAVeVIVPE---GE 4978
Cdd:PRK06087   411 W---------------YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQH-PKIHDACV-VAMPDerlGE 473
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 4979 ggyaMLAAFVQLgddtyntlvkeKAGGDSLTVQVVFLDRVEEELAKRV-PEHMMlttffTLEAMPTTTSGKIDRKRLRE 5056
Cdd:PRK06087   474 ----RSCAYVVL-----------KAPHHSLTLEEVVAFFSRKRVAKYKyPEHIV-----VIDKLPRTASGKIQKFLLRK 532
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
3465-3975 6.37e-28

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 122.48  E-value: 6.37e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 3544
Cdd:cd05959      8 LVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3545 HPASRHEEIFEQTGAQVVVASAQYSARWTS-------SSCHVVTVSKA--------LSSQLPAVVDSTNT-SVRPENAAY 3608
Cdd:cd05959     88 LTPDDYAYYLEDSRARVVVVSGELAPVLAAaltksehTLVVLIVSGGAgpeagallLAELVAAEAEQLKPaATHADDPAF 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3609 IIFTSGSTGVPKGVVLEHRAVATSCLGHGR-AFGITNLSRVLQ-----FA-----SYTFDACIAEiiTTLLCGGcicVPS 3677
Cdd:cd05959    168 WLYSSGSTGRPKGVVHLHADIYWTAELYARnVLGIREDDVCFSaaklfFAyglgnSLTFPLSVGA--TTVLMPE---RPT 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3678 DSdrrnSLAKAISTMDVNWAFLTPSV--ARLLDPGL----IPSLKILAIGGEQSSSADWNRWP-----------GSVQKI 3740
Cdd:cd05959    243 PA----AVFKRIRRYRPTVFFGVPTLyaAMLAAPNLpsrdLSSLRLCVSAGEALPAEVGERWKarfgldildgiGSTEML 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3741 HvygpteccIFCTgyTTKQGFEPSTIGTSVASVSW-VVDPENHNrlAPLGSMGELLMEGPILARGYLNDVDKTEAAFidd 3819
Cdd:cd05959    319 H--------IFLS--NRPGRVRYGTTGKPVPGYEVeLRDEDGGD--VADGEPGELYVRGPSSATMYWNNRDKTRDTF--- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3820 pawllegypghpgrQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvrECL---PEARQLAVeviLPS 3896
Cdd:cd05959    384 --------------QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVE----SALvqhPAVLEAAV---VGV 442
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3897 GQKDHAM-LAAFVQLEEGTQ-NALLDKEaggedsmaqvvflasVEEELAKRLPEHMVP--TVFFSLLhfPTTTSGKTDRK 3972
Cdd:cd05959    443 EDEDGLTkPKAFVVLRPGYEdSEALEEE---------------LKEFVKDRLAPYKYPrwIVFVDEL--PKTATGKIQRF 505

                   ...
gi 1820002560 3973 RLR 3975
Cdd:cd05959    506 KLR 508
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
7624-8121 9.50e-28

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 121.03  E-value: 9.50e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7624 PAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQT 7703
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7704 GAQVVVASAqysarwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHG 7783
Cdd:cd05919     82 EARLVVTSA-------------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7784 R-AFGITNLSRVLQFASYTFDACIA-EIITTLLCGG-CICVPSDSDRRNSLAKAistmdvnwAFLTPSV--------ARL 7852
Cdd:cd05919    125 ReALGLTPGDRVFSSAKMFFGYGLGnSLWFPLAVGAsAVLNPGWPTAERVLATL--------ARFRPTVlygvptfyANL 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7853 LDPGLIP-----SLKILAIGGEQSSSADWNRWP--GSVQKIHVYGPTEccIFCTGYTTKQGfePSTIGTSVASVSW---- 7921
Cdd:cd05919    197 LDSCAGSpdalrSLRLCVSAGEALPRGLGERWMehFGGPILDGIGATE--VGHIFLSNRPG--AWRLGSTGRPVPGyeir 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7922 VVDPENHNrlAPLGSMGELLMEGPILARGYLNDVDKTEAAFiddpawllegypghpgrQGRLYKTGDLVQYNADGNLVYL 8001
Cdd:cd05919    273 LVDEEGHT--IPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-----------------NGGWYRTGDKFCRDADGWYTHA 333
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8002 GRKDSQVKVRGQRVELGEVEHHVreCLPEARQLAVEVILPSGQKnhamlavfvqLGKGTHIAHLEEKAGGEDSMAQVVfl 8081
Cdd:cd05919    334 GRADDMLKVGGQWVSPVEVESLI--IQHPAVAEAAVVAVPESTG----------LSRLTAFVVLKSPAAPQESLARDI-- 399
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 8082 tgtEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLR 8121
Cdd:cd05919    400 ---HRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
7617-8117 1.07e-27

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 120.79  E-value: 1.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 7696
Cdd:cd17631      5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7697 EEIFEQTGAQVVVasaqysarwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVLEHRAVA 7776
Cdd:cd17631     85 AYILADSGAKVLF----------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLL 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7777 TSCLGHGRAFGITNLSRVLQFAS-YTFDACIAEIITTLLCGGCICVPSDSDRRNSLAkAISTMDVNWAFLTPS-VARLLD 7854
Cdd:cd17631    125 WNAVNALAALDLGPDDVLLVVAPlFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLD-LIERHRVTSFFLVPTmIQALLQ 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7855 -PGL----IPSLKILAIGGEQSSSADWNRWPGSVQKIH-VYGPTECCIFCTGYTTKQGFE-PSTIGTSVASVSW-VVDPE 7926
Cdd:cd17631    204 hPRFattdLSSLRAVIYGGAPMPERLLRALQARGVKFVqGYGMTETSPGVTFLSPEDHRRkLGSAGRPVFFVEVrIVDPD 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7927 nhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDS 8006
Cdd:cd17631    284 --GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG--WF---------------HTGDLGRLDEDGYLYIVDRKKD 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8007 QVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKNHAMLAVFVQlgkgthiahleeKAGGEDSMAQVVfltgteE 8086
Cdd:cd17631    345 MIISGGENVYPAEVEDVLYE-HPAVAEVAV-IGVPDEKWGEAVVAVVVP------------RPGAELDEDELI------A 404
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 8087 ELAKRLPKHMVP-TVFF--ALlhfPMTTSGKADR 8117
Cdd:cd17631    405 HCRERLARYKIPkSVEFvdAL---PRNATGKILK 435
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
851-1365 1.20e-27

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 122.18  E-value: 1.20e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  851 DRCIHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVV----PLCFEksmwTVVAMLAVLKAG 926
Cdd:COG1021     24 GETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVvvqlPNVAE----FVIVFFALFRAG 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  927 GAFVPLDPGHpasRHEEI---FKQIGAQVVLTSSQHAmLFA------------SSERHQVTV----SKVSTSQLPTV-VN 986
Cdd:COG1021    100 AIPVFALPAH---RRAEIshfAEQSEAVAYIIPDRHR-GFDyralarelqaevPSLRHVLVVgdagEFTSLDALLAApAD 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  987 FAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQF--ASYTFDACIAEIITTLLYGGCI 1064
Cdd:COG1021    176 LSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAAlpAAHNFPLSSPGVLGVLYAGGTV 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1065 cVPSESDRRNNLAKAISTMDVNCALLTPSVARL------LEPSAVPSLKRLVLQGEQVSFADWNR----WPGSVQTIngY 1134
Cdd:COG1021    256 -VLAPDPSPDTAFPLIERERVTVTALVPPLALLwldaaeRSRYDLSSLRVLQVGGAKLSPELARRvrpaLGCTLQQV--F 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1135 GPTECSVCC-----------NTysgkqgfksgiIGTSVASLS--WVVDAgnHNRLAPLGSIGELLVEGPILARGYLNDID 1201
Cdd:COG1021    333 GMAEGLVNYtrlddpeevilTT-----------QGRPISPDDevRIVDE--DGNPVPPGEVGELLTRGPYTIRGYYRAPE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1202 KTEAAFIDDpawlleGYeghagrrgrlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQLAV 1281
Cdd:COG1021    400 HNARAFTPD------GF----------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLA-HPAVHDAAV 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1282 eVILPS---GQKEHallaAFIQLDkgnhnalfeekasGED-SMAQVV-FLTgvEEELAK-RLPEHMVptilfTVKAMPIT 1355
Cdd:COG1021    463 -VAMPDeylGERSC----AFVVPR-------------GEPlTLAELRrFLR--ERGLAAfKLPDRLE-----FVDALPLT 517
                          570
                   ....*....|
gi 1820002560 1356 TSGKIDRKRL 1365
Cdd:COG1021    518 AVGKIDKKAL 527
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
5625-6137 1.22e-27

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 122.18  E-value: 1.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5625 HDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMV----PLCFEksmwTVVAMLAVLKAGGAFV 5700
Cdd:COG1021     28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVvvqlPNVAE----FVIVFFALFRAGAIPV 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5701 PLDPDHpaSRHEDT--FRHTGAQVVVTSAQHS------------ARWIGTNHQVVTVSAGSLGQLSTLVN-PVGL--PAI 5763
Cdd:COG1021    104 FALPAH--RRAEIShfAEQSEAVAYIIPDRHRgfdyralarelqAEVPSLRHVLVVGDAGEFTSLDALLAaPADLsePRP 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5764 PENAVYIMFTS-GSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQF--ASYTFDACMDEIITTLMYGGCIcVPSDS 5840
Cdd:COG1021    182 DPDDVAFFQLSgGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAAlpAAHNFPLSSPGVLGVLYAGGTV-VLAPD 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5841 DRRNDLVKAISTMDVSCALLTPSVARL------LEPSSVPTLQMLVLQGEQVSFADWNR----WPASVQTIngYGPTECS 5910
Cdd:COG1021    261 PSPDTAFPLIERERVTVTALVPPLALLwldaaeRSRYDLSSLRVLQVGGAKLSPELARRvrpaLGCTLQQV--FGMAEGL 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5911 ICC-----------NTysgkQGfksgiigtsvASVS-----WVVDPEnhDRLAPLGSIGELLVEGPILARGYLNDIQKTA 5974
Cdd:COG1021    339 VNYtrlddpeevilTT----QG----------RPISpddevRIVDED--GNPVPPGEVGELLTRGPYTIRGYYRAPEHNA 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5975 AVFIDDpawlleGYpghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAVeVI 6054
Cdd:COG1021    403 RAFTPD------GF----------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLA-HPAVHDAAV-VA 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6055 LPsgqkDHAMlaafvqleegtqnalldkeasGEDSMAQVVF------LASVEEELAKR-LPEHMVPTVFFSLLHFPTTTS 6127
Cdd:COG1021    465 MP----DEYL---------------------GERSCAFVVPrgepltLAELRRFLRERgLAAFKLPDRLEFVDALPLTAV 519
                          570
                   ....*....|
gi 1820002560 6128 GKTDRKRLRE 6137
Cdd:COG1021    520 GKIDKKALRA 529
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
5626-6136 1.26e-27

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 121.71  E-value: 1.26e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 5705
Cdd:cd05959      8 LVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5706 HPASRHEDTFRHTGAQVVVTSA------QHSARWIGTNHQVVTVSAGSLGQLSTLV--------NPVGLPAI--PENAVY 5769
Cdd:cd05959     88 LTPDDYAYYLEDSRARVVVVSGelapvlAAALTKSEHTLVVLIVSGGAGPEAGALLlaelvaaeAEQLKPAAthADDPAF 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 IMFTSGSTGIPKGVVLEHRAVVTSC--WGRgRAFGITNLSRVLQ----FASYTF-DAC---MDEIITTLMYGGCICVPSD 5839
Cdd:cd05959    168 WLYSSGSTGRPKGVVHLHADIYWTAelYAR-NVLGIREDDVCFSaaklFFAYGLgNSLtfpLSVGATTVLMPERPTPAAV 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5840 SDR----RNDLVKAISTMdvSCALLTPSVARLLEPSSvptLQMLVLQGEQVSFADWNRWPA--SVQTINGYGPTEC-SIC 5912
Cdd:cd05959    247 FKRirryRPTVFFGVPTL--YAAMLAAPNLPSRDLSS---LRLCVSAGEALPAEVGERWKArfGLDILDGIGSTEMlHIF 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5913 CNTYSGKqgFKSGIIGTSVASVSW-VVDPENHDrlAPLGSIGELLVEGPILARGYLNDIQKTAAVFiddpawllegypgh 5991
Cdd:cd05959    322 LSNRPGR--VRYGTTGKPVPGYEVeLRDEDGGD--VADGEPGELYVRGPSSATMYWNNRDKTRDTF-------------- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5992 pgrQGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECL---PEARQLAVeviLPSGQKDHAM-LAA 6067
Cdd:cd05959    384 ---QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVE----SALvqhPAVLEAAV---VGVEDEDGLTkPKA 453
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 6068 FVQLEEGTQnallDKEASGEDsmaqvvflasVEEELAKRLPEHMVP--TVFFSLLhfPTTTSGKTDRKRLR 6136
Cdd:cd05959    454 FVVLRPGYE----DSEALEEE----------LKEFVKDRLAPYKYPrwIVFVDEL--PKTATGKIQRFKLR 508
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1962-2443 1.40e-27

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 120.62  E-value: 1.40e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1962 ALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGA----FVPLDPDHPASRHEDIFRQTGAQVVVTSAQHS 2037
Cdd:cd05922      1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2038 AR----WIGTNHQVVTVSAGSLEQFSTLVNPVdlPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNL 2113
Cdd:cd05922     81 DRlrdaLPASPDPGTVLDADGIRAARASAPAH--EVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2114 LRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRDNLAKAITDMQVN--------WGYLTssvaRL-LDPCLVPSLK 2184
Cdd:cd05922    159 DRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATglagvpstYAMLT----RLgFDPAKLPSLR 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2185 VLVLGGeqvnstdwGKWPSSV-----------QTINGYGPTECCVFCTGYTGIQ-GFQSGNIGTSIASVSWVVDPENHGR 2252
Cdd:cd05922    235 YLTQAG--------GRLPQETiarlrellpgaQVYVMYGQTEATRRMTYLPPERiLEKPGSIGLAIPGGEFEILDDDGTP 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2253 LAPlGSIGELLVEGPILARGYLNDvdktqaafiddpawllEGYPGHEGRQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKV 2332
Cdd:cd05922    307 TPP-GEPGEIVHRGPNVMKGYWND----------------PPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKL 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2333 RGQRVELGEVEHHMRKCLPEANQLAVEVVPPSGERdhamLAAFIRLDDETRNSPLIIKyaednstaqivfltgieeeLSE 2412
Cdd:cd05922    370 FGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEK----LALFVTAPDKIDPKDVLRS-------------------LAE 426
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1820002560 2413 RLPQHMVPTVFFALVHFPTTTSGKTDRKRLR 2443
Cdd:cd05922    427 RLPPYKVPATVRVVDELPLTASGKVDYAALR 457
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
5599-6137 1.64e-27

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 122.42  E-value: 1.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5599 ETTTLEDRQQLWAWNQNVPPAIE---RCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMV 5675
Cdd:PRK05605     6 EMSAFADKPWLQSYAPWTPHDLDygdTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5676 PLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVV---TSAQHSARWIGTN--HQVVTV------- 5743
Cdd:PRK05605    86 AIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIvwdKVAPTVERLRRTTplETIVSVnmiaamp 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5744 ----------------------------------SAGSLGQLSTLVNPvglPAI-PENAVYIMFTSGSTGIPKGVVLEHR 5788
Cdd:PRK05605   166 llqrlalrlpipalrkaraaltgpapgtvpwetlVDAAIGGDGSDVSH---PRPtPDDVALILYTSGTTGKPKGAQLTHR 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5789 AVVTSC-----W----GRGR-----------AFGITnlsRVLQFASY---------TFDacMDEIIT-------TLMYGg 5832
Cdd:PRK05605   243 NLFANAaqgkaWvpglGDGPervlaalpmfhAYGLT---LCLTLAVSiggelvllpAPD--IDLILDamkkhppTWLPG- 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5833 cicVPSDSDRrndLVKAISTMDVSCALLTPSV--ARLLEPSSVptlqmlvlqgeqvsfadwNRWPASV--QTINGYGPTE 5908
Cdd:PRK05605   317 ---VPPLYEK---IAEAAEERGVDLSGVRNAFsgAMALPVSTV------------------ELWEKLTggLLVEGYGLTE 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5909 CS--ICCNTYSGKQgfKSGIIG-----TSVAsvswVVDPENHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDp 5981
Cdd:PRK05605   373 TSpiIVGNPMSDDR--RPGYVGvpfpdTEVR----IVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG- 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5982 aWllegypghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKD 6061
Cdd:PRK05605   446 -W---------------FRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLRE-HPGVEDAAV-VGLPREDGS 507
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6062 HAMLAAFVqLEEGtqnALLDKEAsgedsmaqvvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:PRK05605   508 EEVVAAVV-LEPG---AALDPEG--------------LRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
885-1365 1.84e-27

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 120.24  E-value: 1.84e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  885 ELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGA----FVPLDPGHPASRHEEIFKQIGAQVVLTSSQHA 960
Cdd:cd05922      1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  961 MLFASSerhqvtvskVSTSQLPTVV-----------NFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGE 1029
Cdd:cd05922     81 DRLRDA---------LPASPDPGTVldadgiraaraSAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1030 AFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNNLAKAISTMDVNCALLTPSVARLL-----EPSAVP 1104
Cdd:cd05922    152 YLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLtrlgfDPAKLP 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1105 SLKRLVLQGEQVSFADWNRW----PGSvQTINGYGPTECSVCCNTYSGKQ-GFKSGIIGTSVASLSWVVDAGNHNRLAPl 1179
Cdd:cd05922    232 SLRYLTQAGGRLPQETIARLrellPGA-QVYVMYGQTEATRRMTYLPPERiLEKPGSIGLAIPGGEFEILDDDGTPTPP- 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1180 GSIGELLVEGPILARGYLNDidkteaafiddpawllEGYEGHAGRRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQR 1259
Cdd:cd05922    310 GEPGEIVHRGPNVMKGYWND----------------PPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNR 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1260 VELGEIEHHVRECLPEARQLAVEVILPSGQKEHALLAAfiqldkgnhnalfeeKASGEDSMAQVVfltgveeeLAKRLPE 1339
Cdd:cd05922    374 ISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTA---------------PDKIDPKDVLRS--------LAERLPP 430
                          490       500
                   ....*....|....*....|....*.
gi 1820002560 1340 HMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd05922    431 YKVPATVRVVDELPLTASGKVDYAAL 456
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
7633-8092 2.05e-27

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 120.01  E-value: 2.05e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASA 7712
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7713 qysarwtssschvvtvskalssqlpavvdstntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLS 7792
Cdd:cd05907     86 ------------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7793 RVLQF--ASYTFdACIAEIITTLLCGGCICVPSDSDRrnsLAKAISTMDVNWAFLTPSV-----------------ARLL 7853
Cdd:cd05907    130 RHLSFlpLAHVF-ERRAGLYVPLLAGARIYFASSAET---LLDDLSEVRPTVFLAVPRVwekvyaaikvkavpglkRKLF 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7854 DPGLIPSLKILAIGGeQSSSADWNRWpgsVQKIHV-----YGPTECCIFCTgYTTKQGFEPSTIGTSVasvswvvdPENH 7928
Cdd:cd05907    206 DLAVGGRLRFAASGG-APLPAELLHF---FRALGIpvyegYGLTETSAVVT-LNPPGDNRIGTVGKPL--------PGVE 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7929 NRLAPlgsMGELLMEGPILARGYLNDVDKTEAAFIDDPaWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGR-KDSQ 8007
Cdd:cd05907    273 VRIAD---DGEILVRGPNVMLGYYKNPEATAEALDADG-WL---------------HTGDLGEIDEDGFLHITGRkKDLI 333
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8008 VKVRGQRVELGEVEHHVREClpearqLAVEVILPSGQKnHAMLAVFVQLGKGTHIAHLEEKAGGEDSMAQVVFLTGTEEE 8087
Cdd:cd05907    334 ITSGGKNISPEPIENALKAS------PLISQAVVIGDG-RPFLVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRAE 406

                   ....*
gi 1820002560 8088 LAKRL 8092
Cdd:cd05907    407 IEAAV 411
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3486-3975 2.14e-27

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 119.84  E-value: 2.14e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3486 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPdhpasrheeIFEQTGAQVVVAS 3565
Cdd:cd05971      6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFA---------LFGPEALEYRLSN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3566 AQYSArwtssschVVTvskalssqlpavvDSTNtsvrpeNAAYIIFTSGSTGVPKGVVLEHRAVatscLGHgrafgITNL 3645
Cdd:cd05971     77 SGASA--------LVT-------------DGSD------DPALIIYTSGTTGPPKGALHAHRVL----LGH-----LPGV 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3646 SRVLQFASYTFD--------ACIAEIITTLLCGGCICVPSDSDRRNSL-AKAISTM----DVNWAFLTPSVARLL----D 3708
Cdd:cd05971    121 QFPFNLFPRDGDlywtpadwAWIGGLLDVLLPSLYFGVPVLAHRMTKFdPKAALDLmsryGVTTAFLPPTALKMMrqqgE 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3709 PGLIPSLKILAI--GGEQ--SSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPSTIGTSV-ASVSWVVDpENHN 3783
Cdd:cd05971    201 QLKHAQVKLRAIatGGESlgEELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIpGHRVAIVD-DNGT 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3784 RLAPlGSMGELLME--GPILARGYLNDVDKTEAAFIDDpaWLLegypghpgrqgrlykTGDLVQYNADGNLVYLGRKDSQ 3861
Cdd:cd05971    280 PLPP-GEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD--WLL---------------TGDLGRKDSDGYFWYVGRDDDV 341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3862 VKVRGQRVELGEVEhhvrECL---PEARQLAVeVILP---SGQkdhaMLAAFVQLEEGTqnalldkeaGGEDSMAqvvfl 3935
Cdd:cd05971    342 ITSSGYRIGPAEIE----ECLlkhPAVLMAAV-VGIPdpiRGE----IVKAFVVLNPGE---------TPSDALA----- 398
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 3936 ASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd05971    399 REIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
879-1365 2.37e-27

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 119.48  E-value: 2.37e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  879 TYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSq 958
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  959 hamLFASSERHQVTVSKVSTSQLPTVVNFAKSPVDpgNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHAR 1038
Cdd:TIGR01923   80 ---LLEEKDFQADSLDRIEAAGRYETSLSASFNMD--QIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDN 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1039 VLQFASYTFDACIAEIITTLLYGGCICVPsesDRRNNLAKAISTMDVNCALLTPS-VARLLEPSAVP-SLKRLVLQGEQV 1116
Cdd:TIGR01923  155 WLLSLPLYHISGLSILFRWLIEGATLRIV---DKFNQLLEMIANERVTHISLVPTqLNRLLDEGGHNeNLRKILLGGSAI 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1117 SF-----ADWNRWPgsvqTINGYGPTE-CSVCCnTYSGKQGFKSGIIGTSVASLSWVVdagnhnRLAPLGSIGELLVEGP 1190
Cdd:TIGR01923  232 PAplieeAQQYGLP----IYLSYGMTEtCSQVT-TATPEMLHARPDVGRPLAGREIKI------KVDNKEGHGEIMVKGA 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1191 ILARGYLNDIDKTEAafIDDPAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVR 1270
Cdd:TIGR01923  301 NLMKGYLYQGELTPA--FEQQGWF---------------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLY 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1271 EcLPEARQLAVeviLPS-----GQKEHallaAFIQLDKGnhnalfEEKASGEDSmaqvvfltgveeeLAKRLPEHMVPTI 1345
Cdd:TIGR01923  364 Q-HPGIQEAVV---VPKpdaewGQVPV----AYIVSESD------ISQAKLIAY-------------LTEKLAKYKVPIA 416
                          490       500
                   ....*....|....*....|
gi 1820002560 1346 LFTVKAMPITTSGKIDRKRL 1365
Cdd:TIGR01923  417 FEKLDELPYNASGKILRNQL 436
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
869-1366 2.67e-27

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 119.49  E-value: 2.67e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  869 SAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIfkqi 948
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYI---- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  949 gaqvvLTSSQHAMLFASSErhqvtvskvstsqlptvvnfakspvdpgNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHG 1028
Cdd:cd05919     78 -----ARDCEARLVVTSAD----------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1029 -EAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICV-----PSESDRRNNLAKAISTMDVNCALLTPSVARL--LEP 1100
Cdd:cd05919    125 rEALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVlnpgwPTAERVLATLARFRPTVLYGVPTFYANLLDScaGSP 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1101 SAVPSLKRLVLQGEQVSFADWNRWP--GSVQTINGYGPTEcsVCCNTYSGKQG-FKSGIIGTSV--ASLSWVVDAGNHnr 1175
Cdd:cd05919    205 DALRSLRLCVSAGEALPRGLGERWMehFGGPILDGIGATE--VGHIFLSNRPGaWRLGSTGRPVpgYEIRLVDEEGHT-- 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1176 lAPLGSIGELLVEGPILARGYLNDIDKTEAAFiddpawllegyeghagrRGRLYKTGDLVRCDADGNLVCLGRKDSQVKV 1255
Cdd:cd05919    281 -IPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-----------------NGGWYRTGDKFCRDADGWYTHAGRADDMLKV 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1256 RGQRVELGEIEHHVreCLPEARQLAVEVILPSGqkeHAL--LAAFIQLDKG--NHNALFEEkasgedsmaqvvfltgVEE 1331
Cdd:cd05919    343 GGQWVSPVEVESLI--IQHPAVAEAAVVAVPES---TGLsrLTAFVVLKSPaaPQESLARD----------------IHR 401
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1820002560 1332 ELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQ 1366
Cdd:cd05919    402 HLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
864-1367 2.97e-27

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 120.49  E-value: 2.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  864 ARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEE 943
Cdd:cd05926      1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  944 IFKQIGAQVVLTSSQH---AMLFASSER-------HQVTVSKV--STSQLP-----TVVNFAKSPVDPGNTAYIIFTSGT 1006
Cdd:cd05926     81 YLADLGSKLVLTPKGElgpASRAASKLGlailelaLDVGVLIRapSAESLSnlladKKNAKSEGVPLPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1007 TGIPKGVVLQHRAVTTSCLGHGEAFGYTDHAR---VLQFasYTFDACIAEIITTLLYGGCICVPSE-------SDRRNNL 1076
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRtlvVMPL--FHVHGLVASLLSTLAAGGSVVLPPRfsastfwPDVRDYN 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1077 A---KAISTMdvNCALLTPSVARLLEP--------SAVPSLKRLVLQGEQVSFAdwnrwpgsVQTINGYGPTECS--VCC 1143
Cdd:cd05926    239 AtwyTAVPTI--HQILLNRPEPNPESPppklrfirSCSASLPPAVLEALEATFG--------APVLEAYGMTEAAhqMTS 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1144 NTY-SGKQGFKSGIIGTSVAslswVVDAGNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPaWLlegyegha 1222
Cdd:cd05926    309 NPLpPGPRKPGSVGKPVGVE----VRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG-WF-------- 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1223 grrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREClpEARQLAVEVILPsgqkeHALL----AAF 1298
Cdd:cd05926    376 -------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH--PAVLEAVAFGVP-----DEKYgeevAAA 441
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 1299 IQLdKGNHNALFEEkasgedsmaqvvfltgVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:cd05926    442 VVL-REGASVTEEE----------------LRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
1937-2444 3.55e-27

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 120.39  E-value: 3.55e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1937 EQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 2016
Cdd:PRK07656    13 RAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2017 RHEDIFRQTGAQVVVT---------SAQHSarwIGTNHQVVTVSAGSLEQ-------FSTLVNPVDLPA-----KPENAA 2075
Cdd:PRK07656    93 EAAYILARGDAKALFVlglflgvdySATTR---LPALEHVVICETEEDDPhtekmktFTDFLAAGDPAErapevDPDDVA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2076 YVMFTSGSTGTPKGVVLEHRavvtsclghgqafgvtNLLRALQFTAYTFD-------VCI----------AEIITTLVHG 2138
Cdd:PRK07656   170 DILFTSGTTGRPKGAMLTHR----------------QLLSNAADWAEYLGltegdryLAAnpffhvfgykAGVNAPLMRG 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2139 GCIcVPSDSERRDNLAKAITDMQVN--------WGYLTSSVARllDPCLVPSLKVLVLGG--------EQVNSTdwgkwp 2202
Cdd:PRK07656   234 ATI-LPLPVFDPDEVFRLIETERITvlpgpptmYNSLLQHPDR--SAEDLSSLRLAVTGAasmpvallERFESE------ 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2203 SSVQTI-NGYGPTECCvfctGYTGIQGF------QSGNIGTSIASVSW-VVDPenHGRLAPLGSIGELLVEGPILARGYL 2274
Cdd:PRK07656   305 LGVDIVlTGYGLSEAS----GVTTFNRLdddrktVAGTIGTAIAGVENkIVNE--LGEEVPVGEVGELLVRGPNVMKGYY 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2275 NDVDKTQAAfIDDPAWLlegypgHegrqgrlykTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVE-----Hhmrkc 2349
Cdd:PRK07656   379 DDPEATAAA-IDADGWL------H---------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEevlyeH----- 437
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2350 lPEANQLAVEVVPP--SGERDHAMLAA--FIRLDDETrnsplIIKYAEdnstaqivfltgieeelsERLPQHMVPTVFFA 2425
Cdd:PRK07656   438 -PAVAEAAVIGVPDerLGEVGKAYVVLkpGAELTEEE-----LIAYCR------------------EHLAKYKVPRSIEF 493
                          570
                   ....*....|....*....
gi 1820002560 2426 LVHFPTTTSGKTDRKRLRE 2444
Cdd:PRK07656   494 LDELPKNATGKVLKRALRE 512
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
7632-8121 3.59e-27

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 119.07  E-value: 3.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7632 ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPdhpasrheeIFEQTGAQVVVAS 7711
Cdd:cd05971      6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFA---------LFGPEALEYRLSN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7712 AQYSArwtssschVVTvskalssqlpavvDSTNtsvrpeNAAYIIFTSGSTGVPKGVVLEHRAVatscLGHgrafgITNL 7791
Cdd:cd05971     77 SGASA--------LVT-------------DGSD------DPALIIYTSGTTGPPKGALHAHRVL----LGH-----LPGV 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7792 SRVLQFASYTFD--------ACIAEIITTLLCGGCICVPSDSDRRNSL-AKAISTM----DVNWAFLTPSVARLL----D 7854
Cdd:cd05971    121 QFPFNLFPRDGDlywtpadwAWIGGLLDVLLPSLYFGVPVLAHRMTKFdPKAALDLmsryGVTTAFLPPTALKMMrqqgE 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7855 PGLIPSLKILAI--GGEQ--SSSADWNRWPGSVQKIHVYGPTECCIFCTGYTTKQGFEPSTIGTSV-ASVSWVVDpENHN 7929
Cdd:cd05971    201 QLKHAQVKLRAIatGGESlgEELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIpGHRVAIVD-DNGT 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7930 RLAPlGSMGELLME--GPILARGYLNDVDKTEAAFIDDpaWLLegypghpgrqgrlykTGDLVQYNADGNLVYLGRKDSQ 8007
Cdd:cd05971    280 PLPP-GEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD--WLL---------------TGDLGRKDSDGYFWYVGRDDDV 341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8008 VKVRGQRVELGEVEhhvrECL---PEARQLAVeVILPSGQKNHAMLAvFVqlgkgthiaHLEEKAGGEDSMAQVVfltgt 8084
Cdd:cd05971    342 ITSSGYRIGPAEIE----ECLlkhPAVLMAAV-VGIPDPIRGEIVKA-FV---------VLNPGETPSDALAREI----- 401
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1820002560 8085 EEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLR 8121
Cdd:cd05971    402 QELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
1933-2442 4.77e-27

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 119.74  E-value: 4.77e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAGGAFVP 2008
Cdd:cd05920     19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVvvqlPNVAE----FVVLFFALLRLGAVPVL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2009 LDPDHPASRHEDIFRQTGAQVVVTSAQHSarwiGTNHQvvtvsagslEQFstlvnpVDLPAKPENAAYVMFTSGSTGTPK 2088
Cdd:cd05920     95 ALPSHRRSELSAFCAHAEAVAYIVPDRHA----GFDHR---------ALA------RELAESIPEVALFLLSGGTTGTPK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2089 GVVLEH-------RAVVTSClGHGQAfgvTNLLRALQfTAYTFDVCIAEIITTLVHGGCIcVPSDSERRDNLAKAITDMQ 2161
Cdd:cd05920    156 LIPRTHndyaynvRASAEVC-GLDQD---TVYLAVLP-AAHNFPLACPGVLGTLLAGGRV-VLAPDPSPDAAFPLIEREG 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2162 VNWGYLTSSVARL-LDPCL-----VPSLKVLVLGGEQVNSTDWGKWPS----SVQTIngYGPTECCVfctGYTGIQGFQS 2231
Cdd:cd05920    230 VTVTALVPALVSLwLDAAAsrradLSSLRLLQVGGARLSPALARRVPPvlgcTLQQV--FGMAEGLL---NYTRLDDPDE 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2232 GNIGTSIASVS-----WVVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpawlleGYpghegrqgrlY 2306
Cdd:cd05920    305 VIIHTQGRPMSpddeiRVVDEE--GNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPD------GF----------Y 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2307 KTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVPPS--GERdhamLAAFIRLddetRN 2384
Cdd:cd05920    367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR-HPAVHDAAVVAMPDEllGER----SCAFVVL----RD 437
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2385 SPLiikyaednSTAQI-VFLTgiEEELSE-RLPQHMVPtvffaLVHFPTTTSGKTDRKRL 2442
Cdd:cd05920    438 PPP--------SAAQLrRFLR--ERGLAAyKLPDRIEF-----VDSLPLTAVGKIDKKAL 482
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
5632-6038 4.97e-27

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 120.03  E-value: 4.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPA-ICAWDG-ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 5709
Cdd:cd05904     15 ASAHPSRPAlIDAATGrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5710 RHEDTFRHTGAQVVVTSAQHSARWIGTNHQVVTV----SAGSLGQLSTLVNPVGLPAIPE----NAVYIMFTSGSTGIPK 5781
Cdd:cd05904     95 EIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLdsaeFDSLSFSDLLFEADEAEPPVVVikqdDVAALLYSSGTTGRSK 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5782 GVVLEHRAVVTSCWG--RGRAFGITNLSRVL----QFASYTFDACMdeiITTLMYGGCICVPSDSDRRnDLVKAISTMDV 5855
Cdd:cd05904    175 GVMLTHRNLIAMVAQfvAGEGSNSDSEDVFLcvlpMFHIYGLSSFA---LGLLRLGATVVVMPRFDLE-ELLAAIERYKV 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5856 SCALLTPSV------ARLLEPSSVPTLQMLV-----LQGE-QVSFADwnRWPaSVQTINGYGPTE----CSICCNTysGK 5919
Cdd:cd05904    251 THLPVVPPIvlalvkSPIVDKYDLSSLRQIMsgaapLGKElIEAFRA--KFP-NVDLGQGYGMTEstgvVAMCFAP--EK 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5920 QGFKSGIIGTSVASV-SWVVDPENHDRLaPLGSIGELLVEGPILARGYLNDIQKTAAVfIDDPAWLlegypghpgrqgrl 5998
Cdd:cd05904    326 DRAKYGSVGRLVPNVeAKIVDPETGESL-PPNQTGELWIRGPSIMKGYLNNPEATAAT-IDKEGWL-------------- 389
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1820002560 5999 yKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHH 6038
Cdd:cd05904    390 -HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEAL 428
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
5646-6136 5.15e-27

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 119.74  E-value: 5.15e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5646 GELTYGELD----ALSSKLAGhltqlGVKPEDMVPLCFEKSMWTVVAMLAVLKAGgaFVPLDPDHPASrhEDTFRHT--- 5718
Cdd:cd05909      6 TSLTYRKLLtgaiALARKLAK-----MTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAG--LRELRACikl 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5719 -GAQVVVTSAQ--------------HSARW---------IGTNHQVVTVSAGSLGQLSTLVNPVGLPAIPENAVYIMFTS 5774
Cdd:cd05909     77 aGIKTVLTSKQfieklklhhlfdveYDARIvyledlrakISKADKCKAFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5775 GSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQ----FASYTFDACMdeiITTLMYGGCI-CVPSDSDRRNdLVKA 5849
Cdd:cd05909    157 GSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGCL---WLPLLSGIKVvFHPNPLDYKK-IPEL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5850 ISTMDVSCALLTPS----VARLLEPSSVPTLQMLVLQGEQVSFADWNRWPAS--VQTINGYGPTECS--ICCNTysGKQG 5921
Cdd:cd05909    233 IYDKKATILLGTPTflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSpvISVNT--PQSP 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5922 FKSGIIGTSVASVSW-VVDPENHDRLaPLGSIGELLVEGPILARGYLNDIQKTAAVFIDdpAWllegypghpgrqgrlYK 6000
Cdd:cd05909    311 NKEGTVGRPLPGMEVkIVSVETHEEV-PIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD--GW---------------YD 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6001 TGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVRECLPEARQLAVeVILPSGQKDHAmLAAFVQLEEGTQNALL 6080
Cdd:cd05909    373 TGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAV-VSVPDGRKGEK-IVLLTTTTDTDPSSLN 450
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6081 DkeasgedsmaqvvFLASVEeelakrLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:cd05909    451 D-------------ILKNAG------ISNLAKPSYIHQVEEIPLLGTGKPDYVTLK 487
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
3465-3858 5.25e-27

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 120.98  E-value: 5.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAICAWDG----ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP 3540
Cdd:COG1022     15 DLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3541 LDPDHPASRHEEIFEQTGAQVVVAS--AQY----SARWTSSSC-HVVTV--------SKALS----------SQLPAVVD 3595
Cdd:COG1022     95 IYPTSSAEEVAYILNDSGAKVLFVEdqEQLdkllEVRDELPSLrHIVVLdprglrddPRLLSldellalgreVADPAELE 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3596 STNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQF--ASYTFDACIAeiITTLLCGGCI 3673
Cdd:COG1022    175 ARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlpLAHVFERTVS--YYALAAGATV 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3674 CVPSDSDR-RNSL-------------------AKAISTMD---------VNWAF-LTPSVARLLDPGLIPSL-------- 3715
Cdd:COG1022    253 AFAESPDTlAEDLrevkptfmlavprvwekvyAGIQAKAEeagglkrklFRWALaVGRRYARARLAGKSPSLllrlkhal 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3716 -------KILAI----------GGEqSSSADWNRWPGSVqKIHV---YGPTECCIFCTGyTTKQGFEPSTIGTSVASVSW 3775
Cdd:COG1022    333 adklvfsKLREAlggrlrfavsGGA-ALGPELARFFRAL-GIPVlegYGLTETSPVITV-NRPGDNRIGTVGPPLPGVEV 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3776 VVDPEnhnrlaplgsmGELLMEGPILARGYLNDVDKTEAAFIDDpAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYL 3855
Cdd:COG1022    410 KIAED-----------GEILVRGPNVMKGYYKNPEATAEAFDAD-GWL---------------HTGDIGELDEDGFLRIT 462

                   ...
gi 1820002560 3856 GRK 3858
Cdd:COG1022    463 GRK 465
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
7617-8121 5.61e-27

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 119.78  E-value: 5.61e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 7696
Cdd:cd05959     14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7697 EEIFEQTGAQVVVASAQYSARWTS-------SSCHVVTVSKA--------LSSQLPAVVDSTNT-SVRPENAAYIIFTSG 7760
Cdd:cd05959     94 AYYLEDSRARVVVVSGELAPVLAAaltksehTLVVLIVSGGAgpeagallLAELVAAEAEQLKPaATHADDPAFWLYSSG 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7761 STGVPKGVVLEHRAVATSCLGHGR-AFGITNLSRVLQ-----FA-----SYTFDACIAEiiTTLLCGGcicVPSDSdrrn 7829
Cdd:cd05959    174 STGRPKGVVHLHADIYWTAELYARnVLGIREDDVCFSaaklfFAyglgnSLTFPLSVGA--TTVLMPE---RPTPA---- 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7830 SLAKAISTMDVNWAFLTPSV--ARLLDPGL----IPSLKILAIGGEQSSSADWNRWP-----------GSVQKIHvygpt 7892
Cdd:cd05959    245 AVFKRIRRYRPTVFFGVPTLyaAMLAAPNLpsrdLSSLRLCVSAGEALPAEVGERWKarfgldildgiGSTEMLH----- 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7893 eccIFCTgyTTKQGFEPSTIGTSVASVSW-VVDPENHNrlAPLGSMGELLMEGPILARGYLNDVDKTEAAFiddpawlle 7971
Cdd:cd05959    320 ---IFLS--NRPGRVRYGTTGKPVPGYEVeLRDEDGGD--VADGEPGELYVRGPSSATMYWNNRDKTRDTF--------- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7972 gypghpgrQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvrECL---PEARQLAVeviLPSGQKNHA 8048
Cdd:cd05959    384 --------QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVE----SALvqhPAVLEAAV---VGVEDEDGL 448
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 8049 M-LAVFVQLGKGThiahleeKAGGEDSmaqvvflTGTEEELAKRLPKHMVP--TVFFALLhfPMTTSGKADRKRLR 8121
Cdd:cd05959    449 TkPKAFVVLRPGY-------EDSEALE-------EELKEFVKDRLAPYKYPrwIVFVDEL--PKTATGKIQRFKLR 508
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
7183-7573 6.13e-27

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 118.28  E-value: 6.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7183 YPCSPLQEGLIsLTAKRAGD---YIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSElGLLQVVVE----EKI 7255
Cdd:cd19066      2 IPLSPMQRGMW-FLKKLATDpsaFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAG-RYEQVVLDktvrFRI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7256 Q------WTESEA-LEEYLKEDKAVSMGL-GDPLAHYALVKeaWGGKRW-FVWTIHHALYDGGSLPLILHAVKQVYSGAV 7326
Cdd:cd19066     80 EiidlrnLADPEArLLELIDQIQQTIYDLeRGPLVRVALFR--LADERDvLVVAIHHIIVDGGSFQILFEDISSVYDAAE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7327 LERQ------PSFNAFI----QYLGQQDLEATAAYWQTALSDceavlFPPLPSTVTQPVADTTVEY------QC--PPLS 7388
Cdd:cd19066    158 RQKPtlpppvGSYADYAawleKQLESEAAQADLAYWTSYLHG-----LPPPLPLPKAKRPSQVASYevltleFFlrSEET 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7389 KATLD------TTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPiaGVEAMVGPTIATVPVRLRVQRDQTVFAFLQG 7462
Cdd:cd19066    233 KRLREvaresgTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKR 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7463 LQQQSTDMIAHEQTGLQHIAkLGSGPRHACGFQTLLvvQPVDDVLGSDDMLGEWRSYSKM-QDFTT-----YALMVQFT- 7535
Cdd:cd19066    311 TKEQSREAIEHQRVPFIELV-RHLGVVPEAPKHPLF--EPVFTFKNNQQQLGKTGGFIFTtPVYTSsegtvFDLDLEASe 387
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1820002560 7536 LAAEGVQITASFDARVIEHWVLEKMLRQFSFIMQQLAE 7573
Cdd:cd19066    388 DPDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIE 425
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
7610-8122 6.14e-27

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 119.87  E-value: 6.14e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7610 HDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAGgaFV 7685
Cdd:COG1021     28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVvvqlPNVAE----FVIVFFALFRAG--AI 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7686 P---LdpdhPASRHEEI---FEQTGAQVVVASAQYS-------ARWTSSSC----HVVTVSKA-----LSSQLPAVVDST 7743
Cdd:COG1021    102 PvfaL----PAHRRAEIshfAEQSEAVAYIIPDRHRgfdyralARELQAEVpslrHVLVVGDAgeftsLDALLAAPADLS 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7744 NTSVRPENAAYIIFTSGSTGVPKGVVLEH-------RAVATSClghgrafGITNLSRVLQF--ASYTFDACIAEIITTLL 7814
Cdd:COG1021    178 EPRPDPDDVAFFQLSGGTTGLPKLIPRTHddylysvRASAEIC-------GLDADTVYLAAlpAAHNFPLSSPGVLGVLY 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7815 CGGCIcVPSDSDRRNSLAKAISTMDVNWAFLTPSVARL------LDPGLIPSLKILAIGGEQSSSADWNR----WPGSVQ 7884
Cdd:COG1021    251 AGGTV-VLAPDPSPDTAFPLIERERVTVTALVPPLALLwldaaeRSRYDLSSLRVLQVGGAKLSPELARRvrpaLGCTLQ 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7885 kiHVYGPTE--CCifctgYT----------TKQGfEPstigtsvasVS-----WVVDPEnhNRLAPLGSMGELLMEGPIL 7947
Cdd:COG1021    330 --QVFGMAEglVN-----YTrlddpeevilTTQG-RP---------ISpddevRIVDED--GNPVPPGEVGELLTRGPYT 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7948 ARGYLNDVDKTEAAFIDDpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREc 8027
Cdd:COG1021    391 IRGYYRAPEHNARAFTPD------GF----------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLA- 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8028 LPEARQLAVeVILPS---GQKNHAmlavFVQLgkgthiahleekAGGEDSMAQVV-FLTgteeelAKRLPKHMVPTVFFA 8103
Cdd:COG1021    454 HPAVHDAAV-VAMPDeylGERSCA----FVVP------------RGEPLTLAELRrFLR------ERGLAAFKLPDRLEF 510
                          570
                   ....*....|....*....
gi 1820002560 8104 LLHFPMTTSGKADRKRLRE 8122
Cdd:COG1021    511 VDALPLTAVGKIDKKALRA 529
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
1939-2343 6.30e-27

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 118.48  E-value: 6.30e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 2018
Cdd:cd17631      5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2019 EDIFRQTGAQVVVtsaqhsarwigtnhqvvtvsagsleqfstlvnpvdlpakpENAAYVMFTSGSTGTPKGVVLEHRAVV 2098
Cdd:cd17631     85 AYILADSGAKVLF----------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLL 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2099 TSCLGHGQAFGVTNLLRALqFTAYTFDVCIAEIIT--TLVHGGCICVPS-----------DSERRDNLAKAITDMQvnwG 2165
Cdd:cd17631    125 WNAVNALAALDLGPDDVLL-VVAPLFHIGGLGVFTlpTLLRGGTVVILRkfdpetvldliERHRVTSFFLVPTMIQ---A 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2166 YLTSSVARLLDpclVPSLKVLVLGG----EQVNSTDWGKWPSSVQtinGYGPTECCvfctgyTGIQGFQS-------GNI 2234
Cdd:cd17631    201 LLQHPRFATTD---LSSLRAVIYGGapmpERLLRALQARGVKFVQ---GYGMTETS------PGVTFLSPedhrrklGSA 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2235 GTSIASVSW-VVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpaWLlegypghegrqgrlyKTGDLVR 2313
Cdd:cd17631    269 GRPVFFVEVrIVDPD--GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG--WF---------------HTGDLGR 329
                          410       420       430
                   ....*....|....*....|....*....|
gi 1820002560 2314 YSSDGNLVCLGRKDSQVKVRGQRVELGEVE 2343
Cdd:cd17631    330 LDEDGYLYIVDRKKDMIISGGENVYPAEVE 359
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
851-1368 7.59e-27

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 119.85  E-value: 7.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  851 DRCIHDLFAEQARARPDASAVCAWDG-ELTYGELDELSSKLAAHLVQLGVKREDVVplCFEKSMWT--VVAMLAVLKAGG 927
Cdd:PRK06087    22 DASLADYWQQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRV--AFQLPGWCefTIIYLACLKVGA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  928 AFVPLDpghPASRHEEIFKqigaqvVLTSSQHAMLFASSERHQVTVSKVSTS---QLPT---VVNFAKS----------- 990
Cdd:PRK06087   100 VSVPLL---PSWREAELVW------VLNKCQAKMFFAPTLFKQTRPVDLILPlqnQLPQlqqIVGVDKLapatsslslsq 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  991 ------------PVDPGNTAYIIFTSGTTGIPKGVVLQH-------RAVTT-------------SCLGHGEAF--GYTD- 1035
Cdd:PRK06087   171 iiadyeplttaiTTHGDELAAVLFTSGTEGLPKGVMLTHnnilaseRAYCArlnltwqdvfmmpAPLGHATGFlhGVTAp 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1036 ---HARVLQFASYTFDACiaeiITTLLYGGCICVPSEsdrrnnlakaistmdvncallTPSVARLL-----EPSAVPSLK 1107
Cdd:PRK06087   251 fliGARSVLLDIFTPDAC----LALLEQQRCTCMLGA---------------------TPFIYDLLnllekQPADLSALR 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1108 RLVLQGEQVsfadwnrwPGS-VQTINGYGPTECSVCCNTYSGKQGF---------KSGIIGTSVASLSW-VVDaGNHNRL 1176
Cdd:PRK06087   306 FFLCGGTTI--------PKKvARECQQRGIKLLSVYGSTESSPHAVvnlddplsrFMHTDGYAAAGVEIkVVD-EARKTL 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1177 aPLGSIGELLVEGPILARGYLNDIDKTEAAfIDDPAWllegyeghagrrgrlYKTGDLVRCDADGNLVCLGRKdSQVKVR 1256
Cdd:PRK06087   377 -PPGCEGEEASRGPNVFMGYLDEPELTARA-LDEEGW---------------YYSGDLCRMDEAGYIKITGRK-KDIIVR 438
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1257 -GQRVELGEIEHHVREClPEARQLAVeVILPS---GQKehalLAAFIQLdKGNHNALfeekasgedSMAQVV-FLTgvEE 1331
Cdd:PRK06087   439 gGENISSREVEDILLQH-PKIHDACV-VAMPDerlGER----SCAYVVL-KAPHHSL---------TLEEVVaFFS--RK 500
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1820002560 1332 ELAKRL-PEHMVptilfTVKAMPITTSGKIDRKRL-QDI 1368
Cdd:PRK06087   501 RVAKYKyPEHIV-----VIDKLPRTASGKIQKFLLrKDI 534
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
5636-6137 1.00e-26

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 118.57  E-value: 1.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5636 PHAPAICAWDG--ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHED 5713
Cdd:cd05926      1 PDAPALVVPGStpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5714 TFRHTGAQVVVTS---------AQHSARW------IGTNHQVVTVSAGSLGQL--STLVNPVGLPAIPENAVYIMFTSGS 5776
Cdd:cd05926     81 YLADLGSKLVLTPkgelgpasrAASKLGLailelaLDVGVLIRAPSAESLSNLlaDKKNAKSEGVPLPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5777 TGIPKGVVLEHRAVVTScwgrgrafgITNLSRVLQFASYtfDACM------------DEIITTLMYGGCICVP---SDSD 5841
Cdd:cd05926    161 TGRPKGVPLTHRNLAAS---------ATNITNTYKLTPD--DRTLvvmplfhvhglvASLLSTLAAGGSVVLPprfSAST 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5842 RRNDLVK-------AISTMdvSCALLT---------PSVARLLEPSSVPtLQMLVLQGEQVSFAdwnrwpasVQTINGYG 5905
Cdd:cd05926    230 FWPDVRDynatwytAVPTI--HQILLNrpepnpespPPKLRFIRSCSAS-LPPAVLEALEATFG--------APVLEAYG 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5906 PTECS--ICCNTYSGKQGfKSGIIGTSVASVSWVVDPenHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPaW 5983
Cdd:cd05926    299 MTEAAhqMTSNPLPPGPR-KPGSVGKPVGVEVRILDE--DGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG-W 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5984 LlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClpEARQLAVEVILPsgqkdHA 6063
Cdd:cd05926    375 F---------------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH--PAVLEAVAFGVP-----DE 432
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 6064 ML----AAFVQLEEGTQnalLDKEAsgedsmaqvvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:cd05926    433 KYgeevAAAVVLREGAS---VTEEE--------------LRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
5626-6073 1.02e-26

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 120.21  E-value: 1.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDG----ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVP 5701
Cdd:COG1022     15 DLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5702 LDPDHPASRHEDTFRHTGAQVVVTSAQ-HSARWIGTNHQ------VVTVSAG---------SLGQLSTLVNPVGLPAIPE 5765
Cdd:COG1022     95 IYPTSSAEEVAYILNDSGAKVLFVEDQeQLDKLLEVRDElpslrhIVVLDPRglrddprllSLDELLALGREVADPAELE 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5766 NAVY---------IMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVL----------QFASYTFdacmdeiit 5826
Cdd:COG1022    175 ARRAavkpddlatIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLsflplahvfeRTVSYYA--------- 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5827 tLMYGGCICVPSDSDR-RNDLvKAI--STMdvscalltPSVARLLE----------PSSVPTLQML-------------- 5879
Cdd:COG1022    246 -LAAGATVAFAESPDTlAEDL-REVkpTFM--------LAVPRVWEkvyagiqakaEEAGGLKRKLfrwalavgrryara 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5880 VLQGEQVSFADWNRWP--------------------------------------ASVQTINGYGPTECS--ICCNTYsgk 5919
Cdd:COG1022    316 RLAGKSPSLLLRLKHAladklvfsklrealggrlrfavsggaalgpelarffraLGIPVLEGYGLTETSpvITVNRP--- 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5920 QGFKSGIIGTSVASVSWVVDPEnhdrlaplgsiGELLVEGPILARGYLNDIQKTAAVFIDDpAWLlegypghpgrqgrly 5999
Cdd:COG1022    393 GDNRIGTVGPPLPGVEVKIAED-----------GEILVRGPNVMKGYYKNPEATAEAFDAD-GWL--------------- 445
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 6000 KTGDLVRYDANGNLVCLGRKDSQVKLR-GQRVELGEVEHHVREClPEARQlAVeVIlpsGQkDHAMLAAFVQLEE 6073
Cdd:COG1022    446 HTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKAS-PLIEQ-AV-VV---GD-GRPFLAALIVPDF 513
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1954-2443 1.05e-26

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 117.92  E-value: 1.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1954 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL----DPDHPASRHEDifrqTGAQV 2029
Cdd:cd05971      6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLfalfGPEALEYRLSN----SGASA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2030 VVTsaqhsarwigtnhqvvtvsagsleqfstlvnpvDLPAKPenaAYVMFTSGSTGTPKGVVLEHRAVvtscLGHGQAFG 2109
Cdd:cd05971     82 LVT---------------------------------DGSDDP---ALIIYTSGTTGPPKGALHAHRVL----LGHLPGVQ 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2110 VT-NLLRALQFTAYT----------FDVciaeIITTLVHGgcicVPSDSERRDNL-AKAITDMQVNWG----YLTSSVAR 2173
Cdd:cd05971    122 FPfNLFPRDGDLYWTpadwawigglLDV----LLPSLYFG----VPVLAHRMTKFdPKAALDLMSRYGvttaFLPPTALK 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2174 LLDPCLVP------SLKVLVLGGEQV--NSTDWGKWPSSVQTINGYGPTECCVFCTGYTGIQGFQSGNIGTSI-ASVSWV 2244
Cdd:cd05971    194 MMRQQGEQlkhaqvKLRAIATGGESLgeELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIpGHRVAI 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2245 VDPEnhGRLAPLGSIGELLVE--GPILARGYLNDVDKTQAAFIDDpaWLLegypghegrqgrlykTGDLVRYSSDGNLVC 2322
Cdd:cd05971    274 VDDN--GTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD--WLL---------------TGDLGRKDSDGYFWY 334
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2323 LGRKDSQVKVRGQRVELGEVEHHMRKclpeanqlavevvPPSgerdhAMLAAFIRLDDETRNSplIIKyaednstAQIVF 2402
Cdd:cd05971    335 VGRDDDVITSSGYRIGPAEIEECLLK-------------HPA-----VLMAAVVGIPDPIRGE--IVK-------AFVVL 387
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 2403 LTGIE--EELSE--------RLPQHMVPTVFFALVHFPTTTSGKTDRKRLR 2443
Cdd:cd05971    388 NPGETpsDALAReiqelvktRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
PRK09088 PRK09088
acyl-CoA synthetase; Validated
5631-6141 1.07e-26

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 118.76  E-value: 1.07e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5631 QAKARPHAPAI--CAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPA 5708
Cdd:PRK09088     4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5709 SRHEDTFRHTGAQVVVTSAQHSA-RWIGTNHQVVTVSAGSLGqlstlvnPVGLPAIPENAV-YIMFTSGSTGIPKGVVLE 5786
Cdd:PRK09088    84 SELDALLQDAEPRLLLGDDAVAAgRTDVEDLAAFIASADALE-------PADTPSIPPERVsLILFTSGTSGQPKGVMLS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5787 HRAVvtscwgRGRAFGITNLSRVLQFASYTFDACMDEII-------TTLMYGGCICVPSDSDRRNDLVK-AISTMDVSCA 5858
Cdd:PRK09088   157 ERNL------QQTAHNFGVLGRVDAHSSFLCDAPMFHIIglitsvrPVLAVGGSILVSNGFEPKRTLGRlGDPALGITHY 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5859 LLTPSVARLL------EPSSVPTLQMLVLQGEQVSFADWNRWPAS-VQTINGYGPTEC------SICCNTYSGKQGfKSG 5925
Cdd:PRK09088   231 FCVPQMAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWLDDgIPMVDGFGMSEAgtvfgmSVDCDVIRAKAG-AAG 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5926 IIGTSVASVswVVDpeNHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpAWllegypghpgrqgrlYKTGDLV 6005
Cdd:PRK09088   310 IPTPTVQTR--VVD--DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGD-GW---------------FRTGDIA 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6006 RYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHAMLAAFVQLEEGTqnalldkeas 6085
Cdd:PRK09088   370 RRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLAD-HPGIRECAV-VGMADAQWGEVGYLAIVPADGAP---------- 437
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6086 gedsmaqvVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGAS 6141
Cdd:PRK09088   438 --------LDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
PRK06145 PRK06145
acyl-CoA synthetase; Validated
7611-8036 1.20e-26

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 118.45  E-value: 1.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 7690
Cdd:PRK06145     6 ASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7691 HPASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSKALSSQ----LPAVVDSTNTSVRPENAAYIIFTSGSTGVPK 7766
Cdd:PRK06145    86 LAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSrrlaQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPK 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7767 GVVLEHRAVATSCLGHGRAFGITNLSRVLQFAS-YTFDACIAEIITTLLCGGCICVPSDSDRRNSLAkAISTMDVNWAFL 7845
Cdd:PRK06145   166 GVMHSYGNLHWKSIDHVIALGLTASERLLVVGPlYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA-AIERHRLTCAWM 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7846 TP-SVARLL-----DPGLIPSLKILAIGGEQSSSA---DWNRWPGSVQKIHVYGPTECcifCTGYT-TKQGFEPSTIGTS 7915
Cdd:PRK06145   245 APvMLSRVLtvpdrDRFDLDSLAWCIGGGEKTPESrirDFTRVFTRARYIDAYGLTET---CSGDTlMEAGREIEKIGST 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7916 ---VASVSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLLEGYPGHPGRQGRLYKTgdlvqy 7992
Cdd:PRK06145   322 graLAHVEIRIADGAGRWLPP-NMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--WFRSGDVGYLDEEGFLYLT------ 392
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 7993 nadgnlvylGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAV 8036
Cdd:PRK06145   393 ---------DRKKDMIISGGENIASSEVERVIYE-LPEVAEAAV 426
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4564-5055 1.24e-26

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 117.39  E-value: 1.24e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4564 DGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVL 4643
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4644 AsaqyatlwtslgrsvvivseastsqlpvvtktaDPsvnpgnaAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGIT 4723
Cdd:cd05934     81 V---------------------------------DP-------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4724 DHTRVLQF--ASYTfDACIAEIITTLLCcGCICVPSDSDRRNNLAKAINAMDVNWALLTPSVARML-------DPCvvqS 4794
Cdd:cd05934    121 EDDVYLTVlpLFHI-NAQAVSVLAALSV-GATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLlaqppspDDR---A 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4795 LKILVLGGEQVNSADWDRWPK--SIQTINAYGPTEcSICCTTYSGKQGFKSGTIGTSIVSVSW-VVDPenHNRLAPLGSI 4871
Cdd:cd05934    196 HRLRAAYGAPNPPELHEEFEErfGVRLLEGYGMTE-TIVGVIGPRDEPRRPGSIGRPAPGYEVrIVDD--DGQELPAGEP 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4872 GELLV---EGPILARGYLNDMEKTEAAFiddpawllegygghsgRQGrLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQR 4948
Cdd:cd05934    273 GELVIrglRGWGFFKGYYNMPEATAEAM----------------RNG-WFHTGDLGYRDADGFFYFVDRKKDMIRRRGEN 335
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4949 VELGEVEH----H--VREClteakqlAVeVIVPEGEGGYAmLAAFVQLGDdtyntlvkekagGDSLTVQVVFlDRVEEEL 5022
Cdd:cd05934    336 ISSAEVERailrHpaVREA-------AV-VAVPDEVGEDE-VKAVVVLRP------------GETLDPEELF-AFCEGQL 393
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 5023 AK-RVPEHMMLttfftLEAMPTTTSGKIDRKRLR 5055
Cdd:cd05934    394 AYfKVPRYIRF-----VDDLPKTPTEKVAKAQLR 422
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
4565-5055 1.48e-26

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 118.20  E-value: 1.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4565 GELTYGELDTLSSKLASHLvQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGgaFVPLDPDHPASRHE--HIFRQTGAQVV 4642
Cdd:cd05909      6 TSLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAGLRElrACIKLAGIKTV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4643 LASAQY---ATLW--------------------TSLGRSVVIVSEASTSQLPVVTKTADPSVNPGNAAYAIFTSGSTGIP 4699
Cdd:cd05909     83 LTSKQFiekLKLHhlfdveydarivyledlrakISKADKCKAFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4700 KGVVLEHKAVVTSCLGHGQAFGITDHTRVLQ----FASYTFDACiaeIITTLLCCGCI-CVPSDSDRRnNLAKAINAMDV 4774
Cdd:cd05909    163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGC---LWLPLLSGIKVvFHPNPLDYK-KIPELIYDKKA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4775 NWALLTPS----VARMLDPCVVQSLKILVLGGEQVNSADWDRWPKS--IQTINAYGPTECSICCTTYSGKQGFKSGTIGT 4848
Cdd:cd05909    239 TILLGTPTflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSPVISVNTPQSPNKEGTVGR 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4849 SIVSVSW-VVDPENHNRLaPLGSIGELLVEGPILARGYLNDMEKTEAAFIDdpAWllegygghsgrqgrlYKTGDLVRYD 4927
Cdd:cd05909    319 PLPGMEVkIVSVETHEEV-PIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD--GW---------------YDTGDIGKID 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4928 ADGNLVYLGRKDSQVKLRGQRVELGEVEHHVRECLTEAKQLAVeVIVPEGEGGYAM-LAAFVQLGD-DTYNTLVKEkAGG 5005
Cdd:cd05909    381 GEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAV-VSVPDGRKGEKIvLLTTTTDTDpSSLNDILKN-AGI 458
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5006 DSLTvqvvfldrveeelakrVPEHmmlttFFTLEAMPTTTSGKIDRKRLR 5055
Cdd:cd05909    459 SNLA----------------KPSY-----IHQVEEIPLLGTGKPDYVTLK 487
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
1939-2444 1.48e-26

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 118.88  E-value: 1.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGE------LTYGELDALSSKLASHLVQLGvNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 2012
Cdd:cd05931      3 AAARPDRPAYTFLDDEggreetLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2013 HPASRHE---DIFRQTGAQVVVTSAQHSARWIGTNHqvvtvSAGSLEQFSTLVnpVDLPA------------KPENAAYV 2077
Cdd:cd05931     82 TPGRHAErlaAILADAGPRVVLTTAAALAAVRAFAA-----SRPAAGTPRLLV--VDLLPdtsaadwpppspDPDDIAYL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2078 MFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTnllralqftayTFDVC------------IAEIITTLVHGGCiCV-- 2143
Cdd:cd05931    155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLD-----------PGDVVvswlplyhdmglIGGLLTPLYSGGP-SVlm 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2144 -PSDSERRDNL-AKAITDMQVnwgylTSSVA----------RLLDPCLVP----SLKVLVLGGEQVNstdwgkwPSSVQT 2207
Cdd:cd05931    223 sPAAFLRRPLRwLRLISRYRA-----TISAApnfaydlcvrRVRDEDLEGldlsSWRVALNGAEPVR-------PATLRR 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2208 IN---------------GYGPTECCVFCTGYTGIQGFQS------------------GNIGTSIASVSWV--------VD 2246
Cdd:cd05931    291 FAeafapfgfrpeafrpSYGLAEATLFVSGGPPGTGPVVlrvdrdalagravavaadDPAARELVSCGRPlpdqevriVD 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2247 PENHGRLAPlGSIGELLVEGPILARGYLNDVDKTQAAF-----IDDPAWLlegypghegrqgrlyKTGDLvRYSSDGNLV 2321
Cdd:cd05931    371 PETGRELPD-GEVGEIWVRGPSVASGYWGRPEATAETFgalaaTDEGGWL---------------RTGDL-GFLHDGELY 433
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2322 CLGRKDSQVKVRGQRvelgeveHHmrkclPEANQLAVEVVPPSGERDhaMLAAFIRLDDETRnsPLIIkYAEDNSTAQIV 2401
Cdd:cd05931    434 ITGRLKDLIIVRGRN-------HY-----PQDIEATAEEAHPALRPG--CVAAFSVPDDGEE--RLVV-VAEVERGADPA 496
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 2402 FLTGIEEELSERLP-QHMVPTVFFALV---HFPTTTSGKTDRKRLRE 2444
Cdd:cd05931    497 DLAAIAAAIRAAVArEHGVAPADVVLVrpgSIPRTSSGKIQRRACRA 543
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
7611-8004 1.56e-26

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 119.43  E-value: 1.56e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAICAWDG----ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP 7686
Cdd:COG1022     15 DLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7687 LDPDHPASRHEEIFEQTGAQVVVAS--AQY----SARWTSSSC-HVVTV--------SKALS----------SQLPAVVD 7741
Cdd:COG1022     95 IYPTSSAEEVAYILNDSGAKVLFVEdqEQLdkllEVRDELPSLrHIVVLdprglrddPRLLSldellalgreVADPAELE 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7742 STNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQF--ASYTFDACIAeiITTLLCGGCI 7819
Cdd:COG1022    175 ARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlpLAHVFERTVS--YYALAAGATV 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7820 CVPSDSDR-RNSL-------------------AKAISTMD---------VNWAF-LTPSVARLLDPGLIPSL-------- 7861
Cdd:COG1022    253 AFAESPDTlAEDLrevkptfmlavprvwekvyAGIQAKAEeagglkrklFRWALaVGRRYARARLAGKSPSLllrlkhal 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7862 -------KILAI----------GGEqSSSADWNRWPGSVqKIHV---YGPTECCIFCTGyTTKQGFEPSTIGTSVASVSW 7921
Cdd:COG1022    333 adklvfsKLREAlggrlrfavsGGA-ALGPELARFFRAL-GIPVlegYGLTETSPVITV-NRPGDNRIGTVGPPLPGVEV 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7922 VVDPEnhnrlaplgsmGELLMEGPILARGYLNDVDKTEAAFIDDpAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYL 8001
Cdd:COG1022    410 KIAED-----------GEILVRGPNVMKGYYKNPEATAEAFDAD-GWL---------------HTGDIGELDEDGFLRIT 462

                   ...
gi 1820002560 8002 GRK 8004
Cdd:COG1022    463 GRK 465
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
5626-6135 1.57e-26

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 117.81  E-value: 1.57e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMV----PLCFEksmwTVVAMLAVLKAGGAFVP 5701
Cdd:cd05920     19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVvvqlPNVAE----FVVLFFALLRLGAVPVL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5702 LDPDHpaSRHEDTF--RHTGAQVVVTSAQHSarwiGTNHQvvtvsagSLGQLStlvnpvgLPAIPENAVYIMfTSGSTGI 5779
Cdd:cd05920     95 ALPSH--RRSELSAfcAHAEAVAYIVPDRHA----GFDHR-------ALAREL-------AESIPEVALFLL-SGGTTGT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5780 PKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQF--ASYTFDACMDEIITTLMYGGCIcVPSDSDRRNDLVKAISTMDVSC 5857
Cdd:cd05920    154 PKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRV-VLAPDPSPDAAFPLIEREGVTV 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5858 ALLTPSVARLL------EPSSVPTLQMLVLQGEQVSFADWNRWPA----SVQTIngYGPTECSICcntYSGKQGFKSGII 5927
Cdd:cd05920    233 TALVPALVSLWldaaasRRADLSSLRLLQVGGARLSPALARRVPPvlgcTLQQV--FGMAEGLLN---YTRLDDPDEVII 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5928 GTSVASVS-----WVVDPEnhDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpawlleGYpghpgrqgrlYKTG 6002
Cdd:cd05920    308 HTQGRPMSpddeiRVVDEE--GNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPD------GF----------YRTG 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6003 DLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAVeVILPS---GQKdhamLAAFVQLEEGTQNAL 6079
Cdd:cd05920    370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR-HPAVHDAAV-VAMPDellGER----SCAFVVLRDPPPSAA 443
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6080 LDKEASGEDSMAqvvflasveeelAKRLPEHMVPtvffsLLHFPTTTSGKTDRKRL 6135
Cdd:cd05920    444 QLRRFLRERGLA------------AYKLPDRIEF-----VDSLPLTAVGKIDKKAL 482
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
3475-3976 1.88e-26

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 117.80  E-value: 1.88e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3475 PHAPAICAWDG--ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEE 3552
Cdd:cd05926      1 PDAPALVVPGStpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3553 IFEQTGAQVVV------------ASAQYSAR----WTSSSCHVVTVSKALSSQLPA-VVDSTNTSVRPENAAYIIFTSGS 3615
Cdd:cd05926     81 YLADLGSKLVLtpkgelgpasraASKLGLAIlelaLDVGVLIRAPSAESLSNLLADkKNAKSEGVPLPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3616 TGVPKGVVLEHRAVATSCLGHGRAFGITNLSR---VLQFasYTFDACIAEIITTLLCGGCICVPSdsdrRNSLAKAISTM 3692
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRtlvVMPL--FHVHGLVASLLSTLAAGGSVVLPP----RFSASTFWPDV 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3693 ---DVNWAFLTPSVARLL------DPGlIPSLKILAIggeQSSSAdwnrwPGSVQKIH------------VYGPTECC-- 3749
Cdd:cd05926    235 rdyNATWYTAVPTIHQILlnrpepNPE-SPPPKLRFI---RSCSA-----SLPPAVLEaleatfgapvleAYGMTEAAhq 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3750 IFCTGYTTKQGfEPSTIGTSVASVSWVVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPaWLlegypg 3829
Cdd:cd05926    306 MTSNPLPPGPR-KPGSVGKPVGVEVRILDE--DGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG-WF------ 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3830 hpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClpEARQLAVEVILPsgqkdHAML----A 3905
Cdd:cd05926    376 ---------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH--PAVLEAVAFGVP-----DEKYgeevA 439
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 3906 AFVQLEEGTQnalLDKEAggedsmaqvvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:cd05926    440 AAVVLREGAS---VTEEE--------------LRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
PRK09088 PRK09088
acyl-CoA synthetase; Validated
7614-8126 1.99e-26

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 117.60  E-value: 1.99e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7614 AEQARARPGAPAI--CAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 7691
Cdd:PRK09088     2 AFHARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7692 PASRHEEIFEQTGAQVVVASAQYSArwtsSSCHVVTVSkALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLE 7771
Cdd:PRK09088    82 SASELDALLQDAEPRLLLGDDAVAA----GRTDVEDLA-AFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7772 HRAVATSCLGHGRafgitnLSRVLQFASYTFDACIAEII-------TTLLCGGCICVPSDSDRRNSLAK-AISTMDVNWA 7843
Cdd:PRK09088   157 ERNLQQTAHNFGV------LGRVDAHSSFLCDAPMFHIIglitsvrPVLAVGGSILVSNGFEPKRTLGRlGDPALGITHY 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7844 FLTPSVARLL------DPGLIPSLKILAIGGEQSSSADWNRW-PGSVQKIHVYGPTEC---------CIFCTGYTTKQGF 7907
Cdd:PRK09088   231 FCVPQMAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWlDDGIPMVDGFGMSEAgtvfgmsvdCDVIRAKAGAAGI 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7908 EPSTIGTSVasvswvVDpeNHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpAWllegypghpgrqgrlYKTG 7987
Cdd:PRK09088   311 PTPTVQTRV------VD--DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGD-GW---------------FRTG 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7988 DLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE-----H-HVREC----LPEARQlavevilpsGQKNHamLAVFVQLG 8057
Cdd:PRK09088   367 DIARRDADGFFWVVDRKKDMFISGGENVYPAEIEavladHpGIRECavvgMADAQW---------GEVGY--LAIVPADG 435
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8058 KGTHIAHLeekaggedsmaqvvfLTGTEEELAK-RLPKHMvpTVFFALlhfPMTTSGKADRKRLREIGAS 8126
Cdd:PRK09088   436 APLDLERI---------------RSHLSTRLAKyKVPKHL--RLVDAL---PRTASGKLQKARLRDALAA 485
PRK06145 PRK06145
acyl-CoA synthetase; Validated
3471-3976 2.37e-26

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 117.68  E-value: 2.37e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 3550
Cdd:PRK06145    12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3551 EEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSKALSSQ----LPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEH 3626
Cdd:PRK06145    92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSrrlaQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSY 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3627 RAVATSCLGHGRAFGITNLSRVLQFAS-YTFDACIAEIITTLLCGGCICVPSDSDRRNSLAkAISTMDVNWAFLTP-SVA 3704
Cdd:PRK06145   172 GNLHWKSIDHVIALGLTASERLLVVGPlYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA-AIERHRLTCAWMAPvMLS 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3705 RLL-----DPGLIPSLKILAIGGEQSSSA---DWNRWPGSVQKIHVYGPTECcifCTGYT-TKQGFEPSTIGTS---VAS 3772
Cdd:PRK06145   251 RVLtvpdrDRFDLDSLAWCIGGGEKTPESrirDFTRVFTRARYIDAYGLTET---CSGDTlMEAGREIEKIGSTgraLAH 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3773 VSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLLEGYPGHPGRQGRLYKTgdlvqynadgnl 3852
Cdd:PRK06145   328 VEIRIADGAGRWLPP-NMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--WFRSGDVGYLDEEGFLYLT------------ 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3853 vylGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAveVILPSGQKDHAMLAAFVQLEEGtqnalldkeaggedsmaQV 3932
Cdd:PRK06145   393 ---DRKKDMIISGGENIASSEVERVIYE-LPEVAEAA--VIGVHDDRWGERITAVVVLNPG-----------------AT 449
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 3933 VFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:PRK06145   450 LTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
8263-8636 2.40e-26

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 116.39  E-value: 2.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8263 PASYIQQFYIATGVRAPREAF---NYPFIDLSDAvDIQVLQASCSALLEHFPILRTHFVYFQ-GKLYQVIPRHQDLPFSI 8338
Cdd:cd19536      3 PLSSLQEGMLFHSLLNPGGSVylhNYTYTVGRRL-NLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8339 FEVNGaLAEESQAIH-------IRDLDQTSPLglPTSFTLVRNA-SGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQEP 8410
Cdd:cd19536     82 LDLTP-LEEQLDPLRaykeetkIRRFDLGRAP--LVRAALVRKDeRERFLLVISDHHSILDGWSLYLLVKEILAVYNQLL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8411 ------LLSTTGFHSYLAYV--HNQRSASINYWSRLLKGSHITNiTSKLRPKLGKDTTIRSVKVERV-----IRTPQLPT 8477
Cdd:cd19536    159 eykplsLPPAQPYRDFVAHEraSIQQAASERYWREYLAGATLAT-LPALSEAVGGGPEQDSELLVSVplpvrSRSLAKRS 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8478 GLTMASLVSSAWAVVLSHISGEEDVVYGLVVAGRNSDLPSITEV------------------------SVQDQYISLGES 8533
Cdd:cd19536    238 GIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLlglflntlplrvtlseetvedllkRAQEQELESLSH 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8534 DSIGLDDIVQHCTDWPAkseFDSIIQHQNIEEQPEIQFAG-ETTKLQWFKNSFAVSR-QLFVFSHPRGNSLTITITGNTG 8611
Cdd:cd19536    318 EQVPLADIQRCSEGEPL---FDSIVNFRHFDLDFGLPEWGsDEGMRRGLLFSEFKSNyDVNLSVLPKQDRLELKLAYNSQ 394
                          410       420
                   ....*....|....*....|....*
gi 1820002560 8612 ILTDQCAEKLLVMLCDTISQLSDSL 8636
Cdd:cd19536    395 VLDEEQAQRLAAYYKSAIAELATAP 419
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
3465-3976 3.37e-26

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 118.18  E-value: 3.37e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 3544
Cdd:PRK05605    36 DLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPL 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3545 HPASRHEEIFEQTGAQVVV-----ASAQYSARWTSSSCHVVTVS------------------------KALSSQLPAVVD 3595
Cdd:PRK05605   116 YTAHELEHPFEDHGARVAIvwdkvAPTVERLRRTTPLETIVSVNmiaampllqrlalrlpipalrkarAALTGPAPGTVP 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3596 ---------------STNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLgHGRA------------------FGI 3642
Cdd:PRK05605   196 wetlvdaaiggdgsdVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAA-QGKAwvpglgdgpervlaalpmFHA 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3643 TNLSRVLQFASY---------TFDacIAEIIT-------TLLCGgcicVPSDSDRRNSLAKA--ISTMDVNWAFltpSVA 3704
Cdd:PRK05605   275 YGLTLCLTLAVSiggelvllpAPD--IDLILDamkkhppTWLPG----VPPLYEKIAEAAEErgVDLSGVRNAF---SGA 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3705 RLLDPglipslkilaiggeqSSSADWNRWPGSVQkIHVYGPTECCIFCTGYTTKQGFEPSTIG-----TSVAsvswVVDP 3779
Cdd:PRK05605   346 MALPV---------------STVELWEKLTGGLL-VEGYGLTETSPIIVGNPMSDDRRPGYVGvpfpdTEVR----IVDP 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3780 ENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKD 3859
Cdd:PRK05605   406 EDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--W---------------FRTGDVVVMEEDGFIRIVDRIK 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3860 SQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHAMLAAFVqLEEGtqnALLDKEAggedsmaqvvflasVE 3939
Cdd:PRK05605   469 ELIITGGFNVYPAEVEEVLRE-HPGVEDAAV-VGLPREDGSEEVVAAVV-LEPG---AALDPEG--------------LR 528
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 1820002560 3940 EELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:PRK05605   529 AYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
2561-2990 5.06e-26

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 115.89  E-value: 5.06e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2561 LTPIQH-LYLT--LDPSGrSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFQRQTGGRWQQYISEHDSSSL--- 2634
Cdd:pfam00668    7 LSPAQKrMWFLekLEPHS-SAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPFELeii 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2635 IVNHIHTRDTTEIVEAL--RQSRGSLDIERGPVLAAVLCDAGERQ-SLFVAIHHLVVDLVSWRIL----LEELEDLLLGQ 2707
Cdd:pfam00668   86 DISDLSESEEEEAIEAFiqRDLQSPFDLEKGPLFRAGLFRIAENRhHLLLSMHHIIVDGVSLGILlrdlADLYQQLLKGE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2708 TLPPALSTPFqawhaaqAKYIEEHVPPSAVAQVEldpDQLSYW--------------GVSPDDVLSSYAISEE-FVLDRK 2772
Cdd:pfam00668  166 PLPLPPKTPY-------KDYAEWLQQYLQSEDYQ---KDAAYWleqlegelpvlqlpKDYARPADRSFKGDRLsFTLDED 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2773 TTSTLLGSCNDAFSTRPLELMVA---ALS-YSFatifsdRKPAAIFNEIHGREawdsSIDLTRTVGWFTSMCPV--QAAN 2846
Cdd:pfam00668  236 TEELLRKLAKAHGTTLNDVLLAAyglLLSrYTG------QDDIVVGTPGSGRP----SPDIERMVGMFVNTLPLriDPKG 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2847 GAGLLDAIRETKDCIRSFQDNGWS--YFASQFASASAADAFASLF-PMEVLFNYQGLYQQLErkdslfknLPMPDSCEPA 2923
Cdd:pfam00668  306 GKTFSELIKRVQEDLLSAEPHQGYpfGDLVNDLRLPRDLSRHPLFdPMFSFQNYLGQDSQEE--------EFQLSELDLS 377
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 2924 LAALCPRFALFDVSFVV--EQGCAKVSFVSDKRARHQYRIRQWIQKYKvTLIDMSALLPNR--SAEWTLSD 2990
Cdd:pfam00668  378 VSSVIEEEAKYDLSLTAseRGGGLTIKIDYNTSLFDEETIERFAEHFK-ELLEQAIAHPSQplSELDLLSD 447
PRK09088 PRK09088
acyl-CoA synthetase; Validated
3470-3980 6.41e-26

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 116.06  E-value: 6.41e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3470 QAKARPHAPAI--CAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPA 3547
Cdd:PRK09088     4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3548 SRHEEIFEQTGAQVVVASAQYSArwtsSSCHVVTVSkALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHR 3627
Cdd:PRK09088    84 SELDALLQDAEPRLLLGDDAVAA----GRTDVEDLA-AFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSER 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3628 AVATSCLGHGRafgitnLSRVLQFASYTFDACIAEII-------TTLLCGGCICVPSDSDRRNSLAK-AISTMDVNWAFL 3699
Cdd:PRK09088   159 NLQQTAHNFGV------LGRVDAHSSFLCDAPMFHIIglitsvrPVLAVGGSILVSNGFEPKRTLGRlGDPALGITHYFC 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3700 TPSVARLL------DPGLIPSLKILAIGGEQSSSADWNRW-PGSVQKIHVYGPTEC---------CIFCTGYTTKQGFEP 3763
Cdd:PRK09088   233 VPQMAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWlDDGIPMVDGFGMSEAgtvfgmsvdCDVIRAKAGAAGIPT 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3764 STIGTSVasvswvVDpeNHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpAWllegypghpgrqgrlYKTGDL 3843
Cdd:PRK09088   313 PTVQTRV------VD--DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGD-GW---------------FRTGDI 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3844 VQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHAMLAAFVQLEEGTqnalldkea 3923
Cdd:PRK09088   369 ARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLAD-HPGIRECAV-VGMADAQWGEVGYLAIVPADGAP--------- 437
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 3924 ggedsmaqvVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGAS 3980
Cdd:PRK09088   438 ---------LDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
PRK06178 PRK06178
acyl-CoA synthetase; Validated
7591-8122 6.42e-26

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 117.45  E-value: 6.42e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7591 RQQLwAWNADVP-----PAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVV----P 7661
Cdd:PRK06178    13 LQQA-AWPAGIPrepeyPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVavflP 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7662 LC--FeksmwtVVAMLAVLKAGGAFVPLDPdhPASRHEEIFE--QTGAQVVVASAQY-----SARWTSSSCHVVTVSKA- 7731
Cdd:PRK06178    92 NCpqF------HIVFFGILKLGAVHVPVSP--LFREHELSYElnDAGAEVLLALDQLapvveQVRAETSLRHVIVTSLAd 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7732 -LSSQ----LPAVVDSTNTSV--------------RPENA--------AYIIFTSGSTGVPKGVVLEHR-----AVATSC 7779
Cdd:PRK06178   164 vLPAEptlpLPDSLRAPRLAAagaidllpalractAPVPLpppaldalAALNYTGGTTGMPKGCEHTQRdmvytAAAAYA 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7780 LGHGRAFGITNLSRVLQFASYTFDACiaeIITTLLCGGCICVPSDSDRRNSLAkAISTMDVNWAFLT-PSVARLLD-PGL 7857
Cdd:PRK06178   244 VAVVGGEDSVFLSFLPEFWIAGENFG---LLFPLFSGATLVLLARWDAVAFMA-AVERYRVTRTVMLvDNAVELMDhPRF 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7858 ----IPSLK-ILAIGGEQSSSADW-NRW---PGSVQKIHVYGPTE---CCIFCTGYTTKQ---GFEPSTIGTSVASVSW- 7921
Cdd:PRK06178   320 aeydLSSLRqVRVVSFVKKLNPDYrQRWralTGSVLAEAAWGMTEthtCDTFTAGFQDDDfdlLSQPVFVGLPVPGTEFk 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7922 VVDPENHnRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdpAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYL 8001
Cdd:PRK06178   400 ICDFETG-ELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD--GWL---------------HTGDIGKIDEQGFLHYL 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8002 GRKDSQVKVRGQRVELGEVE----HHvreclPEARQLAVeVILPSGQKNHAMLAvFVQLGKGTHIahleekaggedsmaq 8077
Cdd:PRK06178   462 GRRKEMLKVNGMSVFPSEVEallgQH-----PAVLGSAV-VGRPDPDKGQVPVA-FVQLKPGADL--------------- 519
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 8078 vvfltgTEEELAKRLPKHM----VPTVFFaLLHFPMTTSGKADRKRLRE 8122
Cdd:PRK06178   520 ------TAAALQAWCRENMavykVPEIRI-VDALPMTATGKVRKQDLQA 561
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
3440-3976 6.69e-26

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 117.16  E-value: 6.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3440 LTYNESKK-------IWGwnadvppaiERCVHDLFTEQAKARPHAPAICAWDG-ELTYGELDALSSKLASHLVQLGVNPE 3511
Cdd:PRK06087     4 LTFNEQRRaayrqqgYWG---------DASLADYWQQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3512 DVVplCFEKSMWT--VVAMLAVLKAGGAFVPLDpdhPASRHEEI---FEQTGAQVVVASAQYSARWTSS---SC------ 3577
Cdd:PRK06087    75 DRV--AFQLPGWCefTIIYLACLKVGAVSVPLL---PSWREAELvwvLNKCQAKMFFAPTLFKQTRPVDlilPLqnqlpq 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3578 --HVVTVSK---ALSSQLPAVVDSTNTS------VRPENAAYIIFTSGSTGVPKGVVLEHRAVATSclghGRAF-GITNL 3645
Cdd:PRK06087   150 lqQIVGVDKlapATSSLSLSQIIADYEPlttaitTHGDELAAVLFTSGTEGLPKGVMLTHNNILAS----ERAYcARLNL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3646 SRV--------LQFASYTFDAciaeIITTLLCGGCICVpsdSDRRNSlAKAISTMD---VNWAF-LTPSVARLL-----D 3708
Cdd:PRK06087   226 TWQdvfmmpapLGHATGFLHG----VTAPFLIGARSVL---LDIFTP-DACLALLEqqrCTCMLgATPFIYDLLnllekQ 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3709 PGLIPSLKILAIGGEQSSSADWNR-WPGSVQKIHVYGPTECC--IF-----CTGYTTkqgfepSTIGTSVASVSW-VVDp 3779
Cdd:PRK06087   298 PADLSALRFFLCGGTTIPKKVAREcQQRGIKLLSVYGSTESSphAVvnlddPLSRFM------HTDGYAAAGVEIkVVD- 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3780 ENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKd 3859
Cdd:PRK06087   371 EARKTL-PPGCEGEEASRGPNVFMGYLDEPELTARA-LDEEGW---------------YYSGDLCRMDEAGYIKITGRK- 432
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3860 SQVKVR-GQRVELGEVEHHVREClPEARQLAVeVILPS---GQKdhamLAAFVQLEEGTQNALLdkeaggEDSMAqvvFL 3935
Cdd:PRK06087   433 KDIIVRgGENISSREVEDILLQH-PKIHDACV-VAMPDerlGER----SCAYVVLKAPHHSLTL------EEVVA---FF 497
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 3936 AsvEEELAKRL-PEHMVptvffSLLHFPTTTSGKTDRKRLRE 3976
Cdd:PRK06087   498 S--RKRVAKYKyPEHIV-----VIDKLPRTASGKIQKFLLRK 532
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
428-818 6.73e-26

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 115.20  E-value: 6.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  428 SPLQEGlMSLTTKRAGD---YIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSElGLLQVVVEEKMQ------ 498
Cdd:cd19066      5 SPMQRG-MWFLKKLATDpsaFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAG-RYEQVVLDKTVRfrieii 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  499 ----WTESES-LEEYLNEDKAASMGL-GDRLARYALIKesCGGKRW-FVWTIHHALYDGWSLPLVLDAVKQVYSGAALER 571
Cdd:cd19066     83 dlrnLADPEArLLELIDQIQQTIYDLeRGPLVRVALFR--LADERDvLVVAIHHIIVDGGSFQILFEDISSVYDAAERQK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  572 Q---PSFNTFIQYVSQQ-------DVKAAAAYWQTALADCEAVL-FPPLPSTVTQPVADTTVKYQCPPSPE-------VT 633
Cdd:cd19066    161 PtlpPPVGSYADYAAWLekqleseAAQADLAYWTSYLHGLPPPLpLPKAKRPSQVASYEVLTLEFFLRSEEtkrlrevAR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  634 SSNITTSTLIRAAWAIIASRYTSSEDIVFGTTVTGRNAPitGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEM 713
Cdd:cd19066    241 ESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREA 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  714 IAYEQTG---LQRIMKMGPGPQHACGFQTLLVVHPTDDVLSSDD--TLGEWHSRSDSELQYFTTYALTIQCTlavEGVQI 788
Cdd:cd19066    319 IEHQRVPfieLVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGgfIFTTPVYTSSEGTVFDLDLEASEDPD---GDLLL 395
                          410       420       430
                   ....*....|....*....|....*....|
gi 1820002560  789 TASFDARVVEHWVVEKMLGQFSFVMQQLAE 818
Cdd:cd19066    396 RLEYSRGVYDERTIDRFAERYMTALRQLIE 425
PRK06145 PRK06145
acyl-CoA synthetase; Validated
5632-6137 6.97e-26

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 116.14  E-value: 6.97e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 5711
Cdd:PRK06145    12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5712 EDTFRHTGAQVVVTSAQHSARwIGTNHQVVTVSAGSLGQLSTLVNPvGLPAIPENA------VYIMFTSGSTGIPKGVVL 5785
Cdd:PRK06145    92 AYILGDAGAKLLLVDEEFDAI-VALETPKIVIDAAAQADSRRLAQG-GLEIPPQAAvaptdlVRLMYTSGTTDRPKGVMH 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5786 EHRAVVTSCWGRGRAFGITNLSRVLQFAS-YTFDACMDEIITTLMYGGCICVPSDSDRRNDLvKAISTMDVSCALLTP-S 5863
Cdd:PRK06145   170 SYGNLHWKSIDHVIALGLTASERLLVVGPlYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVL-AAIERHRLTCAWMAPvM 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5864 VARLL---EPS--SVPTLQMLVLQGE---QVSFADWNRWPASVQTINGYGPTE-CSICCNTYSGKQGFKSGIIGTSVASV 5934
Cdd:PRK06145   249 LSRVLtvpDRDrfDLDSLAWCIGGGEktpESRIRDFTRVFTRARYIDAYGLTEtCSGDTLMEAGREIEKIGSTGRALAHV 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5935 SWVVDPENHDRLAPlGSIGELLVEGPILARGYLNDIQKTAAVFIDDpaWLlegypghpgrqgrlyKTGDLVRYDANGNLV 6014
Cdd:PRK06145   329 EIRIADGAGRWLPP-NMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--WF---------------RSGDVGYLDEEGFLY 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6015 CLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAveVILPSGQKDHAMLAAFVQLEEGtqnalldkeasgedsmaQVV 6094
Cdd:PRK06145   391 LTDRKKDMIISGGENIASSEVERVIYE-LPEVAEAA--VIGVHDDRWGERITAVVVLNPG-----------------ATL 450
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 6095 FLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:PRK06145   451 TLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
1944-2444 7.01e-26

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 115.46  E-value: 7.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1944 HAPAICAWDGELTYGELDALSSKLASHLVQLG-VNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIF 2022
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2023 RQTGAQVVVtsaqhsarwigtnhqvvtvsagsleqfstlvnpvdlpakpeNAAYVMFTSGSTGTPKGVVLEHRAVvtscl 2102
Cdd:cd05941     81 TDSEPSLVL-----------------------------------------DPALILYTSGTTGRPKGVVLTHANL----- 114
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2103 ghgqAFGVTNLLRALQFTAYtfDVCI-------------AEIITTLVHGGCICVPSDSERRDNLAKAITDMQVNWGylts 2169
Cdd:cd05941    115 ----AANVRALVDAWRWTED--DVLLhvlplhhvhglvnALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMG---- 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2170 svarlldpclVPSLKVLVLGGEQVNSTDW----------------GKWPSSVQT------ING------YGPTECCV-FC 2220
Cdd:cd05941    185 ----------VPTIYTRLLQYYEAHFTDPqfaraaaaerlrlmvsGSAALPVPTleeweaITGhtllerYGMTEIGMaLS 254
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2221 TGYTGIQgfQSGNIGTSIASVSWVVDPENHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpawlleGYpgheg 2300
Cdd:cd05941    255 NPLDGER--RPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDD------GW----- 321
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2301 rqgrlYKTGDLVRYSSDGNLVCLGR-KDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVPPS--GERdhamLAAFIR 2377
Cdd:cd05941    322 -----FKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLA-HPGVSECAVIGVPDPdwGER----VVAVVV 391
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 2378 LDDEtrnspliikyaednstAQIVFLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:cd05941    392 LRAG----------------AAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
PRK06178 PRK06178
acyl-CoA synthetase; Validated
829-1366 7.21e-26

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 117.06  E-value: 7.21e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  829 ETTTLEDRQQLW--VWNADMP-----PAVDRCIHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKR 901
Cdd:PRK06178     3 EEAYLAELRALQqaAWPAGIPrepeyPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  902 EDVV----PLC--FeksmwtVVAMLAVLKAGGAFVPLDpghPASRHEEIFKQI---GAQVVLTSSQHAMLfASSERHQVT 972
Cdd:PRK06178    83 GDRVavflPNCpqF------HIVFFGILKLGAVHVPVS---PLFREHELSYELndaGAEVLLALDQLAPV-VEQVRAETS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  973 VSKVSTSQL-------PTV---------------------------VNFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHR 1018
Cdd:PRK06178   153 LRHVIVTSLadvlpaePTLplpdslraprlaaagaidllpalractAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1019 -AVTTSCLGHGEAFGYTDHARVLQF------ASYTFDaciaeIITTLLYGGCICVPSESDRRNNLAkAISTMDVN-CALL 1090
Cdd:PRK06178   233 dMVYTAAAAYAVAVVGGEDSVFLSFlpefwiAGENFG-----LLFPLFSGATLVLLARWDAVAFMA-AVERYRVTrTVML 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1091 TPSVARLLEPSAV-----PSLKrlvlQGEQVSF-----ADW-NRW---PGSVQTINGYGPTECSVcCNTYSgkQGFKSG- 1155
Cdd:PRK06178   307 VDNAVELMDHPRFaeydlSSLR----QVRVVSFvkklnPDYrQRWralTGSVLAEAAWGMTETHT-CDTFT--AGFQDDd 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1156 -------------IIGTSVAslswVVDAGNHnRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDdpAWLlegyegha 1222
Cdd:PRK06178   380 fdllsqpvfvglpVPGTEFK----ICDFETG-ELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD--GWL-------- 444
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1223 grrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIE----HHvreclPEARQLAVeVILPS---GQkehaLL 1295
Cdd:PRK06178   445 -------HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEallgQH-----PAVLGSAV-VGRPDpdkGQ----VP 507
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 1296 AAFIQLDKGnhnalfeekaSGEDsmaqvvfltgvEEELAKRLPEHM----VPTILFtVKAMPITTSGKIDRKRLQ 1366
Cdd:PRK06178   508 VAFVQLKPG----------ADLT-----------AAALQAWCRENMavykVPEIRI-VDALPMTATGKVRKQDLQ 560
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
7609-8023 7.84e-26

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 116.18  E-value: 7.84e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7609 VHDLFAEQARARPGAPA-ICAWDG-ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP 7686
Cdd:cd05904      7 LDSVSFLFASAHPSRPAlIDAATGrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7687 LdpdHPASRHEEIFEQ---TGAQVVVASAQYSARWTSSSCHVVTVSKALSSQLPAVVDSTNTS--------VRPENAAYI 7755
Cdd:cd05904     87 A---NPLSTPAEIAKQvkdSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADeaeppvvvIKQDDVAAL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7756 IFTSGSTGVPKGVVLEHR-AVATSCLGH-GRAFGITNLSRVL----QFASYTFDACiaeIITTLLCGGCICVPSDSDRRN 7829
Cdd:cd05904    164 LYSSGTTGRSKGVMLTHRnLIAMVAQFVaGEGSNSDSEDVFLcvlpMFHIYGLSSF---ALGLLRLGATVVVMPRFDLEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7830 SLAkAISTMDVNWAFLTPSV------ARLLDPGLIPSLKILAIG----GEQSSSADWNRWPgSVQKIHVYGPTE-CCIFC 7898
Cdd:cd05904    241 LLA-AIERYKVTHLPVVPPIvlalvkSPIVDKYDLSSLRQIMSGaaplGKELIEAFRAKFP-NVDLGQGYGMTEsTGVVA 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7899 TGYTT-KQGFEPSTIGTSVASV-SWVVDPENhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypgh 7976
Cdd:cd05904    319 MCFAPeKDRAKYGSVGRLVPNVeAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLNNPEATAAT-IDKEGWL------- 389
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 7977 pgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHH 8023
Cdd:cd05904    390 --------HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEAL 428
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
856-1367 8.66e-26

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 117.02  E-value: 8.66e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  856 DLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPG 935
Cdd:PRK05605    36 DLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPL 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  936 HPASRHEEIFKQIGAQVVLTSSQHAMLF-----------------------------------ASSERHQVTV------- 973
Cdd:PRK05605   116 YTAHELEHPFEDHGARVAIVWDKVAPTVerlrrttpletivsvnmiaampllqrlalrlpipaLRKARAALTGpapgtvp 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  974 -SKVSTSQLPTVVNFAKSP-VDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLgHGEAF--GYTDHARVLQFASYTFDA 1049
Cdd:PRK05605   196 wETLVDAAIGGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAA-QGKAWvpGLGDGPERVLAALPMFHA 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1050 ciaeiittllYGGCICVpsesdrrnNLAKAI-STMdvnCALLTPSVARLLE------PS---AVPSL----------KRL 1109
Cdd:PRK05605   275 ----------YGLTLCL--------TLAVSIgGEL---VLLPAPDIDLILDamkkhpPTwlpGVPPLyekiaeaaeeRGV 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1110 VLQGEQVSF-----------ADWNRWPGSVqTINGYGPTECS--VCCNTYSGKQgfKSGIIG-----TSVAslswVVDAG 1171
Cdd:PRK05605   334 DLSGVRNAFsgamalpvstvELWEKLTGGL-LVEGYGLTETSpiIVGNPMSDDR--RPGYVGvpfpdTEVR----IVDPE 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1172 NHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpaWllegyeghagrrgrlYKTGDLVRCDADGNLVCLGRKDS 1251
Cdd:PRK05605   407 DPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--W---------------FRTGDVVVMEEDGFIRIVDRIKE 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1252 QVKVRGQRVELGEIEHHVREcLPEARQLAVeVILPSGQKEHALLAAfIQLDKGnhnALFEEKasgedsmaqvvfltGVEE 1331
Cdd:PRK05605   470 LIITGGFNVYPAEVEEVLRE-HPGVEDAAV-VGLPREDGSEEVVAA-VVLEPG---AALDPE--------------GLRA 529
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1820002560 1332 ELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:PRK05605   530 YCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
PRK06145 PRK06145
acyl-CoA synthetase; Validated
1939-2444 9.48e-26

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 115.75  E-value: 9.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 2018
Cdd:PRK06145    12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2019 EDIFRQTGAQVVVTSAQHSARwIGTNHQVVTVSAGSLEQFSTLVNPVD-----LPAKPENAAYVMFTSGSTGTPKGVVLE 2093
Cdd:PRK06145    92 AYILGDAGAKLLLVDEEFDAI-VALETPKIVIDAAAQADSRRLAQGGLeippqAAVAPTDLVRLMYTSGTTDRPKGVMHS 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2094 HRAVVTSCLGHGQAFGVTNLLRALQFTA-YTFDVCIAEIITTLVHGGCICVPSDSERRDNLAkAITDMQVNWGYL----T 2168
Cdd:PRK06145   171 YGNLHWKSIDHVIALGLTASERLLVVGPlYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA-AIERHRLTCAWMapvmL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2169 SSVARLLDPCL--VPSLKVLVLGGEQVNST---DWGKWPSSVQTINGYGPTECCvfcTGYT----GIQGFQSGNIGTSIA 2239
Cdd:PRK06145   250 SRVLTVPDRDRfdLDSLAWCIGGGEKTPESrirDFTRVFTRARYIDAYGLTETC---SGDTlmeaGREIEKIGSTGRALA 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2240 SVSWVVDPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpaWLLEGYPGHEGRQGRLYKTgdlvryssdgn 2319
Cdd:PRK06145   327 HVEIRIADGA-GRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--WFRSGDVGYLDEEGFLYLT----------- 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2320 lvclGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVPPS--GERDHAMLAAfirlddetrnspliikyaednST 2397
Cdd:PRK06145   393 ----DRKKDMIISGGENIASSEVERVIYE-LPEVAEAAVIGVHDDrwGERITAVVVL---------------------NP 446
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 2398 AQIVFLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:PRK06145   447 GATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
3471-3877 1.01e-25

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 115.80  E-value: 1.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPA-ICAWDG-ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHPAS 3548
Cdd:cd05904     15 ASAHPSRPAlIDAATGrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA---NPLS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3549 RHEEIFEQ---TGAQVVVASAQYSARWTSSSCHVVTVSKALSSQLPAVVDSTNTS--------VRPENAAYIIFTSGSTG 3617
Cdd:cd05904     92 TPAEIAKQvkdSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADeaeppvvvIKQDDVAALLYSSGTTG 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3618 VPKGVVLEHR-AVATSCLGH-GRAFGITNLSRVL----QFASYTFDACiaeIITTLLCGGCICVPSDSDRRNSLAkAIST 3691
Cdd:cd05904    172 RSKGVMLTHRnLIAMVAQFVaGEGSNSDSEDVFLcvlpMFHIYGLSSF---ALGLLRLGATVVVMPRFDLEELLA-AIER 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3692 MDVNWAFLTPSV------ARLLDPGLIPSLKILAIG----GEQSSSADWNRWPgSVQKIHVYGPTE-CCIFCTGYTT-KQ 3759
Cdd:cd05904    248 YKVTHLPVVPPIvlalvkSPIVDKYDLSSLRQIMSGaaplGKELIEAFRAKFP-NVDLGQGYGMTEsTGVVAMCFAPeKD 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3760 GFEPSTIGTSVASV-SWVVDPENhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrly 3838
Cdd:cd05904    327 RAKYGSVGRLVPNVeAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLNNPEATAAT-IDKEGWL--------------- 389
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1820002560 3839 KTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHH 3877
Cdd:cd05904    390 HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEAL 428
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
1953-2367 1.06e-25

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 115.51  E-value: 1.06e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1953 GELTYGELdALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGgaFVPLDPDHPASRHEDI--FRQTGAQVV 2030
Cdd:cd05909      6 TSLTYRKL-LTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAGLRELRacIKLAGIKTV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2031 VTSAQ--------------HSARW---------IGTNHQVVTVSAGSLEQFSTLVNPVDLPAKPENAAYVMFTSGSTGTP 2087
Cdd:cd05909     83 LTSKQfieklklhhlfdveYDARIvyledlrakISKADKCKAFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2088 KGVVLEHRAVVTS---CLGHGQAFGVTNLLRALQ-FTAYTFDVCiaeIITTLVHGGCI-CVPSDSERRdNLAKAITDMQV 2162
Cdd:cd05909    163 KGVVLSHKNLLANveqITAIFDPNPEDVVFGALPfFHSFGLTGC---LWLPLLSGIKVvFHPNPLDYK-KIPELIYDKKA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2163 NWGYLTSS----VARLLDPCLVPSLKVLVLGGEQVNSTDWGKWPSS--VQTINGYGPTECCVFCTGYTGIQGFQSGNIGT 2236
Cdd:cd05909    239 TILLGTPTflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSPVISVNTPQSPNKEGTVGR 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2237 SIASVSW-VVDPENHGRLaPLGSIGELLVEGPILARGYLNDVDKTQAAFiddpawllegypgHEGrqgrLYKTGDLVRYS 2315
Cdd:cd05909    319 PLPGMEVkIVSVETHEEV-PIGEGGLLLVRGPNVMLGYLNEPELTSFAF-------------GDG----WYDTGDIGKID 380
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 2316 SDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKCLPEANQLAVEVVPPS--GER 2367
Cdd:cd05909    381 GEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPDGrkGEK 434
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
1943-2444 1.12e-25

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 115.49  E-value: 1.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1943 PHAPAICAWDG--ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHED 2020
Cdd:cd05926      1 PDAPALVVPGStpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2021 IFRQTGAQVVVTS---------AQHSARW------IGTNHQVVTVSAGSL--EQFSTLVNPVDLPAKPENAAYVMFTSGS 2083
Cdd:cd05926     81 YLADLGSKLVLTPkgelgpasrAASKLGLailelaLDVGVLIRAPSAESLsnLLADKKNAKSEGVPLPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2084 TGTPKGVVLEHRAVVTSclghgqafgVTNLLRALQFTAYTFDVC----------IAEIITTLVHGGCICVP---SDSERR 2150
Cdd:cd05926    161 TGRPKGVPLTHRNLAAS---------ATNITNTYKLTPDDRTLVvmplfhvhglVASLLSTLAAGGSVVLPprfSASTFW 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2151 DNLAKAitdmQVNWgyLTSsvarlldpclVPSLKVLVLGGEQvnsTDWGKWPSS------------------------VQ 2206
Cdd:cd05926    232 PDVRDY----NATW--YTA----------VPTIHQILLNRPE---PNPESPPPKlrfirscsaslppavlealeatfgAP 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2207 TINGYGPTECC--VFCTGYTGIQGfQSGNIGtsIASVSWVVDPENHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAF 2284
Cdd:cd05926    293 VLEAYGMTEAAhqMTSNPLPPGPR-KPGSVG--KPVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2285 IDDPaWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKClPEANQLAVEVVPps 2364
Cdd:cd05926    370 FKDG-WF---------------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH-PAVLEAVAFGVP-- 430
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2365 gerdHAMLaafirldDETRNSPLIIKYAEDNSTAQIVfltgieEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:cd05926    431 ----DEKY-------GEEVAAAVVLREGASVTEEELR------AFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1933-2395 1.18e-25

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 116.74  E-value: 1.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDG----ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP 2008
Cdd:COG1022     15 DLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2009 LDPDHPASRHEDIFRQTGAQVVVTSAQ-HSARWIGTNHQ------VVTVSAG---------SLEQFSTLVNPVDLPA--- 2069
Cdd:COG1022     95 IYPTSSAEEVAYILNDSGAKVLFVEDQeQLDKLLEVRDElpslrhIVVLDPRglrddprllSLDELLALGREVADPAele 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2070 ------KPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLRALQF--TAYTFDVCIAeiITTLVHGGCI 2141
Cdd:COG1022    175 arraavKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlpLAHVFERTVS--YYALAAGATV 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2142 CVPSDSER-RDNL-------------------AKAITDMQ---------VNWGYLTS---SVARLLDPCLVPSLKVL--- 2186
Cdd:COG1022    253 AFAESPDTlAEDLrevkptfmlavprvwekvyAGIQAKAEeagglkrklFRWALAVGrryARARLAGKSPSLLLRLKhal 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2187 -----------VLGGEqvnstdwGKWPSS-----------------VQTINGYGPTECCVFCTGYTgIQGFQSGNIGTSI 2238
Cdd:COG1022    333 adklvfsklreALGGR-------LRFAVSggaalgpelarffralgIPVLEGYGLTETSPVITVNR-PGDNRIGTVGPPL 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2239 ASVSWVVDPEnhgrlaplgsiGELLVEGPILARGYLNDVDKTQAAFIDDpAWLlegypghegrqgrlyKTGDLVRYSSDG 2318
Cdd:COG1022    405 PGVEVKIAED-----------GEILVRGPNVMKGYYKNPEATAEAFDAD-GWL---------------HTGDIGELDEDG 457
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 2319 NLVCLGRKDSQVKVR-GQRVELGEVEHHMRKClPEANQlAVeVVppsGErDHAMLAAFIRLDDETrnsplIIKYAEDN 2395
Cdd:COG1022    458 FLRITGRKKDLIVTSgGKNVAPQPIENALKAS-PLIEQ-AV-VV---GD-GRPFLAALIVPDFEA-----LGEWAEEN 523
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
862-1362 1.32e-25

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 116.18  E-value: 1.32e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  862 ARARPDASAVCAWDGE------LTYGELDELSSKLAAHLVQLGvKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL--- 932
Cdd:cd05931      3 AAARPDRPAYTFLDDEggreetLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppp 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  933 DPGHPASRHEEIFKQIGAQVVLTSSQHAML---FASSERHQVTVSKVSTSQLPTVVN--FAKSPVDPGNTAYIIFTSGTT 1007
Cdd:cd05931     82 TPGRHAERLAAILADAGPRVVLTTAAALAAvraFAASRPAAGTPRLLVVDLLPDTSAadWPPPSPDPDDIAYLQYTSGST 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1008 GIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFD-ACIAEIITTLLYGGCiCV---PSESDRRNNL-AKAIST 1082
Cdd:cd05931    162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmGLIGGLLTPLYSGGP-SVlmsPAAFLRRPLRwLRLISR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1083 MDVNC--------ALLTPSVARL-LEPSAVPSLKRLVLQGEQVS----------FADWNRWPGSVQTinGYGPTECSVcc 1143
Cdd:cd05931    241 YRATIsaapnfayDLCVRRVRDEdLEGLDLSSWRVALNGAEPVRpatlrrfaeaFAPFGFRPEAFRP--SYGLAEATL-- 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1144 nTYSGKQGFKSGII----------------------------GTSVASLSWVVDAGNHNRLAPLGSIGELLVEGPILARG 1195
Cdd:cd05931    317 -FVSGGPPGTGPVVlrvdrdalagravavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASG 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1196 YLNDIDKTEAAFiddpawlleGYEGHAGRRGRLyKTGDL-VRcdADGNLVCLGRKDSQVKVRGQRVELGEIEHHVRECLP 1274
Cdd:cd05931    396 YWGRPEATAETF---------GALAATDEGGWL-RTGDLgFL--HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHP 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1275 EARQLAVEVI-LPSGQKEHALLAAfiqldkgnhnalfeEKASGEDSMAQVVFLTGVEEELAKrlpEH--MVPTILFtVK- 1350
Cdd:cd05931    464 ALRPGCVAAFsVPDDGEERLVVVA--------------EVERGADPADLAAIAAAIRAAVAR---EHgvAPADVVL-VRp 525
                          570
                   ....*....|...
gi 1820002560 1351 -AMPITTSGKIDR 1362
Cdd:cd05931    526 gSIPRTSSGKIQR 538
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
5630-6137 1.35e-25

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 115.77  E-value: 1.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5630 EQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 5709
Cdd:PRK07656    13 RAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5710 RHEDTFRHTGAQVVVT---------SAQHSarwIGTNHQVVTVSAGSLGQLSTLVNPV------GLPAIPENAVY----- 5769
Cdd:PRK07656    93 EAAYILARGDAKALFVlglflgvdySATTR---LPALEHVVICETEEDDPHTEKMKTFtdflaaGDPAERAPEVDpddva 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 -IMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQ----FASYTFDACMdeiITTLMYGGCIcVPSDSDRRN 5844
Cdd:PRK07656   170 dILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAanpfFHVFGYKAGV---NAPLMRGATI-LPLPVFDPD 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5845 DLVKAISTMDVSCAlltpsvarllepSSVPTLQMLVLQGEQVSFADWN--RWPAS------------------VQTI-NG 5903
Cdd:PRK07656   246 EVFRLIETERITVL------------PGPPTMYNSLLQHPDRSAEDLSslRLAVTgaasmpvallerfeselgVDIVlTG 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5904 YGPTECS--ICCNTYSGKQGFKSGIIGTSVASVSW-VVDPenHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVfIDD 5980
Cdd:PRK07656   314 YGLSEASgvTTFNRLDDDRKTVAGTIGTAIAGVENkIVNE--LGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA-IDA 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5981 PAWLlegypgHpgrqgrlykTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECLPEARQLA-VEVIlpsGQ 6059
Cdd:PRK07656   391 DGWL------H---------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVE----EVLYEHPAVAeAAVI---GV 448
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6060 KDHAM---LAAFVQLEEGTQnalLDKEAsgedsmaqvvFLASVEEELAKrlpeHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:PRK07656   449 PDERLgevGKAYVVLKPGAE---LTEEE----------LIAYCREHLAK----YKVPRSIEFLDELPKNATGKVLKRALR 511

                   .
gi 1820002560 6137 E 6137
Cdd:PRK07656   512 E 512
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
3471-3976 1.85e-25

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 115.41  E-value: 1.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGE------LTYGELDALSSKLASHLVQLGvNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 3544
Cdd:cd05931      3 AAARPDRPAYTFLDDEggreetLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3545 HPASRHEE---IFEQTGAQVVVASAQYSA---RWTSSSCHVVTVSKALSSQLPAVV--DSTNTSVRPENAAYIIFTSGST 3616
Cdd:cd05931     82 TPGRHAERlaaILADAGPRVVLTTAAALAavrAFAASRPAAGTPRLLVVDLLPDTSaaDWPPPSPDPDDIAYLQYTSGST 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3617 GVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFD-ACIAEIITTLLCGGCiCV---PSDSDRRNSL-AKAIST 3691
Cdd:cd05931    162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmGLIGGLLTPLYSGGP-SVlmsPAAFLRRPLRwLRLISR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3692 MDVNWAFlTPS------VARLLDPGLIP----SLKILAIGGEQSSSADWNRW---------------PGsvqkihvYGPT 3746
Cdd:cd05931    241 YRATISA-APNfaydlcVRRVRDEDLEGldlsSWRVALNGAEPVRPATLRRFaeafapfgfrpeafrPS-------YGLA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3747 ECCIFCTGYTTKQGF------------------EPSTIGTSVASVSWV--------VDPENHNRLAPlGSMGELLMEGPI 3800
Cdd:cd05931    313 EATLFVSGGPPGTGPvvlrvdrdalagravavaADDPAARELVSCGRPlpdqevriVDPETGRELPD-GEVGEIWVRGPS 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3801 LARGYLNDVDKTEAAF-----IDDPAWLlegypghpgrqgrlyKTGDLvQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 3875
Cdd:cd05931    392 VASGYWGRPEATAETFgalaaTDEGGWL---------------RTGDL-GFLHDGELYITGRLKDLIIVRGRNHYPQDIE 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3876 HHVRECLPEARQLAVevilpsgqkdhamlAAF-VQLEEGTQNALLDKEAGGEDSMAQVVFLASVEEELAKrlpEHMVPT- 3953
Cdd:cd05931    456 ATAEEAHPALRPGCV--------------AAFsVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAR---EHGVAPa 518
                          570       580
                   ....*....|....*....|....*
gi 1820002560 3954 --VFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:cd05931    519 dvVLVRPGSIPRTSSGKIQRRACRA 543
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
1932-2456 2.33e-25

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 117.72  E-value: 2.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1932 HDLFTEQAKARPHAPAICawD---GELTYGELDALSSKLAsHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP 2008
Cdd:PRK08633   618 AEAWIDTAKRNWSRLAVA--DstgGELSYGKALTGALALA-RLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVN 694
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2009 LDpdHPASrhEDIFR----QTGAQVVVTS--------AQHSARWIGTNHQVVTV-----SAGSLEQFSTLVNPVDLPA-- 2069
Cdd:PRK08633   695 LN--YTAS--EAALKsaieQAQIKTVITSrkfleklkNKGFDLELPENVKVIYLedlkaKISKVDKLTALLAARLLPArl 770
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2070 ---------KPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTN---------LLRALQFTAYTFDVCIAEI 2131
Cdd:PRK08633   771 lkrlygptfKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNddvilsslpFFHSFGLTVTLWLPLLEGI 850
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2132 ittlvhgGCICVPSDSERRdNLAKAITDMQVNWGYLTSSVARL------LDPCLVPSLKVLVLGGEQVNS-------TDW 2198
Cdd:PRK08633   851 -------KVVYHPDPTDAL-GIAKLVAKHRATILLGTPTFLRLylrnkkLHPLMFASLRLVVAGAEKLKPevadafeEKF 922
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2199 GKWPssvqtINGYGPTECC---------VFCTGYTGIQGFQSGNIGTSIASVSW-VVDPENHGRLAPlGSIGELLVEGPI 2268
Cdd:PRK08633   923 GIRI-----LEGYGATETSpvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVrIVDPETFEELPP-GEDGLILIGGPQ 996
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2269 LARGYLNDVDKTQAAF--IDDPAWllegypghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHM 2346
Cdd:PRK08633   997 VMKGYLGDPEKTAEVIkdIDGIGW---------------YVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL 1061
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2347 RKCLPEANQ-LAVEVVPpsgerdhamlaafirldDETRNSPLIIKYAEDNSTAQivfltGIEEELSE-RLPQHMVPTVFF 2424
Cdd:PRK08633  1062 AKALGGEEVvFAVTAVP-----------------DEKKGEKLVVLHTCGAEDVE-----ELKRAIKEsGLPNLWKPSRYF 1119
                          570       580       590
                   ....*....|....*....|....*....|..
gi 1820002560 2425 ALVHFPTTTSGKTDRKRLREIgasftAQQLAE 2456
Cdd:PRK08633  1120 KVEALPLLGSGKLDLKGLKEL-----ALALLG 1146
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
1939-2345 3.18e-25

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 114.25  E-value: 3.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPA-ICAWDG-ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHPAS 2016
Cdd:cd05904     15 ASAHPSRPAlIDAATGrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA---NPLS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2017 RHEDIFRQ---TGAQVVVTSAQHSARWIGTNHQVVTV----SAGSLEQFSTLVNPVDLPAKPE----NAAYVMFTSGSTG 2085
Cdd:cd05904     92 TPAEIAKQvkdSGAKLAFTTAELAEKLASLALPVVLLdsaeFDSLSFSDLLFEADEAEPPVVVikqdDVAALLYSSGTTG 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2086 TPKGVVLEHRAVVTSCL----GHGQAFGVTNLLRAL--QFTAYTFDVCiaeIITTLVHGGCICVPSDSERRDNLAkAITD 2159
Cdd:cd05904    172 RSKGVMLTHRNLIAMVAqfvaGEGSNSDSEDVFLCVlpMFHIYGLSSF---ALGLLRLGATVVVMPRFDLEELLA-AIER 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2160 MQVNWGYLTSSV------ARLLDPCLVPSLKVLVLGG--------EQVNStdwgKWPsSVQTINGYGPTE-CCVFCTGYT 2224
Cdd:cd05904    248 YKVTHLPVVPPIvlalvkSPIVDKYDLSSLRQIMSGAaplgkeliEAFRA----KFP-NVDLGQGYGMTEsTGVVAMCFA 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2225 GIQG-FQSGNIGTSIASV-SWVVDPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAfIDDPAWLlegypghegrq 2302
Cdd:cd05904    323 PEKDrAKYGSVGRLVPNVeAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLNNPEATAAT-IDKEGWL----------- 389
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 2303 grlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHH 2345
Cdd:cd05904    390 ----HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEAL 428
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
4544-5068 4.00e-25

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 116.95  E-value: 4.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4544 HDQFAEQARARPDTPAICawD---GELTYGELDTLSSKLAsHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVP 4620
Cdd:PRK08633   618 AEAWIDTAKRNWSRLAVA--DstgGELSYGKALTGALALA-RLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVN 694
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4621 LDpdHPASRH--EHIFRQTGAQVVLAS--------AQYATLWTSLGRSVV----IVSEASTSQ----------LPV--VT 4674
Cdd:PRK08633   695 LN--YTASEAalKSAIEQAQIKTVITSrkfleklkNKGFDLELPENVKVIyledLKAKISKVDkltallaarlLPArlLK 772
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4675 KTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQ----FASYTFdaciaeIITTL--L 4748
Cdd:PRK08633   773 RLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGL------TVTLWlpL 846
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4749 C--CGCICVPSDSDRRnNLAKAINAMDVNWALLTPSVARM------LDPCVVQSLKILVLGGEQVNS--AD--WDRWPKS 4816
Cdd:PRK08633   847 LegIKVVYHPDPTDAL-GIAKLVAKHRATILLGTPTFLRLylrnkkLHPLMFASLRLVVAGAEKLKPevADafEEKFGIR 925
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4817 IqtINAYGPTECS--ICCTT-------YSGKQGFKSGTIGTSI--VSVSwVVDPENHNRLAPlGSIGELLVEGPILARGY 4885
Cdd:PRK08633   926 I--LEGYGATETSpvASVNLpdvlaadFKRQTGSKEGSVGMPLpgVAVR-IVDPETFEELPP-GEDGLILIGGPQVMKGY 1001
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4886 LNDMEKTEAAF--IDDPAWllegygghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVRECLT 4963
Cdd:PRK08633  1002 LGDPEKTAEVIkdIDGIGW---------------YVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALG 1066
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4964 EAKQLAVEVIVPE---GEggyaMLAAFVQLGDDTYNTLVKEKAGGDsltvqvvfldrveeelakrVPEHMMLTTFFTLEA 5040
Cdd:PRK08633  1067 GEEVVFAVTAVPDekkGE----KLVVLHTCGAEDVEELKRAIKESG-------------------LPNLWKPSRYFKVEA 1123
                          570       580
                   ....*....|....*....|....*...
gi 1820002560 5041 MPTTTSGKIDRKRLREIgasftAQQLAE 5068
Cdd:PRK08633  1124 LPLLGSGKLDLKGLKEL-----ALALLG 1146
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
8288-8518 4.92e-25

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 112.30  E-value: 4.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8288 IDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQ-GKLYQVIPRHQDLPFSIFEVNGaLAEESQAIHIRDL---DQTSPL 8363
Cdd:cd19543     30 ITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGlGEPLQVVLKDRKLPWRELDLSH-LSEAEQEAELEALaeeDRERGF 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8364 GL----PTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQ-----QEPLLSTTG-FHSYLAYVHNQ-RSASI 8432
Cdd:cd19543    109 DLarapLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalgegQPPSLPPVRpYRDYIAWLQRQdKEAAE 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8433 NYWSRLLKGSHITNITSKLRPKLGKDTTIRSvkvERVIRTPQLPT----------GLTMASLVSSAWAVVLSHISGEEDV 8502
Cdd:cd19543    189 AYWREYLAGFEEPTPLPKELPADADGSYEPG---EVSFELSAELTarlqelarqhGVTLNTVVQGAWALLLSRYSGRDDV 265
                          250
                   ....*....|....*.
gi 1820002560 8503 VYGLVVAGRNSDLPSI 8518
Cdd:cd19543    266 VFGTTVSGRPAELPGI 281
PRK06178 PRK06178
acyl-CoA synthetase; Validated
3451-3976 5.05e-25

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 114.37  E-value: 5.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3451 WNADVP-----PAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVV----PLC--Fe 3519
Cdd:PRK06178    18 WPAGIPrepeyPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVavflPNCpqF- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3520 ksmwtVVAMLAVLKAGGAFVPLDPdhPASRHEEIFE--QTGAQVVVASAQY-----SARWTSSSCHVVTVSKA--LSSQ- 3589
Cdd:PRK06178    97 -----HIVFFGILKLGAVHVPVSP--LFREHELSYElnDAGAEVLLALDQLapvveQVRAETSLRHVIVTSLAdvLPAEp 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3590 ---LPAVVDSTNTSV--------------RPENA--------AYIIFTSGSTGVPKGVVLEHR-----AVATSCLGHGRA 3639
Cdd:PRK06178   170 tlpLPDSLRAPRLAAagaidllpalractAPVPLpppaldalAALNYTGGTTGMPKGCEHTQRdmvytAAAAYAVAVVGG 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3640 FGITNLSRVLQFASYTFDACiaeIITTLLCGGCICVPSDSDRRNSLAkAISTMDVNWAFLT-PSVARLLD-PGL----IP 3713
Cdd:PRK06178   250 EDSVFLSFLPEFWIAGENFG---LLFPLFSGATLVLLARWDAVAFMA-AVERYRVTRTVMLvDNAVELMDhPRFaeydLS 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3714 SLK-ILAIGGEQSSSADW-NRW---PGSVQKIHVYGPTE---CCIFCTGYTTKQ---GFEPSTIGTSVASVSW-VVDPEN 3781
Cdd:PRK06178   326 SLRqVRVVSFVKKLNPDYrQRWralTGSVLAEAAWGMTEthtCDTFTAGFQDDDfdlLSQPVFVGLPVPGTEFkICDFET 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3782 HnRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdpAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQ 3861
Cdd:PRK06178   406 G-ELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD--GWL---------------HTGDIGKIDEQGFLHYLGRRKEM 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3862 VKVRGQRVELGEVE----HHvreclPEARQLAVeviLPSGQKDHAMLA-AFVQLEEGTQNAlldkeaggedsmaqvvfla 3936
Cdd:PRK06178   468 LKVNGMSVFPSEVEallgQH-----PAVLGSAV---VGRPDPDKGQVPvAFVQLKPGADLT------------------- 520
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 3937 svEEELAKRLPEHM----VPTVFFsLLHFPTTTSGKTDRKRLRE 3976
Cdd:PRK06178   521 --AAALQAWCRENMavykVPEIRI-VDALPMTATGKVRKQDLQA 561
PRK09088 PRK09088
acyl-CoA synthetase; Validated
1938-2448 5.39e-25

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 113.36  E-value: 5.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1938 QAKARPHAPAI--CAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPA 2015
Cdd:PRK09088     4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2016 SRHEDIFRQTGAQVVVTSAQHSA-RWIGTNHQVVTVSAGSLEqfstlvnPVDLP-AKPENAAYVMFTSGSTGTPKGVVLE 2093
Cdd:PRK09088    84 SELDALLQDAEPRLLLGDDAVAAgRTDVEDLAAFIASADALE-------PADTPsIPPERVSLILFTSGTSGQPKGVMLS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2094 HRAVVTSCLGHGQAFGVTNLLRALqFTAYTFDVC--IAEIITTLVHGGCICVPSDSERRDNLAK-AITDMQVNWGYLTSS 2170
Cdd:PRK09088   157 ERNLQQTAHNFGVLGRVDAHSSFL-CDAPMFHIIglITSVRPVLAVGGSILVSNGFEPKRTLGRlGDPALGITHYFCVPQ 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2171 VARLL------DPCLVPSLKVLVLGGEQVNSTDWGKW-PSSVQTINGYGPTEC---------CVFCTGYTGIQGFQSGNI 2234
Cdd:PRK09088   236 MAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWlDDGIPMVDGFGMSEAgtvfgmsvdCDVIRAKAGAAGIPTPTV 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2235 GTSiasvswVVDpeNHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpAWllegypghegrqgrlYKTGDLVRY 2314
Cdd:PRK09088   316 QTR------VVD--DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGD-GW---------------FRTGDIARR 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2315 SSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVPPS--GERDHAMLAAfirlddetrnspliikya 2392
Cdd:PRK09088   372 DADGFFWVVDRKKDMFISGGENVYPAEIEAVLAD-HPGIRECAVVGMADAqwGEVGYLAIVP------------------ 432
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 2393 ednSTAQIVFLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREIGAS 2448
Cdd:PRK09088   433 ---ADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
878-1367 6.29e-25

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 112.05  E-value: 6.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSS 957
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  958 QhamlfasserhqvtvskvstsqlptvvnfakspvDPgntAYIIFTSGTTGIPKGVVLQHRAVttscLGHG-EAFGYTD- 1035
Cdd:cd05972     81 E----------------------------------DP---ALIYFTSGTTGLPKGVLHTHSYP----LGHIpTAAYWLGl 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1036 HARVLQF----------ASYTFDACIAEIITTLLYGGCICVPSesdrrnNLAKAISTMDVNCALLTPSVARLL-----EP 1100
Cdd:cd05972    120 RPDDIHWniadpgwakgAWSSFFGPWLLGATVFVYEGPRFDAE------RILELLERYGVTSFCGPPTAYRMLikqdlSS 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1101 SAVPSLKRLVLQGEQVS--FADWNRWPGSVQTINGYGPTECSVCCNTYSGkQGFKSGIIGTSVASLSWVV--DAGnhnRL 1176
Cdd:cd05972    194 YKFSHLRLVVSAGEPLNpeVIEWWRAATGLPIRDGYGQTETGLTVGNFPD-MPVKPGSMGRPTPGYDVAIidDDG---RE 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1177 APLGSIGELLVE-GPI-LARGYLNDIDKTEAAFiddpawllegyeghagrRGRLYKTGDLVRCDADGNLVCLGRKDSQVK 1254
Cdd:cd05972    270 LPPGEEGDIAIKlPPPgLFLGYVGDPEKTEASI-----------------RGDYYLTGDRAYRDEDGYFWFVGRADDIIK 332
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1255 VRGQR-----VELGEIEHhvreclPEARQLAVeVILPS---GQkehaLLAAFIQLDKGnhnalfeekASGEDSMAqvvfl 1326
Cdd:cd05972    333 SSGYRigpfeVESALLEH------PAVAEAAV-VGSPDpvrGE----VVKAFVVLTSG---------YEPSEELA----- 387
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 1327 tgveEELA----KRLPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:cd05972    388 ----EELQghvkKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
5196-5524 9.17e-25

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 111.73  E-value: 9.17e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5196 MYPCSPLQEGlMSLTAKRAGD---YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSElGLLQVVVE----EK 5268
Cdd:cd19066      1 KIPLSPMQRG-MWFLKKLATDpsaFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAG-RYEQVVLDktvrFR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5269 IQ-------WTESKRLEEYLREDKAVSMGL-GDRLARYALIKEpydGGKRW-FVWTIHHALYDGWSLPRILQAVKQIYSG 5339
Cdd:cd19066     79 IEiidlrnlADPEARLLELIDQIQQTIYDLeRGPLVRVALFRL---ADERDvLVVAIHHIIVDGGSFQILFEDISSVYDA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5340 A------VPERQPSFNAFI----QYLGQQDLEAATLYWQTALAD-CKAALFPTLPPTVTQPVADTTVEYQCPPPSQS--- 5405
Cdd:cd19066    156 AerqkptLPPPVGSYADYAawleKQLESEAAQADLAYWTSYLHGlPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETkrl 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5406 -----ATDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQ 5480
Cdd:cd19066    236 revarESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKE 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 5481 QSTDMIAHEQTG---LQRIAKMSPGARHACGFQTLLVVQPTDDVLGS 5524
Cdd:cd19066    314 QSREAIEHQRVPfieLVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGK 360
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
1955-2445 1.44e-24

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 112.76  E-value: 1.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL-------DPDHPASRHEDIFRQTGA 2027
Cdd:cd05906     40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptydEPNARLRKLRHIWQLLGS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2028 QVVVTSAQHSARWIG----TNHQVVTVSAGSlEQFSTLVNPVDLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLG 2103
Cdd:cd05906    120 PVVLTDAELVAEFAGletlSGLPGIRVLSIE-ELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2104 HGQAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGC--ICVPSDSERRD--NLAKAITDMQVN--W------GYLTSSV 2171
Cdd:cd05906    199 KIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCqqVHVPTEEILADplRWLDLIDRYRVTitWapnfafALLNDLL 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2172 ARLLDPC-LVPSLKVLVLGGEQVnstdwgkwpsSVQTIN------------------GYGPTECCVFCTgYTgiQGFQSG 2232
Cdd:cd05906    279 EEIEDGTwDLSSLRYLVNAGEAV----------VAKTIRrllrllepyglppdairpAFGMTETCSGVI-YS--RSFPTY 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2233 NIGTSIASVSW----------VVDPENhgRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpAWllegypghegrq 2302
Cdd:cd05906    346 DHSQALEFVSLgrpipgvsmrIVDDEG--QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED-GW------------ 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2303 grlYKTGDLVrYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHhmrkCLPEANQL------AVEVVPPSGERDHamLAAFI 2376
Cdd:cd05906    411 ---FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEA----AVEEVPGVepsftaAFAVRDPGAETEE--LAIFF 480
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 2377 rlddetrnSPliiKYAEDNSTAQIvfLTGIEEELSERL---PQHMVPTvffALVHFPTTTSGKTDRKRLREI 2445
Cdd:cd05906    481 --------VP---EYDLQDALSET--LRAIRSVVSREVgvsPAYLIPL---PKEEIPKTSLGKIQRSKLKAA 536
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
6277-6566 1.83e-24

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 110.96  E-value: 1.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6277 MYPCSPLQEGlMSLTAKRAGD---YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSElGLLQVVVE----EK 6349
Cdd:cd19066      1 KIPLSPMQRG-MWFLKKLATDpsaFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAG-RYEQVVLDktvrFR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6350 IQ-------WTESKRLEEYLREDKAVSMGL-GDPLARYAIIKeaWGGKRW-FVWTIHHALYDGWSLPRVLQAVKQAYNGA 6420
Cdd:cd19066     79 IEiidlrnlADPEARLLELIDQIQQTIYDLeRGPLVRVALFR--LADERDvLVVAIHHIIVDGGSFQILFEDISSVYDAA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6421 ------VLETQPSFNAFI----QYLSQQDLEATAAYWQTALADC--EATLF----PPLPSSVKQLVAD---TTVEHQCPL 6481
Cdd:cd19066    157 erqkptLPPPVGSYADYAawleKQLESEAAQADLAYWTSYLHGLppPLPLPkakrPSQVASYEVLTLEfflRSEETKRLR 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6482 PSRSTSDTTTSTLIRAAWAIVASRYTSSDDVVFGTTITGRNAPvtSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQ 6561
Cdd:cd19066    237 EVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQ 314

                   ....*
gi 1820002560 6562 ATEMI 6566
Cdd:cd19066    315 SREAI 319
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
1933-2443 1.96e-24

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 112.08  E-value: 1.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 2012
Cdd:cd05959      8 LVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2013 HPASRHEDIFRQTGAQVVVTSA------QHSARWIGTNHQVVTVSAGSLEQFSTLVNPVDLPA----------KPENAAY 2076
Cdd:cd05959     88 LTPDDYAYYLEDSRARVVVVSGelapvlAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAeaeqlkpaatHADDPAF 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2077 VMFTSGSTGTPKGVVLEHRAVVTSCLGHGQ----------AFGVTNLlralqFTAY------TFDVCiaeiittlVHGGC 2140
Cdd:cd05959    168 WLYSSGSTGRPKGVVHLHADIYWTAELYARnvlgireddvCFSAAKL-----FFAYglgnslTFPLS--------VGATT 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2141 ICVPSDSErRDNLAKAITDMQ--VNWGYLTSSVARLLDPCL----VPSLKVLVLGGEQVNSTDWGKWPS--SVQTINGYG 2212
Cdd:cd05959    235 VLMPERPT-PAAVFKRIRRYRptVFFGVPTLYAAMLAAPNLpsrdLSSLRLCVSAGEALPAEVGERWKArfGLDILDGIG 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2213 PTECC-VFCTGYTGiqgfqSGNIGTSIASVSW----VVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFidd 2287
Cdd:cd05959    314 STEMLhIFLSNRPG-----RVRYGTTGKPVPGyeveLRDED--GGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF--- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2288 pawllegypghegrQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKclpEANQLAVEVVPPSGER 2367
Cdd:cd05959    384 --------------QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQ---HPAVLEAAVVGVEDED 446
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 2368 DHAMLAAFIRLDDETrnspliikyaednsTAQIVFLTGIEEELSERLPQHMVP--TVFFAlvHFPTTTSGKTDRKRLR 2443
Cdd:cd05959    447 GLTKPKAFVVLRPGY--------------EDSEALEEELKEFVKDRLAPYKYPrwIVFVD--ELPKTATGKIQRFKLR 508
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
878-1362 2.22e-24

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 110.69  E-value: 2.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP--GHPASRHEeiFKQIGAQVVLT 955
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTafGPKAIEHR--LRTSGARLVVT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  956 SSqhamlfasSERHQVTvskvstsqlptvvnfakspvdpGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTD 1035
Cdd:cd05973     79 DA--------ANRHKLD----------------------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRP 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1036 HARVLQFAS--------YTFDACIAEIITTLLYGGCICVPSESDrrnnlakAISTMDVNCALLTPSVARLLEPSAVPSLK 1107
Cdd:cd05973    129 EDSFWNAADpgwayglyYAITGPLALGHPTILLEGGFSVESTWR-------VIERLGVTNLAGSPTAYRLLMAAGAEVPA 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1108 RLVLQGEQVSFA------DWNRWPGS---VQTINGYGPTECS-VCCNTYSGKQGFKSGIIGTSVASLSWVVDAGNHNRLA 1177
Cdd:cd05973    202 RPKGRLRRVSSAgepltpEVIRWFDAalgVPIHDHYGQTELGmVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELG 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1178 PlGSIGELLVE---GPILA-RGYLNDIDKTEAafiddpawllegyeghagrrGRLYKTGDLVRCDADGNLVCLGRKDSQV 1253
Cdd:cd05973    282 P-GEPGRLAIDianSPLMWfRGYQLPDTPAID--------------------GGYYLTGDTVEFDPDGSFSFIGRADDVI 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1254 KVRGQR-----VELGEIEHhvreclPEARQLAVeVILPSGQKEHaLLAAFIQLDKGnhnalFEEKASGEDSMAQVVfltg 1328
Cdd:cd05973    341 TMSGYRigpfdVESALIEH------PAVAEAAV-IGVPDPERTE-VVKAFVVLRGG-----HEGTPALADELQLHV---- 403
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 1329 veeelAKRLPEHMVPTILFTVKAMPITTSGKIDR 1362
Cdd:cd05973    404 -----KKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
4567-5057 2.31e-24

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 110.67  E-value: 2.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdhpasrhehiFRQTGAQVVLASA 4646
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPL------------FSAFGPEAIRDRL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4647 QyatlwtsLGRSVVIVSeasTSQLPVVTKTADPsvnpgnaAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITD-- 4724
Cdd:cd05969     69 E-------NSEAKVLIT---TEELYERTDPEDP-------TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPdd 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4725 ---HTRVLQFASYTFDACIAEIITtllccGCICVpSDSDR--RNNLAKAINAMDVNWALLTPSVARML----DPCVVQ-- 4793
Cdd:cd05969    132 iywCTADPGWVTGTVYGIWAPWLN-----GVTNV-VYEGRfdAESWYGIIERVKVTVWYTAPTAIRMLmkegDELARKyd 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4794 --SLKILVLGGEQVNSaDWDRWPKSIQTI---NAYGPTEC-SICCTTYSGkQGFKSGTIGTSIVSVSWVVDPENHNRLAP 4867
Cdd:cd05969    206 lsSLRFIHSVGEPLNP-EAIRWGMEVFGVpihDTWWQTETgSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPP 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4868 lGSIGELLVEG--PILARGYLNDMEKTEAAFIDdpawlleGYgghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLR 4945
Cdd:cd05969    284 -GTKGILALKPgwPSMFRGIWNDEERYKNSFID-------GW----------YLTGDLAYRDEDGYFWFVGRADDIIKTS 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4946 GQRVELGEVEhhvrECLTEAKQLA-VEVI-VPEGEGGYaMLAAFVQLGDDTyntlvkekAGGDSLTVQVVFLDRVEEElA 5023
Cdd:cd05969    346 GHRVGPFEVE----SALMEHPAVAeAGVIgKPDPLRGE-IIKAFISLKEGF--------EPSDELKEEIINFVRQKLG-A 411
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 5024 KRVPEHMMLttfftLEAMPTTTSGKIDRKRLREI 5057
Cdd:cd05969    412 HVAPREIEF-----VDNLPKTRSGKIMRRVLKAK 440
PRK06178 PRK06178
acyl-CoA synthetase; Validated
4525-5056 2.61e-24

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 112.06  E-value: 2.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4525 RQQLwAWNQDVP-----PAIERCVHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMV----P 4595
Cdd:PRK06178    13 LQQA-AWPAGIPrepeyPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVavflP 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4596 LC--FeksmwtVVAMLAVLKAGGAFVPLDPdhPASRHE--HIFRQTGAQVVLASAQYATLW------TSLgRSVVIVSEA 4665
Cdd:PRK06178    92 NCpqF------HIVFFGILKLGAVHVPVSP--LFREHElsYELNDAGAEVLLALDQLAPVVeqvraeTSL-RHVIVTSLA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4666 ----STSQLPVVTKTADPSVNPGNAAYAI------------------------FTSGSTGIPKGVVLEHKAVV-TSCLGH 4716
Cdd:PRK06178   163 dvlpAEPTLPLPDSLRAPRLAAAGAIDLLpalractapvplpppaldalaalnYTGGTTGMPKGCEHTQRDMVyTAAAAY 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4717 GQAFGITDHTRVLQF------ASYTFDaciaeIITTLLCCGCICVPSDSDRRNNLAkAINAMDVNWALLT-PSVARMLD- 4788
Cdd:PRK06178   243 AVAVVGGEDSVFLSFlpefwiAGENFG-----LLFPLFSGATLVLLARWDAVAFMA-AVERYRVTRTVMLvDNAVELMDh 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4789 PCVVQ----SLKilvlggeQVNSADW---------DRWPK---SIQTINAYGPTECSICCTTYSGKQG----FKSGTI-- 4846
Cdd:PRK06178   317 PRFAEydlsSLR-------QVRVVSFvkklnpdyrQRWRAltgSVLAEAAWGMTETHTCDTFTAGFQDddfdLLSQPVfv 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4847 -----GTSIVsvswVVDPENHnRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDdpAWLlegygghsgrqgrlyKTG 4921
Cdd:PRK06178   390 glpvpGTEFK----ICDFETG-ELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD--GWL---------------HTG 447
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4922 DLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE----HHvreclteAKQLAVEVIVPEGEGGYAMLAAFVQLGDDTynt 4997
Cdd:PRK06178   448 DIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEallgQH-------PAVLGSAVVGRPDPDKGQVPVAFVQLKPGA--- 517
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 4998 lvkekaggdsltvqvvflDRVEEELAKRVPEHMM---LTTFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:PRK06178   518 ------------------DLTAAALQAWCRENMAvykVPEIRIVDALPMTATGKVRKQDLQA 561
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
5648-6136 2.77e-24

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 110.30  E-value: 2.77e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSA 5727
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5728 QHSARwigtnhqvvtvsagslgqlstlvnpvglpaIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLS 5807
Cdd:cd05973     81 ANRHK------------------------------LDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5808 RVLQFAS--------YTFDACMDEIITTLMYGGCICVPSDSDRRNDLvkAISTMDVScalltPSVARLLEPSSVPTLQML 5879
Cdd:cd05973    131 SFWNAADpgwayglyYAITGPLALGHPTILLEGGFSVESTWRVIERL--GVTNLAGS-----PTAYRLLMAAGAEVPARP 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5880 VLQGEQVSFA------DWNRWPAS---VQTINGYGPTECS-ICCNTYSGKQGFKSGIIGTSVASVSWVVDPENHDRLAPl 5949
Cdd:cd05973    204 KGRLRRVSSAgepltpEVIRWFDAalgVPIHDHYGQTELGmVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGP- 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5950 GSIGELLVegpilargylnDIQKTaavfiddPAWLLEGY--PGHPGRQGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRG 6027
Cdd:cd05973    283 GEPGRLAI-----------DIANS-------PLMWFRGYqlPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSG 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6028 QRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHaMLAAFVQLEEGTqnalldkEASGEdsmaqvvflasVEEELA--- 6104
Cdd:cd05973    345 YRIGPFDVESALIE-HPAVAEAAV-IGVPDPERTE-VVKAFVVLRGGH-------EGTPA-----------LADELQlhv 403
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 6105 -KRLPEHMVP-TVFFsLLHFPTTTSGKTDRKRLR 6136
Cdd:cd05973    404 kKRLSAHAYPrTIHF-VDELPKTPSGKIQRFLLR 436
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
7621-8122 3.03e-24

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 111.25  E-value: 3.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7621 PGAPAICAWDG--ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEE 7698
Cdd:cd05926      1 PDAPALVVPGStpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7699 IFEQTGAQVVV------------ASAQYSAR----WTSSSCHVVTVSKALSSQLPA-VVDSTNTSVRPENAAYIIFTSGS 7761
Cdd:cd05926     81 YLADLGSKLVLtpkgelgpasraASKLGLAIlelaLDVGVLIRAPSAESLSNLLADkKNAKSEGVPLPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7762 TGVPKGVVLEHRAVATSCLGHGRAFGITNLSR---VLQFasYTFDACIAEIITTLLCGGCICVPSdsdrRNSLAKAISTM 7838
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRtlvVMPL--FHVHGLVASLLSTLAAGGSVVLPP----RFSASTFWPDV 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7839 ---DVNWAFLTPSVARLL------DPGlIPSLKILAIggeQSSSAdwnrwPGSVQKIH------------VYGPTECC-- 7895
Cdd:cd05926    235 rdyNATWYTAVPTIHQILlnrpepNPE-SPPPKLRFI---RSCSA-----SLPPAVLEaleatfgapvleAYGMTEAAhq 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7896 IFCTGYTTKQGfEPSTIGTSVASVSWVVDPenHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPaWLlegypg 7975
Cdd:cd05926    306 MTSNPLPPGPR-KPGSVGKPVGVEVRILDE--DGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG-WF------ 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7976 hpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClpEARQLAVEVILPsgqknHAML----A 8051
Cdd:cd05926    376 ---------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH--PAVLEAVAFGVP-----DEKYgeevA 439
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 8052 VFVQLGKGTHIahleekaggedsmaqvvfltgTEEEL----AKRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:cd05926    440 AAVVLREGASV---------------------TEEELrafcRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
4567-5056 3.13e-24

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 110.16  E-value: 3.13e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPdhpasrhehIFRQTGAQVVLASA 4646
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILP---------FFREHELAFILRRA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4647 QyatlwtslgrSVVIVseastsqLPVVTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHT 4726
Cdd:cd05903     73 K----------AKVFV-------VPERFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4727 RVLQFASYtfdACIAEIITTLLCCGCICVPSDSDRRNNLAKAINAMDVNWALL----TPSVARMLD-----PCVVQSLKI 4797
Cdd:cd05903    136 VFLVASPM---AHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFmmgaTPFLTDLLNaveeaGEPLSRLRT 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4798 LVLGGEQVnsadwdrwPKSI----------QTINAYGPTEC-SICCTTYSGKQGFKSGTIGTSIVSVSWVVDPENHNRLA 4866
Cdd:cd05903    213 FVCGGATV--------PRSLarraaellgaKVCSAYGSTECpGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLA 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4867 PlGSIGELLVEGPILARGYLNDMEKTEAAFIDdpAWllegygghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRG 4946
Cdd:cd05903    285 P-GVEGELLSRGPSVFLGYLDRPDLTADAAPE--GW---------------FRTGDLARLDEDGYLRITGRSKDIIIRGG 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4947 QRVELGEVEHHVrecLTEAKQLAVEVIVPEGEGGYAMLAAFVQLGDdtyntlvkekagGDSLTVQVV--FLDRVeeELAK 5024
Cdd:cd05903    347 ENIPVLEVEDLL---LGHPGVIEAAVVALPDERLGERACAVVVTKS------------GALLTFDELvaYLDRQ--GVAK 409
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1820002560 5025 -RVPEHMMLttfftLEAMPTTTSGKIDRKRLRE 5056
Cdd:cd05903    410 qYWPERLVH-----VDDLPRTPSGKVQKFRLRE 437
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
7617-8036 3.26e-24

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 111.56  E-value: 3.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPAICAWDGE------LTYGELDVLSSNLAGHLVQLGvNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 7690
Cdd:cd05931      3 AAARPDRPAYTFLDDEggreetLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7691 HPASRHEE---IFEQTGAQVVVASAQYSA---RWTSSSCHVVTVSKALSSQLPAVV--DSTNTSVRPENAAYIIFTSGST 7762
Cdd:cd05931     82 TPGRHAERlaaILADAGPRVVLTTAAALAavrAFAASRPAAGTPRLLVVDLLPDTSaaDWPPPSPDPDDIAYLQYTSGST 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7763 GVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFD-ACIAEIITTLLCGGCiCV---PSDSDRRNSL-AKAIST 7837
Cdd:cd05931    162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmGLIGGLLTPLYSGGP-SVlmsPAAFLRRPLRwLRLISR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7838 MDVNWAFlTPS------VARLLDPGLIP----SLKILAIGGEQSSSADWNRW---------------PGsvqkihvYGPT 7892
Cdd:cd05931    241 YRATISA-APNfaydlcVRRVRDEDLEGldlsSWRVALNGAEPVRPATLRRFaeafapfgfrpeafrPS-------YGLA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7893 ECCIFCTGYTTKQGF------------------EPSTIGTSVASVSWV--------VDPENHNRLAPlGSMGELLMEGPI 7946
Cdd:cd05931    313 EATLFVSGGPPGTGPvvlrvdrdalagravavaADDPAARELVSCGRPlpdqevriVDPETGRELPD-GEVGEIWVRGPS 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7947 LARGYLNDVDKTEAAF-----IDDPAWLlegypghpgrqgrlyKTGDLvQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 8021
Cdd:cd05931    392 VASGYWGRPEATAETFgalaaTDEGGWL---------------RTGDL-GFLHDGELYITGRLKDLIIVRGRNHYPQDIE 455
                          490
                   ....*....|....*
gi 1820002560 8022 HHVRECLPEARQLAV 8036
Cdd:cd05931    456 ATAEEAHPALRPGCV 470
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
854-1365 4.25e-24

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 110.92  E-value: 4.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 933
Cdd:cd05959      6 ATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 PGHPASRHEEIFKQIGAQVVLTSSQHAMLFAS----SERHQVTV-------SKVSTSQLPTVVNFAKSPVDPGNT----- 997
Cdd:cd05959     86 TLLTPDDYAYYLEDSRARVVVVSGELAPVLAAaltkSEHTLVVLivsggagPEAGALLLAELVAAEAEQLKPAAThaddp 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  998 AYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARV------LQFA-----SYTFDACIAEiiTTLLYGGCICV 1066
Cdd:cd05959    166 AFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVcfsaakLFFAyglgnSLTFPLSVGA--TTVLMPERPTP 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1067 PSESDR----RNNLAKAISTMdvNCALLTPSVARLLEPSavpSLKRLVLQGEQVSFADWNRWPG--SVQTINGYGPTECS 1140
Cdd:cd05959    244 AAVFKRirryRPTVFFGVPTL--YAAMLAAPNLPSRDLS---SLRLCVSAGEALPAEVGERWKArfGLDILDGIGSTEML 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1141 --VCCNTYSGKqgfKSGIIGTSVA--SLSWVVDAGNHnrlAPLGSIGELLVEGPILARGYLNDIDKTEAAFiddpawlle 1216
Cdd:cd05959    319 hiFLSNRPGRV---RYGTTGKPVPgyEVELRDEDGGD---VADGEPGELYVRGPSSATMYWNNRDKTRDTF--------- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1217 gyeghagrRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhhvrECL---PEARQLAVEVIlpsgQKEHA 1293
Cdd:cd05959    384 --------QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVE----SALvqhPAVLEAAVVGV----EDEDG 447
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 1294 LL--AAFIQLDKGnhnalfeEKASGEDSmaqvvflTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd05959    448 LTkpKAFVVLRPG-------YEDSEALE-------EELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
6841-7041 4.75e-24

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 110.76  E-value: 4.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6841 FVRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNdpawlVEGHgkhpgrrgRLYKTGDLVYYnKDGNLVYIG 6920
Cdd:PRK04813   330 LIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT-----FDGQ--------PAYHTGDAGYL-EDGLLFYQG 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6921 RKDGQVKVRGQRVELGEIENRLREcmpratqmaVEVISPAGAAEQAKtmvvaflqlnDEARDALLGGNVPNDDNLSAQVV 7000
Cdd:PRK04813   396 RIDFQIKLNGYRIELEEIEQNLRQ---------SSYVESAVVVPYNK----------DHKVQYLIAYVVPKEEDFEREFE 456
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 7001 FPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:PRK04813   457 LTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
1954-2442 6.41e-24

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 109.11  E-value: 6.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1954 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTS 2033
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2034 AQHsarwigtnhqvvtvsagsleqfstlvnpvdlpakpENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNL 2113
Cdd:cd05935     81 SEL-----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2114 LRALQFTAYTFDVCIAEIITTLVHGGCICVPSDSERRDNLAKAITDMQVN-WGYLTSSVARLL------DPCLvPSLKVL 2186
Cdd:cd05935    126 DVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTfWTNIPTMLVDLLatpefkTRDL-SSLKVL 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2187 VLGGEQVnstdwgkwPSSV----------QTINGYGPTECCVfCTGYTGIQGFQSGNIGTSIASV-SWVVDPENhGRLAP 2255
Cdd:cd05935    205 TGGGAPM--------PPAVaekllkltglRFVEGYGLTETMS-QTHTNPPLRPKLQCLGIP*FGVdARVIDIET-GRELP 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2256 LGSIGELLVEGPILARGYLNDVDKTQAAFIDDpawllegypghEGRqgRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQ 2335
Cdd:cd05935    275 PNEVGEIVVRGPQIFKGYWNRPEETEESFIEI-----------KGR--RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGF 341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2336 RVELGEVEHHMRKcLPEANQLAVEVVPP--SGERdhamLAAFIRLDDETRNspliiKYAEDNstaqivfltgIEEELSER 2413
Cdd:cd05935    342 KVWPAEVEAKLYK-HPAI*EVCVISVPDerVGEE----VKAFIVLRPEYRG-----KVTEED----------IIEWAREQ 401
                          490       500
                   ....*....|....*....|....*....
gi 1820002560 2414 LPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:cd05935    402 MAAYKYPREVEFVDELPRSASGKILWRLL 430
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
7182-7478 7.83e-24

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 108.68  E-value: 7.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7182 IYPCSPLQEGLI--SLTAKrAGD-YIMQSVLEL--RADVDEdvFCAAWEHVVQSTAALRTRIvqHSElGL---LQVV--- 7250
Cdd:cd19544      1 IYPLAPLQEGILfhHLLAE-EGDpYLLRSLLAFdsRARLDA--FLAALQQVIDRHDILRTAI--LWE-GLsepVQVVwrq 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7251 ----VEEkIQWTESEALEEYLKE---DKAVSMGLGD-PLAHYALVKEAWGGKRWFVWTIHHALYDGGSLPLILHAVKQVY 7322
Cdd:cd19544     75 aelpVEE-LTLDPGDDALAQLRArfdPRRYRLDLRQaPLLRAHVAEDPANGRWLLLLLFHHLISDHTSLELLLEEIQAIL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7323 SG--AVLERQPSFNAFI-QYLGQQDLEATAAYWQTALSDCEAvlfPPLP----------STVTQpvADTTVEyqcPPLSK 7389
Cdd:cd19544    154 AGraAALPPPVPYRNFVaQARLGASQAEHEAFFREMLGDVDE---PTAPfglldvqgdgSDITE--ARLALD---AELAQ 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7390 A------TLDTTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRNAPIAGVEAMVGPTIATVPVRLRVQrDQTVFAFLQGL 7463
Cdd:cd19544    226 RlraqarRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQT 304
                          330
                   ....*....|....*
gi 1820002560 7464 QQQSTDMIAHEQTGL 7478
Cdd:cd19544    305 HARLAELLRHEHASL 319
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
3023-3334 7.91e-24

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 109.04  E-value: 7.91e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3023 FPCTPMQEGILTSQ--GKDPDAYWVCFIYEVipnqETSISLARLQQAWKGVVHQHSLLRTLLVDNVPGSTgttNVVLKD- 3099
Cdd:cd19066      2 IPLSPMQRGMWFLKklATDPSAFNVAIEMFL----TGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYE---QVVLDKt 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3100 PQPSISVFSSEGTATIELFRSRYNPAAQRSIGQLQH----HLSICQLNNGKVYLCLDINHAIIDAHSRGILMHDLQEAYD 3175
Cdd:cd19066     75 VRFRIEIIDLRNLADPEARLLELIDQIQQTIYDLERgplvRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3176 ANLNPQST------SFRDFASYIKQQSQEEA----GRYWAEYLDGV-EPCFFPSLGDSGGANTI-PRTVE--VPSIDSSA 3241
Cdd:cd19066    155 AAERQKPTlpppvgSYADYAAWLEKQLESEAaqadLAYWTSYLHGLpPPLPLPKAKRPSQVASYeVLTLEffLRSEETKR 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3242 VHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRdlPIHNVNSIFGPLISILPCRIHLHKQLTVLEALKTVQ 3321
Cdd:cd19066    235 LREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR--PDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTK 312
                          330
                   ....*....|...
gi 1820002560 3322 ENYASSLSFQTFP 3334
Cdd:cd19066    313 EQSREAIEHQRVP 325
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
4545-5056 8.24e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 110.86  E-value: 8.24e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4545 DQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 4624
Cdd:PRK05605    36 DLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPL 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4625 HPASRHEHIFRQTGAQVVLASAQYATLWTSLGRSV---VIVSEASTSQLPVVTKTA------------------------ 4677
Cdd:PRK05605   116 YTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTpleTIVSVNMIAAMPLLQRLAlrlpipalrkaraaltgpapgtvp 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4678 -----------------DPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSC---------LGHGQ-----------AF 4720
Cdd:PRK05605   196 wetlvdaaiggdgsdvsHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAaqgkawvpgLGDGPervlaalpmfhAY 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4721 GITdhtRVLQFASY---------TFDacIAEIIT-------TLLccgcICVPSDSDRrnnLAKAINAMDVNWALLTPSV- 4783
Cdd:PRK05605   276 GLT---LCLTLAVSiggelvllpAPD--IDLILDamkkhppTWL----PGVPPLYEK---IAEAAEERGVDLSGVRNAFs 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4784 -ARMLDPCVVQslkilvlggeqvnsadwdRWPKsiQT----INAYGPTECS--ICCTTYSGKQgfKSGTIG-----TSIV 4851
Cdd:PRK05605   344 gAMALPVSTVE------------------LWEK--LTggllVEGYGLTETSpiIVGNPMSDDR--RPGYVGvpfpdTEVR 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4852 svswVVDPENHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpaWllegygghsgrqgrlYKTGDLVRYDADGN 4931
Cdd:PRK05605   402 ----IVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--W---------------FRTGDVVVMEEDGF 460
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4932 LVYLGRKDSQVKLRGQRVELGEVEHHVREcLTEAKQLAVeVIVPEGEGGYAMLAAFVqLGDDTynTLVKEKaggdsltvq 5011
Cdd:PRK05605   461 IRIVDRIKELIITGGFNVYPAEVEEVLRE-HPGVEDAAV-VGLPREDGSEEVVAAVV-LEPGA--ALDPEG--------- 526
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 5012 vvFLDRVEEELAK-RVPEhmmltTFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:PRK05605   527 --LRAYCREHLTRyKVPR-----RFYHVDELPRDQLGKVRRREVRE 565
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
7611-8122 1.20e-23

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 109.84  E-value: 1.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAICAWDG-ELTYGELDVLSSNLAGHLVQLGVNPEDVVplCFEKSMWT--VVAMLAVLKAGGAFVPL 7687
Cdd:PRK06087    27 DYWQQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRV--AFQLPGWCefTIIYLACLKVGAVSVPL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7688 DpdhPASRHEEI---FEQTGAQVVVASAQYSARWTSS---SC--------HVVTVSK---ALSSQLPAVVDSTNTS---- 7746
Cdd:PRK06087   105 L---PSWREAELvwvLNKCQAKMFFAPTLFKQTRPVDlilPLqnqlpqlqQIVGVDKlapATSSLSLSQIIADYEPltta 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7747 --VRPENAAYIIFTSGSTGVPKGVVLEHRAVATSclghGRAF-GITNLSRV--------LQFASYTFDAciaeIITTLLC 7815
Cdd:PRK06087   182 itTHGDELAAVLFTSGTEGLPKGVMLTHNNILAS----ERAYcARLNLTWQdvfmmpapLGHATGFLHG----VTAPFLI 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7816 GGCICVpsdSDRRNSlAKAISTMD---VNWAF-LTPSVARLL-----DPGLIPSLKILAIGGEQSSSADWNR-WPGSVQK 7885
Cdd:PRK06087   254 GARSVL---LDIFTP-DACLALLEqqrCTCMLgATPFIYDLLnllekQPADLSALRFFLCGGTTIPKKVAREcQQRGIKL 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7886 IHVYGPTECC--IF-----CTGYTTkqgfepSTIGTSVASVSW-VVDpENHNRLaPLGSMGELLMEGPILARGYLNDVDK 7957
Cdd:PRK06087   330 LSVYGSTESSphAVvnlddPLSRFM------HTDGYAAAGVEIkVVD-EARKTL-PPGCEGEEASRGPNVFMGYLDEPEL 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7958 TEAAfIDDPAWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKdSQVKVR-GQRVELGEVEHHVREClPEARQLAV 8036
Cdd:PRK06087   402 TARA-LDEEGW---------------YYSGDLCRMDEAGYIKITGRK-KDIIVRgGENISSREVEDILLQH-PKIHDACV 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8037 eVILPS---GQKNHAmlavFVQLGKGTHIAHLEEkaggedsmaQVVFLtgTEEELAKRL-PKHMVptvffALLHFPMTTS 8112
Cdd:PRK06087   464 -VAMPDerlGERSCA----YVVLKAPHHSLTLEE---------VVAFF--SRKRVAKYKyPEHIV-----VIDKLPRTAS 522
                          570
                   ....*....|
gi 1820002560 8113 GKADRKRLRE 8122
Cdd:PRK06087   523 GKIQKFLLRK 532
PRK07787 PRK07787
acyl-CoA synthetase; Validated
859-1365 1.20e-23

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 108.92  E-value: 1.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  859 AEQARARPDASAVCAWDGELTYGELDELSSKLAAhlvqlGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPA 938
Cdd:PRK07787     7 AAVAAAADIADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  939 SRHEEIFKQIGAQVVLTSSQHAMlfASSERHQVTVSKVSTSQLPtvvnfaksPVDPGNTAYIIFTSGTTGIPKGVVLQHR 1018
Cdd:PRK07787    82 AERRHILADSGAQAWLGPAPDDP--AGLPHVPVRLHARSWHRYP--------EPDPDAPALIVYTSGTTGPPKGVVLSRR 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1019 AVTTSCLGHGEAFGYTD-----HA---------------------RVLQFASYTFDACIAEIIT--TLLYGgcicVP--- 1067
Cdd:PRK07787   152 AIAADLDALAEAWQWTAddvlvHGlplfhvhglvlgvlgplrignRFVHTGRPTPEAYAQALSEggTLYFG----VPtvw 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1068 SESDRRNNLAKAISTmdvncalltpsvARLL----EPSAVPSLKRLV-LQGEQVsfadwnrwpgsvqtINGYGPTECSVC 1142
Cdd:PRK07787   228 SRIAADPEAARALRG------------ARLLvsgsAALPVPVFDRLAaLTGHRP--------------VERYGMTETLIT 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1143 CNTY-SGKQgfKSGIIGTSVASLSWVVDAGNHNRLAPLG-SIGELLVEGPILARGYLNDIDKTEAAFIDDpAWllegyeg 1220
Cdd:PRK07787   282 LSTRaDGER--RPGWVGLPLAGVETRLVDEDGGPVPHDGeTVGELQVRGPTLFDGYLNRPDATAAAFTAD-GW------- 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1221 hagrrgrlYKTGDLVRCDADGNLVCLGRKDSQ-VKVRGQRVELGEIE-----HhvreclPEARQLAVeVILPsgqkehal 1294
Cdd:PRK07787   352 --------FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIEtallgH------PGVREAAV-VGVP-------- 408
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 1295 laafiqldkgnHNALfeekasGEDSMAQVVFLTGV-EEEL----AKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:PRK07787   409 -----------DDDL------GQRIVAYVVGADDVaADELidfvAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
85-283 1.39e-23

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 109.53  E-value: 1.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   85 VVDPKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNpaWLLE-GHGGY-------------AGRQGRLYKTG 150
Cdd:cd17647    300 VVNRNDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNN--WFVEpDHWNYldkdnnepwrqfwLGPRDRLYRTG 377
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  151 DLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHH------VRECLPEAKQlavevvlplGQKNHATLAAFI--QLDKG 222
Cdd:cd17647    378 DLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHisqhplVRENITLVRR---------DKDEEPTLVSYIvpRFDKP 448
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560  223 THNALLKEKVGGDDSIARVV--------FLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd17647    449 DDESFAQEDVPKEVSTDPIVkgligyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
7611-8021 1.67e-23

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 109.21  E-value: 1.67e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAICAWDGE--LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 7688
Cdd:PRK05852    20 DLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLD 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7689 PDHPASRHEEIFEQTGAQVVVAS-------AQYSARWTSSSCHVVTVSKALSSQL---------PAVVDSTNTSVRPENa 7752
Cdd:PRK05852   100 PALPIAEQRVRSQAAGARVVLIDadgphdrAEPTTRWWPLTVNVGGDSGPSGGTLsvhldaatePTPATSTPEGLRPDD- 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7753 AYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNL-SRVLQFASYTFDACIAEIITTLLCGGCICVPSDSD-RRNS 7830
Cdd:PRK05852   179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRdATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRfSAHT 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7831 LAKAISTMDVNWAFLTPSVARLL--------DPGLIPSLKILaiggeQSSSADWNrwPGSVQKIH---------VYGPTE 7893
Cdd:PRK05852   259 FWDDIKAVGATWYTAVPTIHQILleraatepSGRKPAALRFI-----RSCSAPLT--AETAQALQtefaapvvcAFGMTE 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7894 CC-------IFCTGYTTKQGFEPSTIGTSVASVSWVVDPENHNrlAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdp 7966
Cdd:PRK05852   332 AThqvtttqIEGIGQTENPVVSTGLVGRSTGAQIRIVGSDGLP--LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD-- 407
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 7967 AWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 8021
Cdd:PRK05852   408 GWL---------------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVE 447
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
4567-5057 1.77e-23

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 109.29  E-value: 1.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL-------DPDHPASRHEHIFRQTGA 4639
Cdd:cd05906     40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptydEPNARLRKLRHIWQLLGS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4640 QVVLASAQYA-------TLWTSLGRSVVIVSEASTSQLPVVTKTADPsvnpGNAAYAIFTSGSTGIPKGVVLEHKAVVTS 4712
Cdd:cd05906    120 PVVLTDAELVaefagleTLSGLPGIRVLSIEELLDTAADHDLPQSRP----DDLALLMLTSGSTGFPKAVPLTHRNILAR 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4713 CLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGC--ICVPSDSDRRNNLaKAINAMD-----VNWA------LL 4779
Cdd:cd05906    196 SAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCqqVHVPTEEILADPL-RWLDLIDryrvtITWApnfafaLL 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4780 TPSVARMLDPCV-VQSLKILVLGGEQVNSADWDRWPKSIQT--------INAYGPTE-CSICctTYSgkQGFKSGTIGTS 4849
Cdd:cd05906    275 NDLLEEIEDGTWdLSSLRYLVNAGEAVVAKTIRRLLRLLEPyglppdaiRPAFGMTEtCSGV--IYS--RSFPTYDHSQA 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4850 IVSVSW----------VVDPEnhNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpAWllegygghsgrqgrlYK 4919
Cdd:cd05906    351 LEFVSLgrpipgvsmrIVDDE--GQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED-GW---------------FR 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4920 TGDLVrYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREclteakqlaveviVPEGEGGYAMLAAFVQLGDDTyntlv 4999
Cdd:cd05906    413 TGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEE-------------VPGVEPSFTAAFAVRDPGAET----- 473
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 5000 kekaggDSLTvqVVFLDRVEE-----ELAKRVPEHMMLTTFFTL--------EAMPTTTSGKIDRKRLREI 5057
Cdd:cd05906    474 ------EELA--IFFVPEYDLqdalsETLRAIRSVVSREVGVSPayliplpkEEIPKTSLGKIQRSKLKAA 536
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
7584-8122 2.24e-23

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 109.32  E-value: 2.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7584 DTTTPEDRQQLWAWNADVPPAIE---RCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVV 7660
Cdd:PRK05605     6 EMSAFADKPWLQSYAPWTPHDLDygdTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7661 PLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVV-----ASAQYSARWTSSSCHVVTVS------ 7729
Cdd:PRK05605    86 AIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIvwdkvAPTVERLRRTTPLETIVSVNmiaamp 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7730 ------------------KALSSQLPAVVD---------------STNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVA 7776
Cdd:PRK05605   166 llqrlalrlpipalrkarAALTGPAPGTVPwetlvdaaiggdgsdVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLF 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7777 TSCLgHGRA------------------FGITNLSRVLQFASY---------TFDacIAEIIT-------TLLCGgcicVP 7822
Cdd:PRK05605   246 ANAA-QGKAwvpglgdgpervlaalpmFHAYGLTLCLTLAVSiggelvllpAPD--IDLILDamkkhppTWLPG----VP 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7823 SDSDRRNSLAKA--ISTMDVNWAFltpSVARLLDPglipslkilaiggeqSSSADWNRWPGSVQkIHVYGPTECCIFCTG 7900
Cdd:PRK05605   319 PLYEKIAEAAEErgVDLSGVRNAF---SGAMALPV---------------STVELWEKLTGGLL-VEGYGLTETSPIIVG 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7901 YTTKQGFEPSTIG-----TSVAsvswVVDPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWllegypg 7975
Cdd:PRK05605   380 NPMSDDRRPGYVGvpfpdTEVR----IVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--W------- 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7976 hpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSgqknhamlavfvq 8055
Cdd:PRK05605   447 --------FRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLRE-HPGVEDAAV-VGLPR------------- 503
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 8056 lgkgthiahleeKAGGEDSMAQVVFLTGT---EEELA----KRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:PRK05605   504 ------------EDGSEEVVAAVVLEPGAaldPEGLRaycrEHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
878-1368 2.51e-23

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 108.91  E-value: 2.51e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGH------PASRH-EEIFKQIGA 950
Cdd:cd05906     40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPtydepnARLRKlRHIWQLLGS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  951 QVVLTSSQHAMLFA------SSERHQVTVSKVSTSQLPTVVNFAKSPVDPgntAYIIFTSGTTGIPKGVVLQHRAVTTSC 1024
Cdd:cd05906    120 PVVLTDAELVAEFAgletlsGLPGIRVLSIEELLDTAADHDLPQSRPDDL---ALLMLTSGSTGFPKAVPLTHRNILARS 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1025 LGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGC--ICVPSESDRRN--NLAKAISTMDVN--------CALLTP 1092
Cdd:cd05906    197 AGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCqqVHVPTEEILADplRWLDLIDRYRVTitwapnfaFALLND 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1093 SVARLLEPSA-VPSLKRLVLQGEQVSFADWNRW-----PGSVQT---INGYGPTE-CSVCcnTYSgkQGFKSG------- 1155
Cdd:cd05906    277 LLEEIEDGTWdLSSLRYLVNAGEAVVAKTIRRLlrllePYGLPPdaiRPAFGMTEtCSGV--IYS--RSFPTYdhsqale 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1156 -------IIGTSVAslswVVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpAWllegyeghagrrgrl 1228
Cdd:cd05906    353 fvslgrpIPGVSMR----IVDD--EGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED-GW--------------- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1229 YKTGDLVRCDaDGNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQ---LAVEVILPSGQKEHalLAAFIQLDKGN 1305
Cdd:cd05906    411 FRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEE-VPGVEPsftAAFAVRDPGAETEE--LAIFFVPEYDL 486
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 1306 HNALFEekaSGEDSMAQVVFLTGVEeelakrlPEHMVPTilfTVKAMPITTSGKIDRKRLQDI 1368
Cdd:cd05906    487 QDALSE---TLRAIRSVVSREVGVS-------PAYLIPL---PKEEIPKTSLGKIQRSKLKAA 536
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
3469-3976 2.77e-23

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 108.45  E-value: 2.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3469 EQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 3548
Cdd:PRK07656    13 RAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3549 RHEEIFEQTGAQVVVASAQYsarwtssschvVTVSKALSSQLPA----VVDSTNT------------------------- 3599
Cdd:PRK07656    93 EAAYILARGDAKALFVLGLF-----------LGVDYSATTRLPAlehvVICETEEddphtekmktftdflaagdpaerap 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3600 SVRPENAAYIIFTSGSTGVPKGVVLEHRavatSCLGHGRAF----GITNLSRVLQ----FASYTFDACiaeIITTLLCGG 3671
Cdd:PRK07656   162 EVDPDDVADILFTSGTTGRPKGAMLTHR----QLLSNAADWaeylGLTEGDRYLAanpfFHVFGYKAG---VNAPLMRGA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3672 CICV-----PSD-----SDRRNSLAKAISTMdvnWAFLtpsvarLLDPGLIP----SLKILAIGGeqSSSAdwnrwPGSV 3737
Cdd:PRK07656   235 TILPlpvfdPDEvfrliETERITVLPGPPTM---YNSL------LQHPDRSAedlsSLRLAVTGA--ASMP-----VALL 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3738 QKIH----------VYGPTECCifctGYTTKQGFE------PSTIGTSVASVSWVVDPENHNRLaPLGSMGELLMEGPIL 3801
Cdd:PRK07656   299 ERFEselgvdivltGYGLSEAS----GVTTFNRLDddrktvAGTIGTAIAGVENKIVNELGEEV-PVGEVGELLVRGPNV 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3802 ARGYLNDVDKTEAAfIDDPAWLlegypgHpgrqgrlykTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvrEC 3881
Cdd:PRK07656   374 MKGYYDDPEATAAA-IDADGWL------H---------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVE----EV 433
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3882 LPEARQLA-VEVIlpsGQKDHAM---LAAFVQLEEGTQnalLDKEAggedsmaqvvFLASVEEELAKrlpeHMVPTVFFS 3957
Cdd:PRK07656   434 LYEHPAVAeAAVI---GVPDERLgevGKAYVVLKPGAE---LTEEE----------LIAYCREHLAK----YKVPRSIEF 493
                          570
                   ....*....|....*....
gi 1820002560 3958 LLHFPTTTSGKTDRKRLRE 3976
Cdd:PRK07656   494 LDELPKNATGKVLKRALRE 512
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
4555-5056 2.99e-23

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 108.17  E-value: 2.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4555 PDTPAICAWDG--ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEH 4632
Cdd:cd05926      1 PDAPALVVPGStpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4633 IFRQTGAQVVL------ASAQYATLWTSL---------GRSVVIVSEASTSQLPVVTKTADPSVNPGNAAYA--IFTSGS 4695
Cdd:cd05926     81 YLADLGSKLVLtpkgelGPASRAASKLGLailelaldvGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLAliLHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4696 TGIPKGVVLEHKAVVTSCLGHGQAFGITDHTR---VLQFasYTFDACIAEIITTLLCCGCICVP---SDSDRRNNLAKAi 4769
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRtlvVMPL--FHVHGLVASLLSTLAAGGSVVLPprfSASTFWPDVRDY- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4770 namDVNW---------ALLTPSVARM----------------LDPCVVQSLkilvlggEQVNSAdwdrwpksiQTINAYG 4824
Cdd:cd05926    238 ---NATWytavptihqILLNRPEPNPespppklrfirscsasLPPAVLEAL-------EATFGA---------PVLEAYG 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4825 PTECSICCTTY---SGKQgfKSGTIGTSIVSVSWVVDPenHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPa 4901
Cdd:cd05926    299 MTEAAHQMTSNplpPGPR--KPGSVGKPVGVEVRILDE--DGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG- 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4902 WLlegygghsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVRECltEAKQLAVEVIVPE---GE 4978
Cdd:cd05926    374 WF---------------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH--PAVLEAVAFGVPDekyGE 436
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 4979 ggyaMLAAFVQLGDDTYNTlvkEKAggdsltvqvvFLDRVEEELAK-RVPehmmlTTFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:cd05926    437 ----EVAAAVVLREGASVT---EEE----------LRAFCRKHLAAfKVP-----KKVYFVDELPKTATGKIQRRKVAE 493
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
5625-6138 3.96e-23

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 110.40  E-value: 3.96e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5625 HDLFTEQAKARPHAPAICawD---GELTYGELDALSSKLAGHLTQLgVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVP 5701
Cdd:PRK08633   618 AEAWIDTAKRNWSRLAVA--DstgGELSYGKALTGALALARLLKRE-LKDEENVGILLPPSVAGALANLALLLAGKVPVN 694
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5702 LDpdHPASrhEDTFRHTGAQ----VVVTSAQH-------------------------SARwIGTNHQVVTVSAGSLGQLS 5752
Cdd:PRK08633   695 LN--YTAS--EAALKSAIEQaqikTVITSRKFleklknkgfdlelpenvkviyledlKAK-ISKVDKLTALLAARLLPAR 769
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5753 TLVNPVGLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTScwgrgrafgITNLSRVLQFASytfdacmDEII------- 5825
Cdd:PRK08633   770 LLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN---------IEQISDVFNLRN-------DDVIlsslpff 833
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5826 -------TTLM---YG-GCICVPSDSDRRNdLVKAISTMDVSCALLTPSVARL------LEPSSVPTLQMLVLQGEQV-- 5886
Cdd:PRK08633   834 hsfgltvTLWLpllEGiKVVYHPDPTDALG-IAKLVAKHRATILLGTPTFLRLylrnkkLHPLMFASLRLVVAGAEKLkp 912
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5887 SFADWNRWPASVQTINGYGPTECS--ICCNT-------YSGKQGFKSGIIGTSVASVSW-VVDPENHDRLAPlGSIGELL 5956
Cdd:PRK08633   913 EVADAFEEKFGIRILEGYGATETSpvASVNLpdvlaadFKRQTGSKEGSVGMPLPGVAVrIVDPETFEELPP-GEDGLIL 991
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5957 VEGPILARGYLNDIQKTAAVF--IDDPAWllegypghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGE 6034
Cdd:PRK08633   992 IGGPQVMKGYLGDPEKTAEVIkdIDGIGW---------------YVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGA 1056
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6035 VEHHVRECLPEARQLAVEVILPSGQKdhamlaafvqleeGTQNALLDKEASGEdsmaqvvfLASVEEELAK-RLPEHMVP 6113
Cdd:PRK08633  1057 VEEELAKALGGEEVVFAVTAVPDEKK-------------GEKLVVLHTCGAED--------VEELKRAIKEsGLPNLWKP 1115
                          570       580
                   ....*....|....*....|....*
gi 1820002560 6114 TVFFSLLHFPTTTSGKTDRKRLREI 6138
Cdd:PRK08633  1116 SRYFKVEALPLLGSGKLDLKGLKEL 1140
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5645-6136 4.62e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 106.61  E-value: 4.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5645 DGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVV 5724
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5725 TSAqhsarwigtnhqvvtvsagslgqlstlvnpvglpaipenaVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGIT 5804
Cdd:cd05934     81 VDP----------------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5805 NLSRVLQF--ASYTfDACMDEIITTLMYGG-CICVPSDSDRRndLVKAISTMDVSCALLTPSVARLL---EPSSVPTLQM 5878
Cdd:cd05934    121 EDDVYLTVlpLFHI-NAQAVSVLAALSVGAtLVLLPRFSASR--FWSDVRRYGATVTNYLGAMLSYLlaqPPSPDDRAHR 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5879 L-VLQGEQVSFADWNRWPA--SVQTINGYGPTECSICcntysgkqgfksgIIGTSVASVSW-------------VVDPEN 5942
Cdd:cd05934    198 LrAAYGAPNPPELHEEFEErfGVRLLEGYGMTETIVG-------------VIGPRDEPRRPgsigrpapgyevrIVDDDG 264
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5943 HDrlAPLGSIGELLV---EGPILARGYLNDIQKTAAVFiddpawllegypghpgRQGrLYKTGDLVRYDANGNLVCLGRK 6019
Cdd:cd05934    265 QE--LPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM----------------RNG-WFHTGDLGYRDADGFFYFVDRK 325
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6020 DSQVKLRGQRVELGEVE-----HhvreclPEARQLAVeVILPSGQKDHAmLAAFVQLEEGtqnALLDKEAsgedsmaqvv 6094
Cdd:cd05934    326 KDMIRRRGENISSAEVErailrH------PAVREAAV-VAVPDEVGEDE-VKAVVVLRPG---ETLDPEE---------- 384
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 6095 flasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:cd05934    385 ----LFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
5647-6136 4.71e-23

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 106.75  E-value: 4.71e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5647 ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTS 5726
Cdd:cd05971      6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5727 AqhsarwigtnhqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFgitNL 5806
Cdd:cd05971     86 G------------------------------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPF---NL 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5807 SRVLQFASYT------FDACMDEIITTLMYG----GCICVPSDSDRRNDLVkaiSTMDVSCALLTPSVARLL----EPSS 5872
Cdd:cd05971    127 FPRDGDLYWTpadwawIGGLLDVLLPSLYFGvpvlAHRMTKFDPKAALDLM---SRYGVTTAFLPPTALKMMrqqgEQLK 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5873 VPTLQMLVLQ--GEQV--SFADWNRWPASVQTINGYGPTECSICCNTYSGKQGFKSGIIGTSV-ASVSWVVDpENHDRLA 5947
Cdd:cd05971    204 HAQVKLRAIAtgGESLgeELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIpGHRVAIVD-DNGTPLP 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5948 PlGSIGELLVE--GPILARGYLNDIQKTAAVFIDDpaWLLegypghpgrqgrlykTGDLVRYDANGNLVCLGRKDSQVKL 6025
Cdd:cd05971    283 P-GEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD--WLL---------------TGDLGRKDSDGYFWYVGRDDDVITS 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6026 RGQRVELGEVEhhvrECL---PEARQLAVeVILP---SGQkdhaMLAAFVQLEEGTqnalldkeaSGEDSMAqvvflASV 6099
Cdd:cd05971    345 SGYRIGPAEIE----ECLlkhPAVLMAAV-VGIPdpiRGE----IVKAFVVLNPGE---------TPSDALA-----REI 401
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1820002560 6100 EEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:cd05971    402 QELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
4566-4955 4.75e-23

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 106.41  E-value: 4.75e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4566 ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLAS 4645
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4646 AQYATLwtslgrsvvivseastsqlpvvtktadpsvnpgnaAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDH 4725
Cdd:cd05935     81 SELDDL-----------------------------------ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4726 TRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLAKAINAMDVN--WALLTPSVARMLDPCV----VQSLKILV 4799
Cdd:cd05935    126 DVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTfwTNIPTMLVDLLATPEFktrdLSSLKVLT 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4800 LGGEQVNSADWDRWPK--SIQTINAYGPTEcSICCTTYSGKQGFKSGTIGTSIVSV-SWVVDPENHNRLAPlGSIGELLV 4876
Cdd:cd05935    206 GGGAPMPPAVAEKLLKltGLRFVEGYGLTE-TMSQTHTNPPLRPKLQCLGIP*FGVdARVIDIETGRELPP-NEVGEIVV 283
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 4877 EGPILARGYLNDMEKTEAAFIDDpawllegygghSGRqgRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE 4955
Cdd:cd05935    284 RGPQIFKGYWNRPEETEESFIEI-----------KGR--RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE 349
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
3601-3975 4.96e-23

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 107.42  E-value: 4.96e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3601 VRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQ----FASYTFDACiaeIITTLLCGGCI-CV 3675
Cdd:cd05909    144 VQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGC---LWLPLLSGIKVvFH 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3676 PSDSDRRnSLAKAISTMDVNWAFLTPS----VARLLDPGLIPSLKILAIGGEQSSSADWNRWpgsVQKIHV-----YGPT 3746
Cdd:cd05909    221 PNPLDYK-KIPELIYDKKATILLGTPTflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEF---QEKFGIrilegYGTT 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3747 ECCIFCTGYTTKQGFEPSTIGTSVASVSW-VVDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdpAWlle 3825
Cdd:cd05909    297 ECSPVISVNTPQSPNKEGTVGRPLPGMEVkIVSVETHEEV-PIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD--GW--- 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3826 gypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVRECLPEARQLAVeVILPSGQKDHAmLA 3905
Cdd:cd05909    371 ------------YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAV-VSVPDGRKGEK-IV 436
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 3906 AFVQLEEGTQNALLD--KEAGgedsmaqvvflasveeelakrLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd05909    437 LLTTTTDTDPSSLNDilKNAG---------------------ISNLAKPSYIHQVEEIPLLGTGKPDYVTLK 487
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
7611-8122 4.96e-23

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 107.68  E-value: 4.96e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 7690
Cdd:PRK07656     9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7691 HPASRHEEIFEQTGAQVVVASAQYsarwtssschvVTVSKALSSQLPA----VVDSTNT--------------------- 7745
Cdd:PRK07656    89 YTADEAAYILARGDAKALFVLGLF-----------LGVDYSATTRLPAlehvVICETEEddphtekmktftdflaagdpa 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7746 ----SVRPENAAYIIFTSGSTGVPKGVVLEHRavatSCLGHGRAF----GITNLSRVLQ----FASYTFDACiaeIITTL 7813
Cdd:PRK07656   158 erapEVDPDDVADILFTSGTTGRPKGAMLTHR----QLLSNAADWaeylGLTEGDRYLAanpfFHVFGYKAG---VNAPL 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7814 LCGGCICV-----PSD-----SDRRNSLAKAISTMdvnWAFLtpsvarLLDPGLIP----SLKILAIGGeqSSSAdwnrw 7879
Cdd:PRK07656   231 MRGATILPlpvfdPDEvfrliETERITVLPGPPTM---YNSL------LQHPDRSAedlsSLRLAVTGA--ASMP----- 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7880 PGSVQKIH----------VYGPTECCifctGYTTKQGFE------PSTIGTSVASVSWVVDPENHNRLaPLGSMGELLME 7943
Cdd:PRK07656   295 VALLERFEselgvdivltGYGLSEAS----GVTTFNRLDddrktvAGTIGTAIAGVENKIVNELGEEV-PVGEVGELLVR 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7944 GPILARGYLNDVDKTEAAfIDDPAWLlegypgHpgrqgrlykTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhh 8023
Cdd:PRK07656   370 GPNVMKGYYDDPEATAAA-IDADGWL------H---------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVE-- 431
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8024 vrECL---PEARQLAVeVILP---SGQKNHAmlavFVQLGKGTHIahleekaggedsmaqvvfltgTEEEL----AKRLP 8093
Cdd:PRK07656   432 --EVLyehPAVAEAAV-IGVPderLGEVGKA----YVVLKPGAEL---------------------TEEELiaycREHLA 483
                          570       580
                   ....*....|....*....|....*....
gi 1820002560 8094 KHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:PRK07656   484 KYKVPRSIEFLDELPKNATGKVLKRALRE 512
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
4567-5055 6.19e-23

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 106.27  E-value: 6.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdhpasrhehiFRQTGAQVVLASA 4646
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPL------------TTLLGPKDIEYRL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4647 QYAtlwtslgRSVVIVSEAStsqlpvvtktaDPSVNpgnaayaIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHT 4726
Cdd:cd05972     69 EAA-------GAKAIVTDAE-----------DPALI-------YFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4727 RVL--------QFASYTFDACIAEIITTLLCCGCICVPSdsdrrnNLAKAINAMDVNWALLTPSVARML---DPC--VVQ 4793
Cdd:cd05972    124 IHWniadpgwaKGAWSSFFGPWLLGATVFVYEGPRFDAE------RILELLERYGVTSFCGPPTAYRMLikqDLSsyKFS 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4794 SLKILVLGGEQVNSADWDRWPKS--IQTINAYGPTECSICCTTYSGkQGFKSGTIGTSIVSVSWVVDPENHNRLAPlGSI 4871
Cdd:cd05972    198 HLRLVVSAGEPLNPEVIEWWRAAtgLPIRDGYGQTETGLTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPP-GEE 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4872 GELLVE-GPI-LARGYLNDMEKTEAAFIDDpaWllegygghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRV 4949
Cdd:cd05972    276 GDIAIKlPPPgLFLGYVGDPEKTEASIRGD--Y---------------YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRI 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4950 ELGEVE----HH--VREClteakqlAVeVIVPEGEGGyAMLAAFVQLGDDTYNT--LVKEkaggdsltvqvvFLDRVEEE 5021
Cdd:cd05972    339 GPFEVEsallEHpaVAEA-------AV-VGSPDPVRG-EVVKAFVVLTSGYEPSeeLAEE------------LQGHVKKV 397
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 5022 LAK----RVPEhmmlttfFTLEaMPTTTSGKIDRKRLR 5055
Cdd:cd05972    398 LAPykypREIE-------FVEE-LPKTISGKIRRVELR 427
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1933-2444 7.01e-23

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 107.53  E-value: 7.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDG-ELTYGELDALSSKLASHLVQLGVNPEDVVplCFEKSMWT--VVAMLAVLKAGGAFVPL 2009
Cdd:PRK06087    27 DYWQQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRV--AFQLPGWCefTIIYLACLKVGAVSVPL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2010 DPdhpASRHEDI-----------------FRQTGAQVVVTSAQHSARWIGtnhQVVTV-------SAGSLEQ----FSTL 2061
Cdd:PRK06087   105 LP---SWREAELvwvlnkcqakmffaptlFKQTRPVDLILPLQNQLPQLQ---QIVGVdklapatSSLSLSQiiadYEPL 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2062 VNPVdlPAKPENAAYVMFTSGSTGTPKGVVLEH-------RAVVT-------------SCLGHGQAF--GVTN--LL--R 2115
Cdd:PRK06087   179 TTAI--TTHGDELAAVLFTSGTEGLPKGVMLTHnnilaseRAYCArlnltwqdvfmmpAPLGHATGFlhGVTApfLIgaR 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2116 ALQFTAYTFDVCiaeiITTLVHGGCICVPSDSERRDNLAKAITDmqvnwgyltssvarllDPCLVPSLKVLVLGGEQVNS 2195
Cdd:PRK06087   257 SVLLDIFTPDAC----LALLEQQRCTCMLGATPFIYDLLNLLEK----------------QPADLSALRFFLCGGTTIPK 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2196 TDWGK-WPSSVQTINGYGPTECC--VF-----CTGYTGiqgfqsGNIGTSIASVSW-VVDpENHGRLaPLGSIGELLVEG 2266
Cdd:PRK06087   317 KVAREcQQRGIKLLSVYGSTESSphAVvnlddPLSRFM------HTDGYAAAGVEIkVVD-EARKTL-PPGCEGEEASRG 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2267 PILARGYLNDVDKTQAAfIDDPAWllegypghegrqgrlYKTGDLVRYSSDGNLVCLGRKdSQVKVR-GQRVELGEVEHH 2345
Cdd:PRK06087   389 PNVFMGYLDEPELTARA-LDEEGW---------------YYSGDLCRMDEAGYIKITGRK-KDIIVRgGENISSREVEDI 451
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2346 MRKClPEANQLAVEVVPPS--GERdhamLAAFIRLDDETRNSPLiikyaEDnstaQIVFLTgiEEELSERL-PQHMVptv 2422
Cdd:PRK06087   452 LLQH-PKIHDACVVAMPDErlGER----SCAYVVLKAPHHSLTL-----EE----VVAFFS--RKRVAKYKyPEHIV--- 512
                          570       580
                   ....*....|....*....|..
gi 1820002560 2423 ffALVHFPTTTSGKTDRKRLRE 2444
Cdd:PRK06087   513 --VIDKLPRTASGKIQKFLLRK 532
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
1506-1804 7.30e-23

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 105.60  E-value: 7.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1506 IYPCSPLQEG-----LMSltakRAGD-YIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIvqHSElGL---LQVV-- 1574
Cdd:cd19544      1 IYPLAPLQEGilfhhLLA----EEGDpYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAI--LWE-GLsepVQVVwr 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1575 -----IEEnIQWTEPKSLEEYLSE-----------DKAvsvglgdPLARyAFVKEACGGKRWFV-WTIHHAVYDGWSLPL 1637
Cdd:cd19544     74 qaelpVEE-LTLDPGDDALAQLRArfdprryrldlRQA-------PLLR-AHVAEDPANGRWLLlLLFHHLISDHTSLEL 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1638 ILHAVKQVYSGGVLQWQPS--FNAFI-QYLGQQDLEATVAYWQTALADCEAvlfPTLPPTVT------QPVADATVeyqc 1708
Cdd:cd19544    145 LLEEIQAILAGRAAALPPPvpYRNFVaQARLGASQAEHEAFFREMLGDVDE---PTAPFGLLdvqgdgSDITEARL---- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1709 pPLSKATSD----------TTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNTPVTGVEAMVGPTIATVPVRLRVQrDQ 1778
Cdd:cd19544    218 -ALDAELAQrlraqarrlgVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GR 295
                          330       340
                   ....*....|....*....|....*....
gi 1820002560 1779 TVFAFLQGLQQQATDMIAHEQTGL---QR 1804
Cdd:cd19544    296 SVREAVRQTHARLAELLRHEHASLalaQR 324
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
3465-3976 8.02e-23

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 107.28  E-value: 8.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAICAWDGE--LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 3542
Cdd:PRK05852    20 DLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLD 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3543 PDHPASRHEEIFEQTGAQVVVAS-------AQYSARWTSSSCHVVTVSKALSSQL---------PAVVDSTNTSVRPENa 3606
Cdd:PRK05852   100 PALPIAEQRVRSQAAGARVVLIDadgphdrAEPTTRWWPLTVNVGGDSGPSGGTLsvhldaatePTPATSTPEGLRPDD- 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3607 AYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNL-SRVLQFASYTFDACIAEIITTLLCGGCICVPSDSD-RRNS 3684
Cdd:PRK05852   179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRdATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRfSAHT 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3685 LAKAISTMDVNWAFLTPSVARLL--------DPGLIPSLKILaiggeQSSSADWNrwPGSVQKIH---------VYGPTE 3747
Cdd:PRK05852   259 FWDDIKAVGATWYTAVPTIHQILleraatepSGRKPAALRFI-----RSCSAPLT--AETAQALQtefaapvvcAFGMTE 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3748 CC-------IFCTGYTTKQGFEPSTIGTSVASVSWVVDPENHNrlAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdp 3820
Cdd:PRK05852   332 AThqvtttqIEGIGQTENPVVSTGLVGRSTGAQIRIVGSDGLP--LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD-- 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3821 AWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVElgevehhvreclPEarqlAVEVILPSgqKD 3900
Cdd:PRK05852   408 GWL---------------RTGDLGSLSAAGDLSIRGRIKELINRGGEKIS------------PE----RVEGVLAS--HP 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3901 HAMLAAFVqleeGTQNALLdkeagGEDSMAQVVFLASVE---EELA----KRLPEHMVPTVFFSLLHFPTTTSGKTDRKR 3973
Cdd:PRK05852   455 NVMEAAVF----GVPDQLY-----GEAVAAVIVPRESAPptaEELVqfcrERLAAFEIPASFQEASGLPHTAKGSLDRRA 525

                   ...
gi 1820002560 3974 LRE 3976
Cdd:PRK05852   526 VAE 528
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
3486-3875 8.76e-23

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 105.64  E-value: 8.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3486 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVAS 3565
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3566 AQYsarwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNL 3645
Cdd:cd05935     81 SEL-----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3646 SRVLQFASYTFDA-CIAEIITTLLCGGCICVPSDSDrRNSLAKAISTMDVN-WAFLTPSVARLL-DPGL----IPSLKIL 3718
Cdd:cd05935    126 DVILACLPLFHVTgFVGSLNTAVYVGGTYVLMARWD-RETALELIEKYKVTfWTNIPTMLVDLLaTPEFktrdLSSLKVL 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3719 AIGGEQSSSADWNRWPGSVQKIHV--YGPTECCIfCTGYTTKQGFEPSTIGTSVASV-SWVVDPENHNRLAPlGSMGELL 3795
Cdd:cd05935    205 TGGGAPMPPAVAEKLLKLTGLRFVegYGLTETMS-QTHTNPPLRPKLQCLGIP*FGVdARVIDIETGRELPP-NEVGEIV 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3796 MEGPILARGYLNDVDKTEAAFIDDpawllegypghPGRqgRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 3875
Cdd:cd05935    283 VRGPQIFKGYWNRPEETEESFIEI-----------KGR--RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE 349
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3484-3975 1.22e-22

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 105.07  E-value: 1.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3484 DGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVV 3563
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3564 ASAqysarwtssschvvtvskalssqlpavvdstntsvrpenaAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGIT 3643
Cdd:cd05934     81 VDP----------------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3644 NLSRVLQF--ASYTfDACIAEIITTLLCGG-CICVPSDSDRR--NSLAKAISTmdvnWAFLTPSVARLL-------DPGL 3711
Cdd:cd05934    121 EDDVYLTVlpLFHI-NAQAVSVLAALSVGAtLVLLPRFSASRfwSDVRRYGAT----VTNYLGAMLSYLlaqppspDDRA 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3712 IPSLKILAIGGEQSSSADW-NRWpgSVQKIHVYGPTECcIFCTGYTTKQGFEPSTIGTSVASVSW-VVDPenHNRLAPLG 3789
Cdd:cd05934    196 HRLRAAYGAPNPPELHEEFeERF--GVRLLEGYGMTET-IVGVIGPRDEPRRPGSIGRPAPGYEVrIVDD--DGQELPAG 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3790 SMGELLM---EGPILARGYLNDVDKTEAAFiddpawllegypghpgRQGrLYKTGDLVQYNADGNLVYLGRKDSQVKVRG 3866
Cdd:cd05934    271 EPGELVIrglRGWGFFKGYYNMPEATAEAM----------------RNG-WFHTGDLGYRDADGFFYFVDRKKDMIRRRG 333
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3867 QRVELGEVE-----HhvreclPEARQLAVeVILPSGQKDHAmLAAFVQLEEGtqnALLDKEAggedsmaqvvflasVEEE 3941
Cdd:cd05934    334 ENISSAEVErailrH------PAVREAAV-VAVPDEVGEDE-VKAVVVLRPG---ETLDPEE--------------LFAF 388
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 3942 LAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd05934    389 CEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK06164 PRK06164
acyl-CoA synthetase; Validated
3465-3987 1.28e-22

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 106.75  E-value: 1.28e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmWtVVAMLAVLKAGGAFVP 3540
Cdd:PRK06164    14 SLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVavwlPNCIE---W-VVLFLACARLGATVIA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3541 LDPDHPASRHEEIFEQTGAQVVV--------------ASAQYSARWTSSSCHVVTVS-------------KALSSQLPAV 3593
Cdd:PRK06164    90 VNTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailAAVPPDALPPLRAIAVVDDAadatpapapgarvQLFALPDPAP 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3594 VDSTNTSVRPENAAYIIFT-SGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGG- 3671
Cdd:PRK06164   170 PAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAp 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3672 CICVPS-DSDRRnslAKAISTMDVNWAFLTPSV-ARLLD----PGLIPSLKILAIGGEQSSSAD---WNRWPGSVQKiHV 3742
Cdd:PRK06164   250 LVCEPVfDAART---ARALRRHRVTHTFGNDEMlRRILDtageRADFPSARLFGFASFAPALGElaaLARARGVPLT-GL 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3743 YGPTECCIFCTGYTTKQGFEPSTIGTSV-----ASVSwVVDPENhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFI 3817
Cdd:PRK06164   326 YGSSEVQALVALQPATDPVSVRIEGGGRpaspeARVR-ARDPQD-GALLPDGESGEIEIRAPSLMRGYLDNPDATARALT 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3818 DDpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVEVILPSG 3897
Cdd:PRK06164   404 DD------GY----------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL-PGVAAAQVVGATRDG 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3898 QkdhAMLAAFVQLEEGTQnalLDKEAggedsmaqvvFLASVEEELAKrlpeHMVPTVFFSLLHFPTTTSG---KTDRKRL 3974
Cdd:PRK06164   467 K---TVPVAFVIPTDGAS---PDEAG----------LMAACREALAG----FKVPARVQVVEAFPVTESAngaKIQKHRL 526
                          570
                   ....*....|...
gi 1820002560 3975 REIGASFTAQQLA 3987
Cdd:PRK06164   527 REMAQARLAAERA 539
AMP-binding pfam00501
AMP-binding enzyme;
6708-6807 1.58e-22

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 104.70  E-value: 1.58e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6708 FTEQALARPNAPAVCAWDGE-LTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 6786
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100
                   ....*....|....*....|.
gi 1820002560 6787 PASRHEDILRQTGAQVILASA 6807
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDD 101
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
877-1365 1.61e-22

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 104.87  E-value: 1.61e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVlts 956
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVA--- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  957 sqhamlfasserhqvtvskVSTSQLPTVvnfakspvdpgntAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDH 1036
Cdd:cd05935     78 -------------------VVGSELDDL-------------ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1037 ARVLQFASYTFDACIAEIITTLLY-GGCICVPSESDR---RNNLAK-------AISTMdVNCALLTPSVarllEPSAVPS 1105
Cdd:cd05935    126 DVILACLPLFHVTGFVGSLNTAVYvGGTYVLMARWDRetaLELIEKykvtfwtNIPTM-LVDLLATPEF----KTRDLSS 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1106 LKRLVLQGEQVSFADWNRWPG--SVQTINGYGPTEcsVCCNTYSGKQG-FKS---GIIGTSVASLswVVDAGNHNRLAPl 1179
Cdd:cd05935    201 LKVLTGGGAPMPPAVAEKLLKltGLRFVEGYGLTE--TMSQTHTNPPLrPKLqclGIP*FGVDAR--VIDIETGRELPP- 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1180 GSIGELLVEGPILARGYLNDIDKTEAAFIDDpawllegyeghAGRrgRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQR 1259
Cdd:cd05935    276 NEVGEIVVRGPQIFKGYWNRPEETEESFIEI-----------KGR--RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1260 VELGEIEH--HVRECLPEarqlaVEVILPSGQKEHALLAAFIQLDKGnhnalFEEKASGEDsmaqvvfltgVEEELAKRL 1337
Cdd:cd05935    343 VWPAEVEAklYKHPAI*E-----VCVISVPDERVGEEVKAFIVLRPE-----YRGKVTEED----------IIEWAREQM 402
                          490       500
                   ....*....|....*....|....*...
gi 1820002560 1338 PEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd05935    403 AAYKYPREVEFVDELPRSASGKILWRLL 430
PRK09274 PRK09274
peptide synthase; Provisional
5628-6030 1.62e-22

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 106.52  E-value: 1.62e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5628 FTEQAKARPHAPAICAWDG----------ELTYGELDALSSKLAGHLTQLGVKPED----MVPLCFEksmwTVVAMLAVL 5693
Cdd:PRK09274    12 LPRAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMravlMVTPSLE----FFALTFALF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5694 KAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSAQ-HSARWI-----GTNHQVVTVSAGSLGQLSTLVnpvGLPAIPENA 5767
Cdd:PRK09274    88 KAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKaHLARRLfgwgkPSVRRLVTVGGRLLWGGTTLA---TLLRDGAAA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5768 VYIM------------FTSGSTGIPKGVVLEHR---AVVTSCwgrGRAFGITNLSRVLQ----FAsyTFDACMdeiittl 5828
Cdd:PRK09274   165 PFPMadlapddmaailFTSGSTGTPKGVVYTHGmfeAQIEAL---REDYGIEPGEIDLPtfplFA--LFGPAL------- 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5829 myGGCICVP---------SDSDRrndLVKAI-----STMDVSCALLTPsVARLLE--PSSVPTLQMLVLQGEQVSFADWN 5892
Cdd:PRK09274   233 --GMTSVIPdmdptrpatVDPAK---LFAAIerygvTNLFGSPALLER-LGRYGEanGIKLPSLRRVISAGAPVPIAVIE 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5893 RW----PASVQTINGYGPTE----CSICCNTYSGKQGFKS----GI-IGTSVASVSWVV-----DPENH---DRLAPLGS 5951
Cdd:PRK09274   307 RFramlPPDAEILTPYGATEalpiSSIESREILFATRAATdngaGIcVGRPVDGVEVRIiaisdAPIPEwddALRLATGE 386
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 5952 IGELLVEGPILARGYLNDIQKTAAVFIDDpawllegypghpGRQGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRV 6030
Cdd:PRK09274   387 IGEIVVAGPMVTRSYYNRPEATRLAKIPD------------GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
6277-6573 1.70e-22

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 104.44  E-value: 1.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6277 MYPCSPLQEG-----LMSltakRAGD-YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIvqHSElGL---LQVV-- 6345
Cdd:cd19544      1 IYPLAPLQEGilfhhLLA----EEGDpYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAI--LWE-GLsepVQVVwr 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6346 -----VEEkIQWTESKRLEEYLRE---DKAVSMGLGD-PLARYAIIKEAWGGKRWFVWTIHHALYDGWSLpRVLQAVKQA 6416
Cdd:cd19544     74 qaelpVEE-LTLDPGDDALAQLRArfdPRRYRLDLRQaPLLRAHVAEDPANGRWLLLLLFHHLISDHTSL-ELLLEEIQA 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6417 Y---NGAVLETQPSFNAFI-QYLSQQDLEATAAYWQTALADCEAtlfPPLP---SSVkQLVADTTVEHQCPLPSRSTSDt 6489
Cdd:cd19544    152 IlagRAAALPPPVPYRNFVaQARLGASQAEHEAFFREMLGDVDE---PTAPfglLDV-QGDGSDITEARLALDAELAQR- 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6490 ttstlIRA---------------AWAIVASRYTSSDDVVFGTTITGRNAPVTSIDAIVGPTIATVPLRVRLQkDQTVSSF 6554
Cdd:cd19544    227 -----LRAqarrlgvspaslfhlAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREA 300
                          330
                   ....*....|....*....
gi 1820002560 6555 LGYLQQQATEMIAYEQTGL 6573
Cdd:cd19544    301 VRQTHARLAELLRHEHASL 319
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
5626-6137 1.98e-22

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 105.99  E-value: 1.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDG-ELTYGELDALSSKLAGHLTQLGVKPEDMVplCFEKSMWT--VVAMLAVLKAGGAFVPL 5702
Cdd:PRK06087    27 DYWQQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRV--AFQLPGWCefTIIYLACLKVGAVSVPL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5703 DPdhpASRHED---TFRHTGAQVVVT-----SAQHSARWIGTNHQVVT-------------VSAGSLGQL----STLVNP 5757
Cdd:PRK06087   105 LP---SWREAElvwVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQlqqivgvdklapaTSSLSLSQIiadyEPLTTA 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5758 VglPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTScwgrGRAF-GITNLSRV--------LQFASYTFDAcmdeIITTL 5828
Cdd:PRK06087   182 I--TTHGDELAAVLFTSGTEGLPKGVMLTHNNILAS----ERAYcARLNLTWQdvfmmpapLGHATGFLHG----VTAPF 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5829 MYGGCIcVPSDSDRRNDLVKAISTMDVSCAL-LTPSVARLL-----EPSSVPTLQMLVLQGEQVsfadwnrwPAS-VQTI 5901
Cdd:PRK06087   252 LIGARS-VLLDIFTPDACLALLEQQRCTCMLgATPFIYDLLnllekQPADLSALRFFLCGGTTI--------PKKvAREC 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5902 NGYGPTECSICCNTYSGKQGF---------KSGIIGTSVASVSW-VVDpENHDRLaPLGSIGELLVEGPILARGYLNDIQ 5971
Cdd:PRK06087   323 QQRGIKLLSVYGSTESSPHAVvnlddplsrFMHTDGYAAAGVEIkVVD-EARKTL-PPGCEGEEASRGPNVFMGYLDEPE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5972 KTAAVfIDDPAWllegypghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQLAV 6051
Cdd:PRK06087   401 LTARA-LDEEGW---------------YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQH-PKIHDACV 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6052 eVILPS---GQKdhamLAAFVQLEEGTQNALLdkeasgEDSMAqvvFLAsvEEELAKRL-PEHMVptvffSLLHFPTTTS 6127
Cdd:PRK06087   464 -VAMPDerlGER----SCAYVVLKAPHHSLTL------EEVVA---FFS--RKRVAKYKyPEHIV-----VIDKLPRTAS 522
                          570
                   ....*....|
gi 1820002560 6128 GKTDRKRLRE 6137
Cdd:PRK06087   523 GKIQKFLLRK 532
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
4550-5057 2.76e-22

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 105.33  E-value: 2.76e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4550 QARARPDTPAICAWDGELTYGELDTLSSKLASHLV-QLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 4628
Cdd:PRK06839    11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4629 RHEHIFRQTGAQVVLASAQYATLWTSL-GRSVVIVSEASTSQLPVVTKTADPSVNPG-NAAYAI-FTSGSTGIPKGVVLE 4705
Cdd:PRK06839    91 ELIFQLKDSGTTVLFVEKTFQNMALSMqKVSYVQRVISITSLKEIEDRKIDNFVEKNeSASFIIcYTSGTTGKPKGAVLT 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4706 HKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEI-ITTLLCCGCICVPsdsdRRNNLAKAINAMD---VNWALLTP 4781
Cdd:PRK06839   171 QENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVIIVP----RKFEPTKALSMIEkhkVTVVMGVP 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4782 SVARMLDPCV------VQSLKILVLGG----EQVNSADWDRWPKSIQtinAYGPTECSICCTTYSgKQGF--KSGTIGTS 4849
Cdd:PRK06839   247 TIHQALINCSkfettnLQSVRWFYNGGapcpEELMREFIDRGFLFGQ---GFGMTETSPTVFMLS-EEDArrKVGSIGKP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4850 IVSVSWVVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAFiddpawllegygghsgRQGRLYkTGDLVRYDAD 4929
Cdd:PRK06839   323 VLFCDYELIDENKNKVEV-GEVGELLIRGPNVMKEYWNRPDATEETI----------------QDGWLC-TGDLARVDED 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4930 GNLVYLGRKDSQVKLRGQRVELGEVEHHVREcLTEAKQLAVeVIVPEGEGGYAMLAAFVqlgddtyntlvkeKAGGDSLT 5009
Cdd:PRK06839   385 GFVYIVGRKKEMIISGGENIYPLEVEQVINK-LSDVYEVAV-VGRQHVKWGEIPIAFIV-------------KKSSSVLI 449
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 5010 VQVVfLDRVEEELAK-RVPEhmmltTFFTLEAMPTTTSGKIDRKRLREI 5057
Cdd:PRK06839   450 EKDV-IEHCRLFLAKyKIPK-----EIVFLKELPKNATGKIQKAQLVNQ 492
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
1906-2444 2.85e-22

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 105.85  E-value: 2.85e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1906 ETTTPEDRQQLWAWNQEVPPAIE---RCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVV 1982
Cdd:PRK05605     6 EMSAFADKPWLQSYAPWTPHDLDygdTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1983 PLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVV---TSAQHSARWIGTN--HQVVTV------- 2050
Cdd:PRK05605    86 AIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIvwdKVAPTVERLRRTTplETIVSVnmiaamp 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2051 -----------------------SAGSLEQFSTLV--------NPVDLPA-KPENAAYVMFTSGSTGTPKGVVLEHRAVV 2098
Cdd:PRK05605   166 llqrlalrlpipalrkaraaltgPAPGTVPWETLVdaaiggdgSDVSHPRpTPDDVALILYTSGTTGKPKGAQLTHRNLF 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2099 TSCLgHGQAF------GVTNLLRAL-QFTAYTFDVCIAeiITTLVHGGCICVPS-------DSERR-------------D 2151
Cdd:PRK05605   246 ANAA-QGKAWvpglgdGPERVLAALpMFHAYGLTLCLT--LAVSIGGELVLLPApdidlilDAMKKhpptwlpgvpplyE 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2152 NLAKAITDMQVNwgyLTS-----SVARLLDPCLVpslkvlvlggeqvnstdwGKWPSSV--QTINGYGPTECC--VFCT- 2221
Cdd:PRK05605   323 KIAEAAEERGVD---LSGvrnafSGAMALPVSTV------------------ELWEKLTggLLVEGYGLTETSpiIVGNp 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2222 -------GYTGIQgFQSGNIGtsiasvswVVDPENHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpaWlleg 2294
Cdd:PRK05605   382 msddrrpGYVGVP-FPDTEVR--------IVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--W---- 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2295 ypghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVeVVPPSGERDHAMLAA 2374
Cdd:PRK05605   447 -----------FRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLRE-HPGVEDAAV-VGLPREDGSEEVVAA 513
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2375 fIRLDDETRNSPliikyaednstaqivflTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:PRK05605   514 -VVLEPGAALDP-----------------EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
852-1365 2.89e-22

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 104.90  E-value: 2.89e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  852 RCIHDLFAEQARARPDASAVCAWDG--ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAF 929
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  930 VPLDPGHPASRHEE---------IFKQIGAQVVLTSSQhamLFASSERHQVTV-SKVSTSQLPTvvnFAKSPVDPGNTAY 999
Cdd:cd05923     81 ALINPRLKAAELAEliergemtaAVIAVDAQVMDAIFQ---SGVRVLALSDLVgLGEPESAGPL---IEDPPREPEQPAF 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1000 IIFTSGTTGIPKGVVLQHRAVTTSCL--GHGEAFGYTDHARVLQFAS-YTFDACIAEIITTLLYGGCICVPSEsDRRNNL 1076
Cdd:cd05923    155 VFYTSGTTGLPKGAVIPQRAAESRVLfmSTQAGLRHGRHNVVLGLMPlYHVIGFFAVLVAALALDGTYVVVEE-FDPADA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1077 AKAISTMDVNCALLTPS------VARLLEPSAVPSLKRLVLQGEQVSFADWNR----WPGsvQTINGYGPTEcsVCCNTY 1146
Cdd:cd05923    234 LKLIEQERVTSLFATPThldalaAAAEFAGLKLSSLRHVTFAGATMPDAVLERvnqhLPG--EKVNIYGTTE--AMNSLY 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1147 --------SGKQGFKSGIIGTSVaslswvvdAGNHNRLAPLGSIGELLVEGPILA--RGYLNDIDKTEAAFIDdpawlle 1216
Cdd:cd05923    310 mrdartgtEMRPGFFSEVRIVRI--------GGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD------- 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1217 gyeghagrrgRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhhvrECL---PEARQLAVeVILPSgQKEHA 1293
Cdd:cd05923    375 ----------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIE----RVLsrhPGVTEVVV-IGVAD-ERWGQ 438
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 1294 LLAAFIQLDKGNHNAlfeekasgeDSMAQVVfltgVEEELA--KRlpehmvPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd05923    439 SVTACVVPREGTLSA---------DELDQFC----RASELAdfKR------PRRYFFLDELPKNAMNKVLRRQL 493
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
4116-4443 3.30e-22

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 104.03  E-value: 3.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4116 YPCSPLQEGlMSLTAKRAGD---YIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSElGLLQVVVEERIQ--- 4189
Cdd:cd19066      2 IPLSPMQRG-MWFLKKLATDpsaFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAG-RYEQVVLDKTVRfri 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4190 ---------WTESESLEEYPREDKAVSMGVGDRLARYALIKEpydGGKRW-FVWTMHHALYDGWSLPRILHAVKQAYSGv 4259
Cdd:cd19066     80 eiidlrnlaDPEARLLELIDQIQQTIYDLERGPLVRVALFRL---ADERDvLVVAIHHIIVDGGSFQILFEDISSVYDA- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4260 vLERQ--------PSFNAFI----QYLSQQDPEAAAAYWQTALVD-CKAALFPTLPPTVTQPVADTTVEYQCPPPSQS-- 4324
Cdd:cd19066    156 -AERQkptlpppvGSYADYAawleKQLESEAAQADLAYWTSYLHGlPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETkr 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4325 ------ATDITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQ 4398
Cdd:cd19066    235 lrevarESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTK 312
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 4399 QQATDMIAHEQTG---LQRIAKMSPGARHACGFQTLLVVQPTDDVLGS 4443
Cdd:cd19066    313 EQSREAIEHQRVPfieLVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGK 360
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
846-1370 3.37e-22

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 105.63  E-value: 3.37e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  846 MPPAVDRCIHDLFAEQARARPDASAVCAWDGEL--TYGELDELSSKLAAHLVQLGVKREDVV----PLCFEksmWTVVAM 919
Cdd:PRK12583    12 DKPLLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVgiwaPNCAE---WLLTQF 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  920 lAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVL------TSSQHAMLFA-SSERHQVTVSKVSTSQLP---TVVNFAK 989
Cdd:PRK12583    89 -ATARIGAILVNINPAYRASELEYALGQSGVRWVIcadafkTSDYHAMLQElLPGLAEGQPGALACERLPelrGVVSLAP 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  990 SPVdPGNTAY-----------------------------IIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVL 1040
Cdd:PRK12583   168 APP-PGFLAWhelqargetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLC 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1041 qfASYTFDACIAEIITTLL---YGGCICVPSESDRRNNLAKAIStmDVNCALL----TPSVARLLEPS----AVPSLKRL 1109
Cdd:PRK12583   247 --VPVPLYHCFGMVLANLGcmtVGACLVYPNEAFDPLATLQAVE--EERCTALygvpTMFIAELDHPQrgnfDLSSLRTG 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1110 VLQGEQVSFADWNRWPGSVQ----TInGYGPTECSVCCNtysgkQGFKSGIIGTSVASL--------SWVVDA-GNhnrL 1176
Cdd:PRK12583   323 IMAGAPCPIEVMRRVMDEMHmaevQI-AYGMTETSPVSL-----QTTAADDLERRVETVgrtqphleVKVVDPdGA---T 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1177 APLGSIGELLVEGPILARGYLNDIDKTEAAfIDDPAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVR 1256
Cdd:PRK12583   394 VPRGEIGELCTRGYSVMKGYWNNPEATAES-IDEDGWM---------------HTGDLATMDEQGYVRIVGRSKDMIIRG 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1257 GQRVELGEIEHHVrecLPEARQLAVEVILPSGQKEHALLAAFIQLDKGnhnalfeEKASGEDsmaqvvfltgVEEELAKR 1336
Cdd:PRK12583   458 GENIYPREIEEFL---FTHPAVADVQVFGVPDEKYGEEIVAWVRLHPG-------HAASEEE----------LREFCKAR 517
                          570       580       590
                   ....*....|....*....|....*....|....
gi 1820002560 1337 LPEHMVPTILFTVKAMPITTSGKIDRKRLQDIGA 1370
Cdd:PRK12583   518 IAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISI 551
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
841-1360 4.05e-22

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 105.35  E-value: 4.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  841 VWNADMPPAVDRCIHDLFAEQARARPDASAVCaWDGE-------LTYGELDELSSKLAAHLVQLGVKREDVV----PLCF 909
Cdd:cd17634     42 PSIKWFEDATLNLAANALDRHLRENGDRTAII-YEGDdtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVaiymPMIP 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  910 EksmwTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSS----------------QHAMLFASSERHQVTV 973
Cdd:cd17634    121 E----AAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvplkknvdDALNPNVTSVEHVIVL 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  974 SKVST-----------------SQLPTvvnFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHR----AVTTSC-----LGH 1027
Cdd:cd17634    197 KRTGSdidwqegrdlwwrdliaKASPE---HQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGgylvYAATTMkyvfdYGP 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1028 GEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGcicVPSESDrRNNLAKAISTMDVNCALLTPSVARLLEPSA----- 1102
Cdd:cd17634    274 GDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEG---VPNWPT-PARMWQVVDKHGVNILYTAPTAIRALMAAGddaie 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1103 ---VPSLKRLVLQGEQVSFADWnRW------PGSVQTINGYGPTECS-VCCNTYSGKQGFKSG-----IIGTSVAslswV 1167
Cdd:cd17634    350 gtdRSSLRILGSVGEPINPEAY-EWywkkigKEKCPVVDTWWQTETGgFMITPLPGAIELKAGsatrpVFGVQPA----V 424
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1168 VDAGNHNrlAPLGSIGELLVEGPI--LARGYLNDIDKTEAAFiddpawlLEGYEGhagrrgrLYKTGDLVRCDADGNLVC 1245
Cdd:cd17634    425 VDNEGHP--QPGGTEGNLVITDPWpgQTRTLFGDHERFEQTY-------FSTFKG-------MYFSGDGARRDEDGYYWI 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1246 LGRKDSQVKVRGQRVELGEIEhHVRECLPEARQLAVeVILPSGQKEHAlLAAFIQLDKGnhnalfeekasgedsmaqVVF 1325
Cdd:cd17634    489 TGRSDDVINVAGHRLGTAEIE-SVLVAHPKVAEAAV-VGIPHAIKGQA-PYAYVVLNHG------------------VEP 547
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1820002560 1326 LTGVEEELAKRLPEHM----VPTILFTVKAMPITTSGKI 1360
Cdd:cd17634    548 SPELYAELRNWVRKEIgplaTPDVVHWVDSLPKTRSGKI 586
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
996-1362 5.04e-22

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 101.57  E-value: 5.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  996 NTAYIIFTSGTTGIPKGVVLQHR---AVTTSCLGHGEAFGYTDHARVLQFASYTFDacIAEIITTLLYGGCICVPSESDR 1072
Cdd:cd17635      2 DPLAVIFTSGTTGEPKAVLLANKtffAVPDILQKEGLNWVVGDVTYLPLPATHIGG--LWWILTCLIHGGLCVTGGENTT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1073 RNNLAKAISTMDVNCALLTPSVARLLEP------SAVPSLkRLVLQGEQVSFADWNR---WPGSVQTINGYGPTECSVCC 1143
Cdd:cd17635     80 YKSLFKILTTNAVTTTCLVPTLLSKLVSelksanATVPSL-RLIGYGGSRAIAADVRfieATGLTNTAQVYGLSETGTAL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1144 NTYSGKQGFKSGIIGTSVASLSWVVdAGNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpaWLlegyeghag 1223
Cdd:cd17635    159 CLPTDDDSIEINAVGRPYPGVDVYL-AATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG--WV--------- 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1224 rrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhHVRECLPEARQLAVEVIlpsgqkEHALLAAFIQLdk 1303
Cdd:cd17635    227 ------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECACYEI------SDEEFGELVGL-- 291
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 1304 gnhnalfEEKASGEDSMAQVvflTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDR 1362
Cdd:cd17635    292 -------AVVASAELDENAI---RALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK06188 PRK06188
acyl-CoA synthetase; Validated
4552-5056 5.26e-22

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 104.68  E-value: 5.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4552 RARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHP-ASRH 4630
Cdd:PRK06188    23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL---HPlGSLD 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4631 EHIFR----------------QTGAQVVLASAQYATLWTSLGRSVV---IVSEASTSQlpvvTKTADPSVNPGNAAYAIF 4691
Cdd:PRK06188   100 DHAYVledagistlivdpapfVERALALLARVPSLKHVLTLGPVPDgvdLLAAAAKFG----PAPLVAAALPPDIAGLAY 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4692 TSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFA--SYtfdACIAEIITTLLCCGCICVPSDSDRRNNLAkAI 4769
Cdd:PRK06188   176 TGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTplSH---AGGAFFLPTLLRGGTVIVLAKFDPAEVLR-AI 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4770 NAMDVNWALLTPS-VARMLD-PCV----VQSLKILVLGGEQVNSAdwdRWPKSIQTI-----NAYGPTECSICCTT---- 4834
Cdd:PRK06188   252 EEQRITATFLVPTmIYALLDhPDLrtrdLSSLETVYYGASPMSPV---RLAEAIERFgpifaQYYGQTEAPMVITYlrkr 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4835 -YSGKQGFKSGTIGTSIVSVSWVVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAFIDDpaWLlegyggHsgr 4913
Cdd:PRK06188   329 dHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQ-GEVGEICVRGPLVMDGYWNRPEETAEAFRDG--WL------H--- 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4914 qgrlykTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHhvreCLTEAKQLA-VEVI-VPEGEGGYAMLAAFVQLG 4991
Cdd:PRK06188   397 ------TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVED----VLAEHPAVAqVAVIgVPDEKWGEAVTAVVVLRP 466
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4992 DDTYNT-----LVKEKAGGDSLTVQVVFLDrveeelakrvpehmmlttfftleAMPTTTSGKIDRKRLRE 5056
Cdd:PRK06188   467 GAAVDAaelqaHVKERKGSVHAPKQVDFVD-----------------------SLPLTALGKPDKKALRA 513
PRK07787 PRK07787
acyl-CoA synthetase; Validated
4548-4955 5.62e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 103.92  E-value: 5.62e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4548 AEQARARPDTPAICAWDGELTYGELDTLSSKLAShlvqlGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPA 4627
Cdd:PRK07787     7 AAVAAAADIADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4628 SRHEHIFRQTGAQVVLASAQyatlWTSLGRSVVIVSEASTSQlpvvtkTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHK 4707
Cdd:PRK07787    82 AERRHILADSGAQAWLGPAP----DDPAGLPHVPVRLHARSW------HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRR 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4708 AVVTSCLGHGQAFGIT-DHT-------------------------RVLQFASYTFDACIAEIIT--TLLccgcICVPSDS 4759
Cdd:PRK07787   152 AIAADLDALAEAWQWTaDDVlvhglplfhvhglvlgvlgplrignRFVHTGRPTPEAYAQALSEggTLY----FGVPTVW 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4760 DRrnnLAKAinamdvnwalltPSVARMLDPCvvqslKILVLGGEQVNSADWDRWPKSI--QTINAYGPTECSICCTTY-S 4836
Cdd:PRK07787   228 SR---IAAD------------PEAARALRGA-----RLLVSGSAALPVPVFDRLAALTghRPVERYGMTETLITLSTRaD 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4837 GKQgfKSGTIGTSIVSVSWVVDPENHNRLAPLG-SIGELLVEGPILARGYLNDMEKTEAAFIDDpAWllegygghsgrqg 4915
Cdd:PRK07787   288 GER--RPGWVGLPLAGVETRLVDEDGGPVPHDGeTVGELQVRGPTLFDGYLNRPDATAAAFTAD-GW------------- 351
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 4916 rlYKTGDLVRYDADGNLVYLGRKDSQ-VKLRGQRVELGEVE 4955
Cdd:PRK07787   352 --FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIE 390
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
5632-6137 5.96e-22

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 104.63  E-value: 5.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGE------LTYGELDALSSKLAGHLTQLGvKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 5705
Cdd:cd05931      3 AAARPDRPAYTFLDDEggreetLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5706 HPASRHEDT---FRHTGAQVVVTSAQHSARWIGTNHQVVTVSAGSL----GQLSTLVNPVGLPAIPENAV-YIMFTSGST 5777
Cdd:cd05931     82 TPGRHAERLaaiLADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLlvvdLLPDTSAADWPPPSPDPDDIaYLQYTSGST 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5778 GIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICV---PSDSDRRNDL-VKAISTM 5853
Cdd:cd05931    162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVlmsPAAFLRRPLRwLRLISRY 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5854 DVSCallTPS-------VARLLEPSSVPTL-----QMLVLQGEQVS----------FADWNRWPASVQTinGYGPTECSI 5911
Cdd:cd05931    242 RATI---SAApnfaydlCVRRVRDEDLEGLdlsswRVALNGAEPVRpatlrrfaeaFAPFGFRPEAFRP--SYGLAEATL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5912 ccnTYSGKQGFKSGII---------------------GTSVASVSWV--------VDPENHDRLAPlGSIGELLVEGPIL 5962
Cdd:cd05931    317 ---FVSGGPPGTGPVVlrvdrdalagravavaaddpaARELVSCGRPlpdqevriVDPETGRELPD-GEVGEIWVRGPSV 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5963 ARGYLNDIQKTAAVF-----IDDPAWLlegypghpgrqgrlyKTGDL-VRYDanGNLVCLGRKDSQVKLRGQRVELGEVE 6036
Cdd:cd05931    393 ASGYWGRPEATAETFgalaaTDEGGWL---------------RTGDLgFLHD--GELYITGRLKDLIIVRGRNHYPQDIE 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6037 HHVRECLPEARQLAVevilpsgqkdhamlAAF-VQLEEGTQNALLDKEASGEDSMAQVVFLASVEEELAKrlpEHMVPT- 6114
Cdd:cd05931    456 ATAEEAHPALRPGCV--------------AAFsVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAR---EHGVAPa 518
                          570       580
                   ....*....|....*....|....*
gi 1820002560 6115 --VFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:cd05931    519 dvVLVRPGSIPRTSSGKIQRRACRA 543
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
7632-8021 6.88e-22

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 102.94  E-value: 6.88e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7632 ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVAS 7711
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7712 AQYsarwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNL 7791
Cdd:cd05935     81 SEL-----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7792 SRVLQFASYTFDA-CIAEIITTLLCGGCICVPSDSDrRNSLAKAISTMDVN-WAFLTPSVARLL-DPGL----IPSLKIL 7864
Cdd:cd05935    126 DVILACLPLFHVTgFVGSLNTAVYVGGTYVLMARWD-RETALELIEKYKVTfWTNIPTMLVDLLaTPEFktrdLSSLKVL 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7865 AIGGEQSSSADWNRWPGSVQKIHV--YGPTECCIfCTGYTTKQGFEPSTIGTSVASV-SWVVDPENHNRLAPlGSMGELL 7941
Cdd:cd05935    205 TGGGAPMPPAVAEKLLKLTGLRFVegYGLTETMS-QTHTNPPLRPKLQCLGIP*FGVdARVIDIETGRELPP-NEVGEIV 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7942 MEGPILARGYLNDVDKTEAAFIDDpawllegypghPGRqgRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 8021
Cdd:cd05935    283 VRGPQIFKGYWNRPEETEESFIEI-----------KGR--RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE 349
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
5622-6081 8.55e-22

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 103.74  E-value: 8.55e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5622 RCVHDLFTEQAKARPHAPAICAWDG--ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAF 5699
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5700 VPLDP-------DHPASRHEDT--FRHTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLGQLstlvnPVGLPAIPENAVYI 5770
Cdd:cd05923     81 ALINPrlkaaelAELIERGEMTaaVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPL-----IEDPPREPEQPAFV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5771 MFTSGSTGIPKGVVLEHRA----------VVTSCWGRG-RAFGITNLSRVLQFASYtfdacmdeIITTLMYGGCICVPSD 5839
Cdd:cd05923    156 FYTSGTTGLPKGAVIPQRAaesrvlfmstQAGLRHGRHnVVLGLMPLYHVIGFFAV--------LVAALALDGTYVVVEE 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5840 sDRRNDLVKAISTMDVSCALLTPS------VARLLEPSSVPTLQMLVLQGEQVSFADWNRWPASVQT--INGYGPTEcsI 5911
Cdd:cd05923    228 -FDPADALKLIEQERVTSLFATPThldalaAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGekVNIYGTTE--A 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5912 CCNTY--------SGKQGFKSGIigtSVASVSwvvdpENHDRLAPLGSIGELLVEGPILA--RGYLNDIQKTAAVFIDdp 5981
Cdd:cd05923    305 MNSLYmrdartgtEMRPGFFSEV---RIVRIG-----GSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-- 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5982 awllegypghpgrqgRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECL---PEARQLAVeVILPSg 6058
Cdd:cd05923    375 ---------------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIE----RVLsrhPGVTEVVV-IGVAD- 433
                          490       500
                   ....*....|....*....|....
gi 1820002560 6059 QKDHAMLAAFVQLEEGTQNA-LLD 6081
Cdd:cd05923    434 ERWGQSVTACVVPREGTLSAdELD 457
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
7610-8134 8.62e-22

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 105.78  E-value: 8.62e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7610 HDLFAEQARARPGAPAICawD---GELTYGELDVLSSNLAgHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP 7686
Cdd:PRK08633   618 AEAWIDTAKRNWSRLAVA--DstgGELSYGKALTGALALA-RLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVN 694
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7687 LDpdHPASrhEEIF----EQTGAQVVVASAQY----SARWTSSSC----HVV-------TVSK-------ALSSQLPA-- 7738
Cdd:PRK08633   695 LN--YTAS--EAALksaiEQAQIKTVITSRKFleklKNKGFDLELpenvKVIyledlkaKISKvdkltalLAARLLPArl 770
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7739 VVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHR-------AVAT-----------SCLGHGRAFGITnlsrvlqfasy 7800
Cdd:PRK08633   771 LKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHnilsnieQISDvfnlrnddvilSSLPFFHSFGLT----------- 839
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7801 tfdaciaeiITTL--LCGG--CICVPSDSDRRnSLAKAISTMDVNWAFLTPSVARL------LDPGLIPSLKILAIGGEq 7870
Cdd:PRK08633   840 ---------VTLWlpLLEGikVVYHPDPTDAL-GIAKLVAKHRATILLGTPTFLRLylrnkkLHPLMFASLRLVVAGAE- 908
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7871 sssadwnRWPGSV-----QKIHV-----YGPTECC---------IFCTGYTTKQGFEPSTIGTSVASVSW-VVDPENHNR 7930
Cdd:PRK08633   909 -------KLKPEVadafeEKFGIrilegYGATETSpvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVrIVDPETFEE 981
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7931 LAPlGSMGELLMEGPILARGYLNDVDKTEAAF--IDDPAWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQV 8008
Cdd:PRK08633   982 LPP-GEDGLILIGGPQVMKGYLGDPEKTAEVIkdIDGIGW---------------YVTGDKGHLDEDGFLTITDRYSRFA 1045
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8009 KVRGQRVELGEVEHHVRECLPEARQLAVEVILPSGQKNHaMLAVFVQLGKGThIAHLEEKAggedsmaqvvfltgteeeL 8088
Cdd:PRK08633  1046 KIGGEMVPLGAVEEELAKALGGEEVVFAVTAVPDEKKGE-KLVVLHTCGAED-VEELKRAI------------------K 1105
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 8089 AKRLPKHMVPTVFFALLHFPMTTSGKADRKRLREIgasftAQQLAE 8134
Cdd:PRK08633  1106 ESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL-----ALALLG 1146
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
3461-3920 8.70e-22

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 103.74  E-value: 8.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3461 RCVHDLFTEQAKARPHAPAICAWDG--ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAF 3538
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3539 VPLDPDHPASRHEEIFE---------QTGAQVVVASAQYSARWTSSSCHVVTVSKALSSQLPAvvdstNTSVRPENAAYI 3609
Cdd:cd05923     81 ALINPRLKAAELAELIErgemtaaviAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIE-----DPPREPEQPAFV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3610 IFTSGSTGVPKGVVLEHRAVATSCL-----------GHGRAFGITNLSRVLQFasytfdacIAEIITTLLCGGCICVPSD 3678
Cdd:cd05923    156 FYTSGTTGLPKGAVIPQRAAESRVLfmstqaglrhgRHNVVLGLMPLYHVIGF--------FAVLVAALALDGTYVVVEE 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3679 SDRRNSLaKAISTMDVNWAFLTPS------VARLLDPGLIPSLKILAIGGEQSSSADWNR----WPGsvQKIHVYGPTEC 3748
Cdd:cd05923    228 FDPADAL-KLIEQERVTSLFATPThldalaAAAEFAGLKLSSLRHVTFAGATMPDAVLERvnqhLPG--EKVNIYGTTEA 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3749 CIFC------TGYTTKQGFEpstigtsvASVSWVVDPENHNRLAPLGSMGELLMEGPILA--RGYLNDVDKTEAAFIDdp 3820
Cdd:cd05923    305 MNSLymrdarTGTEMRPGFF--------SEVRIVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-- 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3821 awllegypghpgrqgRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvrECL---PEARQLAVeVILPSg 3897
Cdd:cd05923    375 ---------------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIE----RVLsrhPGVTEVVV-IGVAD- 433
                          490       500
                   ....*....|....*....|....
gi 1820002560 3898 QKDHAMLAAFVQLEEGTQNA-LLD 3920
Cdd:cd05923    434 ERWGQSVTACVVPREGTLSAdELD 457
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3487-3975 9.54e-22

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 102.60  E-value: 9.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdhpasrheeiFEQTGAQVVvasa 3566
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPL------------FTAFGPKAI---- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3567 qySARWTSSSCHVVtvskalssqlpaVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLS 3646
Cdd:cd05973     65 --EHRLRTSGARLV------------VTDAANRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3647 RVLQFAS--------YTFDACIAEIITTLLCGGCICVPSDSDrrnslakAISTMDVNWAFLTPSVARLLDPGLIPSLKIL 3718
Cdd:cd05973    131 SFWNAADpgwayglyYAITGPLALGHPTILLEGGFSVESTWR-------VIERLGVTNLAGSPTAYRLLMAAGAEVPARP 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3719 AIGGEQSSSA------DWNRWPGSVQKIHV---YGPTECCIF-CTGYTTKQGFEPSTIGTSVASVSWVVDPENHNRLAPl 3788
Cdd:cd05973    204 KGRLRRVSSAgepltpEVIRWFDAALGVPIhdhYGQTELGMVlANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGP- 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3789 GSMGELLMegpilargylnDVDKTeaafiddPAWLLEGY--PGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRG 3866
Cdd:cd05973    283 GEPGRLAI-----------DIANS-------PLMWFRGYqlPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSG 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3867 QRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHaMLAAFVQLEEGTQnalldkeaGGEDsmaqvvflasVEEELA--- 3943
Cdd:cd05973    345 YRIGPFDVESALIE-HPAVAEAAV-IGVPDPERTE-VVKAFVVLRGGHE--------GTPA----------LADELQlhv 403
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 3944 -KRLPEHMVP-TVFFsLLHFPTTTSGKTDRKRLR 3975
Cdd:cd05973    404 kKRLSAHAYPrTIHF-VDELPKTPSGKIQRFLLR 436
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
4543-5056 1.02e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 104.07  E-value: 1.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4543 VHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQL-GVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL 4621
Cdd:PRK05677    26 IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNT 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4622 DPDHPASRHEHIFRQTGAQVVLASAQYATLWTSL----GRSVVIVSEAS-----------------------TSQLPVVT 4674
Cdd:PRK05677   106 NPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVlpktGVKHVIVTEVAdmlpplkrllinavvkhvkkmvpAYHLPQAV 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4675 KTAD----------PSVNPGNAAYAI--FTSGSTGIPKGVVLEH----------KAVVTSCLGHGQAFGITDhTRVLQFA 4732
Cdd:PRK05677   186 KFNDalakgagqpvTEANPQADDVAVlqYTGGTTGVAKGAMLTHrnlvanmlqcRALMGSNLNEGCEILIAP-LPLYHIY 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4733 SYTFDaCIAEIIT---TLLccgcICVPSDSDRR-NNLAK-------AINAMDVnwALLTPSVARMLDpcvVQSLKILVLG 4801
Cdd:PRK05677   265 AFTFH-CMAMMLIgnhNIL----ISNPRDLPAMvKELGKwkfsgfvGLNTLFV--ALCNNEAFRKLD---FSALKLTLSG 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4802 GEQVNSADWDRWPK--SIQTINAYGPTECSICcTTYSGKQGFKSGTIGTSIVSVSW-VVDPENHNrlAPLGSIGELLVEG 4878
Cdd:PRK05677   335 GMALQLATAERWKEvtGCAICEGYGMTETSPV-VSVNPSQAIQVGTIGIPVPSTLCkVIDDDGNE--LPLGEVGELCVKG 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4879 PILARGYLNDMEKTEAAFiDDPAWLlegygghsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhHV 4958
Cdd:PRK05677   412 PQVMKGYWQRPEATDEIL-DSDGWL---------------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELE-DV 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4959 RECLTEAKQLAVeVIVPEGEGGYAmLAAFVqlgddtyntLVKEkagGDSLTVQVVFLDRVEEELAKRVPEHMMLTtfftl 5038
Cdd:PRK05677   475 LAALPGVLQCAA-IGVPDEKSGEA-IKVFV---------VVKP---GETLTKEQVMEHMRANLTGYKVPKAVEFR----- 535
                          570
                   ....*....|....*...
gi 1820002560 5039 EAMPTTTSGKIDRKRLRE 5056
Cdd:PRK05677   536 DELPTTNVGKILRRELRD 553
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
7747-8045 1.08e-21

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 103.18  E-value: 1.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7747 VRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQ----FASYTFDACiaeIITTLLCGGCI-CV 7821
Cdd:cd05909    144 VQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGC---LWLPLLSGIKVvFH 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7822 PSDSDRRnSLAKAISTMDVNWAFLTPS----VARLLDPGLIPSLKILAIGGEQSSSADWNRWpgsVQKIHV-----YGPT 7892
Cdd:cd05909    221 PNPLDYK-KIPELIYDKKATILLGTPTflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEF---QEKFGIrilegYGTT 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7893 ECCIFCTGYTTKQGFEPSTIGTSVASVSW-VVDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdpAWlle 7971
Cdd:cd05909    297 ECSPVISVNTPQSPNKEGTVGRPLPGMEVkIVSVETHEEV-PIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD--GW--- 370
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 7972 gypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVRECLPEARQLAVeVILPSGQK 8045
Cdd:cd05909    371 ------------YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAV-VSVPDGRK 431
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
6281-6464 1.41e-21

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 97.80  E-value: 1.41e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6281 SPLQEGLMSLTAKRAgDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSElGLLQVVVEE-KIQWT------ 6353
Cdd:COG4908      2 SPAQKRFLFLEPGSN-AYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDG-EPVQRIDPDaDLPLEvvdlsa 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6354 -----ESKRLEEYLREDKAVSMGLG-DPLARYAIIKEAWGGKRwFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQP- 6426
Cdd:COG4908     80 lpepeREAELEELVAEEASRPFDLArGPLLRAALIRLGEDEHV-LLLTIHHIISDGWSLGILLRELAALYAALLEGEPPp 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 6427 ------SFNAFI----QYLSQQDLEATAAYWQTALADCEATLfpPLPS 6464
Cdd:COG4908    159 lpelpiQYADYAawqrAWLQSEALEKQLEYWRQQLAGAPPVL--ELPT 204
PRK06178 PRK06178
acyl-CoA synthetase; Validated
5599-6137 1.49e-21

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 103.58  E-value: 1.49e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5599 ETTTLEDRQQLW--AWNQNVP-----PAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKP 5671
Cdd:PRK06178     3 EEAYLAELRALQqaAWPAGIPrepeyPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5672 EDMV----PLC--FeksmwtVVAMLAVLKAGGAFVPLDPdhPASRHEdtFRH----TGAQVVVT-----------SAQHS 5730
Cdd:PRK06178    83 GDRVavflPNCpqF------HIVFFGILKLGAVHVPVSP--LFREHE--LSYelndAGAEVLLAldqlapvveqvRAETS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5731 ARwigtnHQVVTVSAGSLGQLSTLVNPVGL---PAIPENAVYIM------------------------FTSGSTGIPKGV 5783
Cdd:PRK06178   153 LR-----HVIVTSLADVLPAEPTLPLPDSLrapRLAAAGAIDLLpalractapvplpppaldalaalnYTGGTTGMPKGC 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5784 VLEHRAVV-TSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDsdrRNDLVKAISTMD----VSCA 5858
Cdd:PRK06178   228 EHTQRDMVyTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLA---RWDAVAFMAAVEryrvTRTV 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5859 LLTPSVARLLEPSSVPTLQMLVLQGEQ-VSF-----ADW-NRWPA---SVQTINGYGPTECSIcCNTYSgkQGFKSG--- 5925
Cdd:PRK06178   305 MLVDNAVELMDHPRFAEYDLSSLRQVRvVSFvkklnPDYrQRWRAltgSVLAEAAWGMTETHT-CDTFT--AGFQDDdfd 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5926 -----------IIGTSVAsvswVVDPENHdRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDdpAWLlegypghpgr 5994
Cdd:PRK06178   382 llsqpvfvglpVPGTEFK----ICDFETG-ELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD--GWL---------- 444
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5995 qgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVE----HHvreclPEARQLAVeviLPSGQKDHAMLA-AFV 6069
Cdd:PRK06178   445 -----HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEallgQH-----PAVLGSAV---VGRPDPDKGQVPvAFV 511
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 6070 QLEEGTQNAlldkeasgedsmaqvvflasvEEELAKRLPEHM----VPTVFFsLLHFPTTTSGKTDRKRLRE 6137
Cdd:PRK06178   512 QLKPGADLT---------------------AAALQAWCRENMavykVPEIRI-VDALPMTATGKVRKQDLQA 561
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
878-1365 1.61e-21

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 102.07  E-value: 1.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPghpasrheeIFKQIGAQVVLTSS 957
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILP---------FFREHELAFILRRA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  958 QHAMLFASSERHQVtvskvstsqlptvvNFAKspvDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHA 1037
Cdd:cd05903     73 KAKVFVVPERFRQF--------------DPAA---MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1038 RVLQFASytfdacIAEiITTLLYGGCICV----PSESDRRNNLAKAISTMD---VNCAL-LTPSVARLLE-----PSAVP 1104
Cdd:cd05903    136 VFLVASP------MAH-QTGFVYGFTLPLllgaPVVLQDIWDPDKALALMRehgVTFMMgATPFLTDLLNaveeaGEPLS 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1105 SLKRLVLQGEQVsfadwnrwPGSV----QTING------YGPTEC-SVCCNTYSGKQGFKSGIIGTSVASLSWVVDAGNH 1173
Cdd:cd05903    209 RLRTFVCGGATV--------PRSLarraAELLGakvcsaYGSTECpGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTG 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1174 NRLAPlGSIGELLVEGPILARGYLNDIDKTEAAFIDdpAWllegyeghagrrgrlYKTGDLVRCDADGNLVCLGRKDSQV 1253
Cdd:cd05903    281 ATLAP-GVEGELLSRGPSVFLGYLDRPDLTADAAPE--GW---------------FRTGDLARLDEDGYLRITGRSKDII 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1254 KVRGQRVELGEIEhhvrECL---PEARQLAVeVILPS---GQKehalLAAFIQLDKGnHNALFEEkasgedsmaQVVFLT 1327
Cdd:cd05903    343 IRGGENIPVLEVE----DLLlghPGVIEAAV-VALPDerlGER----ACAVVVTKSG-ALLTFDE---------LVAYLD 403
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1820002560 1328 GVeeELAK-RLPEHMVptilfTVKAMPITTSGKIDRKRL 1365
Cdd:cd05903    404 RQ--GVAKqYWPERLV-----HVDDLPRTPSGKVQKFRL 435
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
4541-4955 1.83e-21

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 102.59  E-value: 1.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4541 RCVHDQFAEQARARPDTPAICAWDG--ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAF 4618
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4619 VPLDPD-HPASRHEHI--------FRQTGAQVVLASAQYATLWTSLGRSVVIVSEASTSQLPvvtktADPSVNPGNAAYA 4689
Cdd:cd05923     81 ALINPRlKAAELAELIergemtaaVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLI-----EDPPREPEQPAFV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4690 IFTSGSTGIPKGVVLEHKAVVTSCLG----HGQAFGitDHTRVLQFAS-YTFDACIAEIITTLLCCGCICVPSDsDRRNN 4764
Cdd:cd05923    156 FYTSGTTGLPKGAVIPQRAAESRVLFmstqAGLRHG--RHNVVLGLMPlYHVIGFFAVLVAALALDGTYVVVEE-FDPAD 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4765 LAKAINAMDVNWALLTPS------VARMLDPCVVQSLKILVLGGEQVNSADWDRWPKSIQT--INAYGPTEcsICCTTY- 4835
Cdd:cd05923    233 ALKLIEQERVTSLFATPThldalaAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGekVNIYGTTE--AMNSLYm 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4836 -------SGKQGFKSgtiGTSIVSVSwvvdpENHNRLAPLGSIGELLVEGPILA--RGYLNDMEKTEAAFIDdpawlleg 4906
Cdd:cd05923    311 rdartgtEMRPGFFS---EVRIVRIG-----GSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------- 374
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 4907 ygghsgrqgRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE 4955
Cdd:cd05923    375 ---------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIE 414
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1952-2443 1.88e-21

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 101.60  E-value: 1.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1952 DGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVV 2031
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2032 TsaqhsarwigtnhqvvtvsagsleqfstlvnpvDLpakpenaAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVT 2111
Cdd:cd05934     81 V---------------------------------DP-------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2112 NLLRALQFTA--YTFDVCIAeIITTLVHGG-CICVPSDSERRdnLAKAITDMQVNWGYLTSSVARLL-------DPClvp 2181
Cdd:cd05934    121 EDDVYLTVLPlfHINAQAVS-VLAALSVGAtLVLLPRFSASR--FWSDVRRYGATVTNYLGAMLSYLlaqppspDDR--- 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2182 SLKVLVLGGEQVNSTDWGKWPS--SVQTINGYGPTECCvFCTGYTGIQGFQSGNIGTSIASVSW-VVDPenHGRLAPLGS 2258
Cdd:cd05934    195 AHRLRAAYGAPNPPELHEEFEErfGVRLLEGYGMTETI-VGVIGPRDEPRRPGSIGRPAPGYEVrIVDD--DGQELPAGE 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2259 IGELLV---EGPILARGYLNDVDKTQAAFiddpawllegypghegRQGrLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQ 2335
Cdd:cd05934    272 PGELVIrglRGWGFFKGYYNMPEATAEAM----------------RNG-WFHTGDLGYRDADGFFYFVDRKKDMIRRRGE 334
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2336 RVELGEVE-----HhmrkclPEANQLAVEVVP-PSGERDhamLAAFIRLDDETRNSPliikyaednstaqivflTGIEEE 2409
Cdd:cd05934    335 NISSAEVErailrH------PAVREAAVVAVPdEVGEDE---VKAVVVLRPGETLDP-----------------EELFAF 388
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1820002560 2410 LSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLR 2443
Cdd:cd05934    389 CEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
878-1366 2.31e-21

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 101.42  E-value: 2.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpghpasrheeiFKQIGAQVVLtss 957
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPL------------FSAFGPEAIR--- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  958 qhamlfassERHQVTVSKV--STSQLptvvnfaKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSclghgeafgYTD 1035
Cdd:cd05969     66 ---------DRLENSEAKVliTTEEL-------YERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFY---------YFT 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1036 HARVLQFASYTFDACIAE--IITTLLYG-------GCICVPSESD-RRNNLAKAISTMDVNCALLTPSVARLL-----EP 1100
Cdd:cd05969    121 GKYVLDLHPDDIYWCTADpgWVTGTVYGiwapwlnGVTNVVYEGRfDAESWYGIIERVKVTVWYTAPTAIRMLmkegdEL 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1101 SA---VPSLKRLVLQGEQVSfADWNRWPGSVQTI---NGYGPTECS--VCCNtYSGkQGFKSGIIGTSVASLSWVVDAGN 1172
Cdd:cd05969    201 ARkydLSSLRFIHSVGEPLN-PEAIRWGMEVFGVpihDTWWQTETGsiMIAN-YPC-MPIKPGSMGKPLPGVKAAVVDEN 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1173 HNRLAPlGSIGELLVEG--PILARGYLNDIDKTEAAFIDdpawlleGYeghagrrgrlYKTGDLVRCDADGNLVCLGRKD 1250
Cdd:cd05969    278 GNELPP-GTKGILALKPgwPSMFRGIWNDEERYKNSFID-------GW----------YLTGDLAYRDEDGYFWFVGRAD 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1251 SQVKVRGQRVELGEIEhhvrECLPEARQLA-VEVILPSGQKEHALLAAFIQLDKGnhnalFEekASGEdsmaqvvfltgV 1329
Cdd:cd05969    340 DIIKTSGHRVGPFEVE----SALMEHPAVAeAGVIGKPDPLRGEIIKAFISLKEG-----FE--PSDE-----------L 397
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 1330 EEEL----AKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQ 1366
Cdd:cd05969    398 KEEIinfvRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
5626-6137 2.91e-21

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 102.27  E-value: 2.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDGE--LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 5703
Cdd:PRK05852    20 DLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLD 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5704 PDHPASRHEDTFRHTGAQVVVTS-------AQHSARWIGTNHQVVTVSAGSLGQLSTLVNPVGLPAI---------PENA 5767
Cdd:PRK05852   100 PALPIAEQRVRSQAAGARVVLIDadgphdrAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPatstpeglrPDDA 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5768 VyIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNL-SRVLQFASYTFDACMDEIITTLMYGGCICVPSDSD-RRND 5845
Cdd:PRK05852   180 M-IMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRdATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRfSAHT 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5846 LVKAISTMDVSCALLTPSVARLL------EPSSVPTLQMLVLQG------EQVSFADWNRWPASVqtINGYGPTECS--- 5910
Cdd:PRK05852   259 FWDDIKAVGATWYTAVPTIHQILleraatEPSGRKPAALRFIRScsapltAETAQALQTEFAAPV--VCAFGMTEAThqv 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5911 ----ICCNTYSGKQGFKSGIIGTSVASVSWVVDPENHDrlAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDdpAWLle 5986
Cdd:PRK05852   337 tttqIEGIGQTENPVVSTGLVGRSTGAQIRIVGSDGLP--LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD--GWL-- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5987 gypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVElgevehhvreclPEarqlAVEVILPSgqKDHAMLA 6066
Cdd:PRK05852   411 -------------RTGDLGSLSAAGDLSIRGRIKELINRGGEKIS------------PE----RVEGVLAS--HPNVMEA 459
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 6067 AFVqleeGTQNALLdkeasGEDSMAQVVFLASVE---EELA----KRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:PRK05852   460 AVF----GVPDQLY-----GEAVAAVIVPRESAPptaEELVqfcrERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
7921-8216 3.02e-21

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 98.28  E-value: 3.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7921 WVVDPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwlleGYPGHPGRQGRLYKTGDLVQYNADGNLVY 8000
Cdd:COG3433     23 AIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPF----IPVPYPAQPGRQADDLRLLLRRGLGPGGG 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8001 LGRkdsQVKVRGQRVELGEVEHHVRECLPEARQLAVEVilpsgqkNHAMLAVFVQLGKGTHIAHLEEKAggedsmaqvvf 8080
Cdd:COG3433     99 LER---LVQQVVIRAERGEEEELLLVLRAAAVVRVAVL-------AALRGAGVGLLLIVGAVAALDGLA----------- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8081 ltgTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLReiGASFTAQQLAETQTSSQGPKRQPLTEAEqtMQQLWAR 8160
Cdd:COG3433    158 ---AAAALAALDKVPPDVVAASAVVALDALLLLALKVVARA--APALAAAEALLAAASPAPALETALTEEE--LRADVAE 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 8161 VLGIDADIIGLDDSFFRLGGDSIAAMKLVGEARRTGLQLSVADIFRHPRLIDLASL 8216
Cdd:COG3433    231 LLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWAL 286
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
4531-5056 3.03e-21

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 102.65  E-value: 3.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4531 WNQDVPPAIE--------RCVHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLV-QLGVKPEDMVPLCFEKS 4601
Cdd:PRK08751     7 WLQSYPAGVAaeidleqfRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNC 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4602 MWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLASAQYAT--------------LWTSLG-------RSVV 4660
Cdd:PRK08751    87 LQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTtvqqviadtpvkqvITTGLGdmlgfpkAALV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4661 ---------IVSEASTSQ-------LPVVTKTADPSVN--PGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGI 4722
Cdd:PRK08751   167 nfvvkyvkkLVPEYRINGairfreaLALGRKHSMPTLQiePDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAG 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4723 TD------HTRVLQFASYTFDACIAEIITTLLCCGC---ICVPSD--------SDRRNNLAKAINAMdVNWALLTPSVAR 4785
Cdd:PRK08751   247 TGkleegcEVVITALPLYHIFALTANGLVFMKIGGCnhlISNPRDmpgfvkelKKTRFTAFTGVNTL-FNGLLNTPGFDQ 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4786 mLDpcvVQSLKILVLGGEQVNSADWDRWPK--SIQTINAYGPTECS--ICCTTYSGKQgfKSGTIGTSIVSVSWVVDpEN 4861
Cdd:PRK08751   326 -ID---FSSLKMTLGGGMAVQRSVAERWKQvtGLTLVEAYGLTETSpaACINPLTLKE--YNGSIGLPIPSTDACIK-DD 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4862 HNRLAPLGSIGELLVEGPILARGYLNDMEKTeAAFIDDPAWLlegygghsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQ 4941
Cdd:PRK08751   399 AGTVLAIGEIGELCIKGPQVMKGYWKRPEET-AKVMDADGWL---------------HTGDIARMDEQGFVYIVDRKKDM 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4942 VKLRGQRVELGEVEhhvreclteakqlavEVI--VPegegGYAMLAAfVQLGDdtyntlvkEKAGGdslTVQVVFLDRVE 5019
Cdd:PRK08751   463 ILVSGFNVYPNEIE---------------DVIamMP----GVLEVAA-VGVPD--------EKSGE---IVKVVIVKKDP 511
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 5020 EELAKRVPEHMM--LTTF-------FTLEaMPTTTSGKIDRKRLRE 5056
Cdd:PRK08751   512 ALTAEDVKAHARanLTGYkqpriieFRKE-LPKTNVGKILRRELRD 556
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
1955-2445 3.03e-21

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 101.42  E-value: 3.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL----DPDHPASRHEDifrqTGAQVV 2030
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLfsafGPEAIRDRLEN----SEAKVL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2031 VTSAQHSARwigtnhqvvtvsagsleqfstlvnpvdlpAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGv 2110
Cdd:cd05969     77 ITTEELYER-----------------------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLD- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2111 tnlLRALQFTAYTFDV-----CIAEIITTLVHGGCICVPSDSERRDNLAKAITDMQVNWGYLTSSVARLL---DPCLV-- 2180
Cdd:cd05969    127 ---LHPDDIYWCTADPgwvtgTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLmkeGDELArk 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2181 ---PSLKVLVLGGEQVN--STDWGKWPSSVQTINGYGPTEccvfcTGYTGI-----QGFQSGNIGTSIASV-SWVVDpeN 2249
Cdd:cd05969    204 ydlSSLRFIHSVGEPLNpeAIRWGMEVFGVPIHDTWWQTE-----TGSIMIanypcMPIKPGSMGKPLPGVkAAVVD--E 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2250 HGRLAPLGSIGELLVEG--PILARGYLNDVDKTQAAFIDdpawlleGYpghegrqgrlYKTGDLVRYSSDGNLVCLGRKD 2327
Cdd:cd05969    277 NGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFID-------GW----------YLTGDLAYRDEDGYFWFVGRAD 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2328 SQVKVRGQRVELGEVEhhmrkclpeanqlavevvppSGERDHAMLA--AFIRLDDETRNSplIIKyaednstAQIVFLTG 2405
Cdd:cd05969    340 DIIKTSGHRVGPFEVE--------------------SALMEHPAVAeaGVIGKPDPLRGE--IIK-------AFISLKEG 390
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2406 IE--EELSERL----PQHMVPTVFFALVHF----PTTTSGKTDRKRLREI 2445
Cdd:cd05969    391 FEpsDELKEEIinfvRQKLGAHVAPREIEFvdnlPKTRSGKIMRRVLKAK 440
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7630-8121 3.05e-21

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 100.83  E-value: 3.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7630 DGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVV 7709
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7710 ASAqysarwtssschvvtvskalssqlpavvdstntsvrpenaAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGIT 7789
Cdd:cd05934     81 VDP----------------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7790 NLSRVLQF--ASYTfDACIAEIITTLLCGG-CICVPSDSDRR--NSLAKAISTmdvnWAFLTPSVARLL-------DPGL 7857
Cdd:cd05934    121 EDDVYLTVlpLFHI-NAQAVSVLAALSVGAtLVLLPRFSASRfwSDVRRYGAT----VTNYLGAMLSYLlaqppspDDRA 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7858 IPSLKILAIGGEQSSSADW-NRWpgSVQKIHVYGPTECcIFCTGYTTKQGFEPSTIGTSVASVSW-VVDPenHNRLAPLG 7935
Cdd:cd05934    196 HRLRAAYGAPNPPELHEEFeERF--GVRLLEGYGMTET-IVGVIGPRDEPRRPGSIGRPAPGYEVrIVDD--DGQELPAG 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7936 SMGELLM---EGPILARGYLNDVDKTEAAFiddpawllegypghpgRQGrLYKTGDLVQYNADGNLVYLGRKDSQVKVRG 8012
Cdd:cd05934    271 EPGELVIrglRGWGFFKGYYNMPEATAEAM----------------RNG-WFHTGDLGYRDADGFFYFVDRKKDMIRRRG 333
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8013 QRVELGEVE-----HhvreclPEARQLAVeVILPSgqknhamlavfvqlgkgthiahleeKAGGEDSMAQVVFLTG---T 8084
Cdd:cd05934    334 ENISSAEVErailrH------PAVREAAV-VAVPD-------------------------EVGEDEVKAVVVLRPGetlD 381
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 8085 EEEL----AKRLPKHMVPTVFFALLHFPMTTSGKADRKRLR 8121
Cdd:cd05934    382 PEELfafcEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
861-1368 3.08e-21

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 101.86  E-value: 3.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  861 QARARPDASAVCAWDGELTYGELDELSSKLAAHLV-QLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPAS 939
Cdd:PRK06839    11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  940 RHEEIFKQIGAQVVLTSSQHAMLFASSERHQVTVSKVSTSQLPTVVNFAKSPVDPGN--TAYII-FTSGTTGIPKGVVLQ 1016
Cdd:PRK06839    91 ELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNesASFIIcYTSGTTGKPKGAVLT 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1017 HRAVTTSCLGHGEAFGYTDHarvlqfasytfDACIAEI------------ITTLLYGGCICVPSESDRRNNLaKAISTMD 1084
Cdd:PRK06839   171 QENMFWNALNNTFAIDLTMH-----------DRSIVLLplfhiggiglfaFPTLFAGGVIIVPRKFEPTKAL-SMIEKHK 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1085 VNCALLTPSV-ARLLEPS--AVPSLKRLvlqgeqvsfadwnRW------PGSVQTI-----------NGYGPTECSVCCN 1144
Cdd:PRK06839   239 VTVVMGVPTIhQALINCSkfETTNLQSV-------------RWfynggaPCPEELMrefidrgflfgQGFGMTETSPTVF 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1145 TYSgKQGF--KSGIIGTSVASLSWVVDAGNHNRLAPlGSIGELLVEGPILARGYLNDIDKTEAAFiddpawllegyegha 1222
Cdd:PRK06839   306 MLS-EEDArrKVGSIGKPVLFCDYELIDENKNKVEV-GEVGELLIRGPNVMKEYWNRPDATEETI--------------- 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1223 gRRGRLYkTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQLAVeVILPSgQKEHALLAAFIQLD 1302
Cdd:PRK06839   369 -QDGWLC-TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINK-LSDVYEVAV-VGRQH-VKWGEIPIAFIVKK 443
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 1303 KGnhNALFEEKasgedsmaqvvfltgVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDI 1368
Cdd:PRK06839   444 SS--SVLIEKD---------------VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
3464-3988 3.50e-21

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 103.85  E-value: 3.50e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3464 HDLFTEQAKARPHAPAICawD---GELTYGELDALSSKLAsHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP 3540
Cdd:PRK08633   618 AEAWIDTAKRNWSRLAVA--DstgGELSYGKALTGALALA-RLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVN 694
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3541 LDpdHPASrhEEIF----EQTGAQVVVASAQY----SARWTSSSC----HVV-------TVSK-------ALSSQLPA-- 3592
Cdd:PRK08633   695 LN--YTAS--EAALksaiEQAQIKTVITSRKFleklKNKGFDLELpenvKVIyledlkaKISKvdkltalLAARLLPArl 770
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3593 VVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHR-------AVAT-----------SCLGHGRAFGITnlsrvlqfasy 3654
Cdd:PRK08633   771 LKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHnilsnieQISDvfnlrnddvilSSLPFFHSFGLT----------- 839
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3655 tfdaciaeiITTL--LCGG--CICVPSDSDRRnSLAKAISTMDVNWAFLTPSVARL------LDPGLIPSLKILAIGGEq 3724
Cdd:PRK08633   840 ---------VTLWlpLLEGikVVYHPDPTDAL-GIAKLVAKHRATILLGTPTFLRLylrnkkLHPLMFASLRLVVAGAE- 908
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3725 sssadwnRWPGSV-----QKIHV-----YGPTECC---------IFCTGYTTKQGFEPSTIGTSVASVSW-VVDPENHNR 3784
Cdd:PRK08633   909 -------KLKPEVadafeEKFGIrilegYGATETSpvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVrIVDPETFEE 981
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3785 LAPlGSMGELLMEGPILARGYLNDVDKTEAAF--IDDPAWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQV 3862
Cdd:PRK08633   982 LPP-GEDGLILIGGPQVMKGYLGDPEKTAEVIkdIDGIGW---------------YVTGDKGHLDEDGFLTITDRYSRFA 1045
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3863 KVRGQRVELGEVEHHVRECLPEARQLAVEVILPSGQKdhamlaafvqleeGTQNALLDKEAGGEdsmaqvvfLASVEEEL 3942
Cdd:PRK08633  1046 KIGGEMVPLGAVEEELAKALGGEEVVFAVTAVPDEKK-------------GEKLVVLHTCGAED--------VEELKRAI 1104
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 3943 AK-RLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIgasftAQQLAE 3988
Cdd:PRK08633  1105 KEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL-----ALALLG 1146
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
5200-5384 4.26e-21

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 96.65  E-value: 4.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5200 SPLQEGLMSLTAKRAgDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSElGLLQVVVEE-KIQWT------ 5272
Cdd:COG4908      2 SPAQKRFLFLEPGSN-AYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDG-EPVQRIDPDaDLPLEvvdlsa 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5273 -----ESKRLEEYLREDKAVSMGLGDR-LARYALIKEPYDGGkrWFVWTIHHALYDGWSLPRILQAVKQIYSGAV----- 5341
Cdd:COG4908     80 lpepeREAELEELVAEEASRPFDLARGpLLRAALIRLGEDEH--VLLLTIHHIISDGWSLGILLRELAALYAALLegepp 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5342 --PERQPSFNAFI----QYLGQQDLEAATLYWQTALADCKAAL-FPTLPP 5384
Cdd:COG4908    158 plPELPIQYADYAawqrAWLQSEALEKQLEYWRQQLAGAPPVLeLPTDRP 207
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
2561-2750 5.21e-21

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 96.26  E-value: 5.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2561 LTPIQHLYLTLDPsGRSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFqRQTGGRWQQYIseHDSSSLIVNHIH 2640
Cdd:COG4908      1 LSPAQKRFLFLEP-GSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRF-VEEDGEPVQRI--DPDADLPLEVVD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2641 TRDT------TEIVEALRQSRG-SLDIERGPVL-AAVLCDAGERQSLFVAIHHLVVDLVSWRI----LLEELEDLLLGQT 2708
Cdd:COG4908     77 LSALpepereAELEELVAEEASrPFDLARGPLLrAALIRLGEDEHVLLLTIHHIISDGWSLGIllreLAALYAALLEGEP 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 2709 LP-PALSTPFQAWHAAQAKYieehvppsavAQVELDPDQLSYW 2750
Cdd:COG4908    157 PPlPELPIQYADYAAWQRAW----------LQSEALEKQLEYW 189
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
2072-2439 6.00e-21

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 98.49  E-value: 6.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2072 ENAAYVMFTSGSTGTPKGVVLEHRAVVTS---CLGHGQAFGVTNLLRALQFTAYTFDvcIAEIITTLVHGGCICVPSDSE 2148
Cdd:cd17635      1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVpdiLQKEGLNWVVGDVTYLPLPATHIGG--LWWILTCLIHGGLCVTGGENT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2149 RRDNLAKAITDMQVN--------WGYLTSSVARLLDPClvPSLKVLVLGGEQVNSTD--WGKWPSSVQTINGYGPTECCV 2218
Cdd:cd17635     79 TYKSLFKILTTNAVTttclvptlLSKLVSELKSANATV--PSLRLIGYGGSRAIAADvrFIEATGLTNTAQVYGLSETGT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2219 FCTGYTGIQGFQSGNIGTSIASVSWVVdPENHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpaWLlegypgh 2298
Cdd:cd17635    157 ALCLPTDDDSIEINAVGRPYPGVDVYL-AATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG--WV------- 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2299 egrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVPpsgerDHAMLAAFIRl 2378
Cdd:cd17635    227 --------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEG-VSGVQECACYEIS-----DEEFGELVGL- 291
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 2379 ddetrnspLIIKYAEDNSTAqivfLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDR 2439
Cdd:cd17635    292 --------AVVASAELDENA----IRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
5648-6137 6.16e-21

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 100.15  E-value: 6.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHpaSRHEDTF--RHTGAQVVVT 5725
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFF--REHELAFilRRAKAKVFVV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5726 SAqhsaRWIGTNHQvvtvsagslgqlstlvnpvglpAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITN 5805
Cdd:cd05903     80 PE----RFRQFDPA----------------------AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGP 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5806 LSRVLQFASYTFdacmdeiITTLMYGGCICV----PSDSDRRNDLVKAISTMD---VSCAL-LTPSVARLLE-----PSS 5872
Cdd:cd05903    134 GDVFLVASPMAH-------QTGFVYGFTLPLllgaPVVLQDIWDPDKALALMRehgVTFMMgATPFLTDLLNaveeaGEP 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5873 VPTLQMLVLQGEQVsfadwnrwPASV----QTING------YGPTEC-SICCNTYSGKQGFKSGIIGTSVASVSWVVDPE 5941
Cdd:cd05903    207 LSRLRTFVCGGATV--------PRSLarraAELLGakvcsaYGSTECpGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDD 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5942 NHDRLAPlGSIGELLVEGPILARGYLndiqktaavfiDDPAWLLEGYPGHpgrqgrLYKTGDLVRYDANGNLVCLGRKDS 6021
Cdd:cd05903    279 TGATLAP-GVEGELLSRGPSVFLGYL-----------DRPDLTADAAPEG------WFRTGDLARLDEDGYLRITGRSKD 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6022 QVKLRGQRVELGEVEhhvrECL---PEARQLAVeVILPS---GQKdhamLAAFVQLEEGtqnALLDKEASGEdsmaqvvF 6095
Cdd:cd05903    341 IIIRGGENIPVLEVE----DLLlghPGVIEAAV-VALPDerlGER----ACAVVVTKSG---ALLTFDELVA-------Y 401
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 6096 LASVeeELAK-RLPEHMVptvffSLLHFPTTTSGKTDRKRLRE 6137
Cdd:cd05903    402 LDRQ--GVAKqYWPERLV-----HVDDLPRTPSGKVQKFRLRE 437
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
3487-3977 6.54e-21

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 100.27  E-value: 6.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL----DPDHPASRheeiFEQTGAQVV 3562
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLfsafGPEAIRDR----LENSEAKVL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3563 VASAQYSARWTssschvvtvskalssqlpavvdstntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGhgrafgi 3642
Cdd:cd05969     77 ITTEELYERTD-----------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFT------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3643 tnlsrvlqfASYTFDA-------CIAE----------IITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFLTPSVAR 3705
Cdd:cd05969    121 ---------GKYVLDLhpddiywCTADpgwvtgtvygIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIR 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3706 LL-DPGLIP-------SLKILAIGGEqSSSADWNRWPGSVQK--IH-VYGPTECCIFCTGYTTKQGFEPSTIGTSVASVS 3774
Cdd:cd05969    192 MLmKEGDELarkydlsSLRFIHSVGE-PLNPEAIRWGMEVFGvpIHdTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVK 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3775 WVVDPENHNRLAPlGSMGELLMEG--PILARGYLNDVDKTEAAFIDdpawlleGYpghpgrqgrlYKTGDLVQYNADGNL 3852
Cdd:cd05969    271 AAVVDENGNELPP-GTKGILALKPgwPSMFRGIWNDEERYKNSFID-------GW----------YLTGDLAYRDEDGYF 332
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3853 VYLGRKDSQVKVRGQRVELGEVEhhvrECLPEARQLA-VEVIlpsGQKD---HAMLAAFVQLEEGTqnalldkEAGGEds 3928
Cdd:cd05969    333 WFVGRADDIIKTSGHRVGPFEVE----SALMEHPAVAeAGVI---GKPDplrGEIIKAFISLKEGF-------EPSDE-- 396
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 3929 maqvvflasVEEELAKRLPEHMVPTVFFSLLHF----PTTTSGKTDRKRLREI 3977
Cdd:cd05969    397 ---------LKEEIINFVRQKLGAHVAPREIEFvdnlPKTRSGKIMRRVLKAK 440
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
4545-5076 7.72e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 101.01  E-value: 7.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4545 DQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 4624
Cdd:PRK07786    21 NQLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFR 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4625 HPASRHEHIFRQTGAQVVLASAQYATLWTSL-----GRSVVIVSEASTSQLPV----VTKTADPSVNPGN-----AAYAI 4690
Cdd:PRK07786   101 LTPPEIAFLVSDCGAHVVVTEAALAPVATAVrdivpLLSTVVVAGGSSDDSVLgyedLLAEAGPAHAPVDipndsPALIM 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4691 FTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFD-ACIAEIITTLLCCGCICV-PSDSDRRNNLAKA 4768
Cdd:PRK07786   181 YTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHiAGIGSMLPGLLLGAPTVIyPLGAFDPGQLLDV 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4769 INAMDVNWALLTPsvARMLDPCVVQS-----LKILVLGGEQVNSAD------WDRWPKSiQTINAYGPTECSICCTTYSG 4837
Cdd:PRK07786   261 LEAEKVTGIFLVP--AQWQAVCAEQQarprdLALRVLSWGAAPASDtllrqmAATFPEA-QILAAFGQTEMSPVTCMLLG 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4838 KQGF-KSGTIGTSIVSVSWVVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAFidDPAWLlegyggHSgrqgr 4916
Cdd:PRK07786   338 EDAIrKLGSVGKVIPTVAARVVDENMNDVPV-GEVGEIVYRAPTLMSGYWNNPEATAEAF--AGGWF------HS----- 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4917 lyktGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHhvrecLTEAKQLAVEVIV---PEGEGGYAMLAafvqlgdd 4993
Cdd:PRK07786   404 ----GDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVEN-----VLASHPDIVEVAVigrADEKWGEVPVA-------- 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4994 tyntLVKEKAGGDSLTvqvvfLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREigaSFTAQQLAEMRTSS 5073
Cdd:PRK07786   467 ----VAAVRNDDAALT-----LEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE---RYGACVNVERRSAS 534

                   ...
gi 1820002560 5074 QGP 5076
Cdd:PRK07786   535 AGF 537
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
83-379 7.89e-21

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 97.13  E-value: 7.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   83 SWVVDPKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAWlleghGGYAGRQGRLYKTGDLVRYDADGNLv 162
Cdd:COG3433     23 AIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIP-----VPYPAQPGRQADDLRLLLRRGLGPG- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  163 clGRKDSQVKLRGQRVELGEVEHHVRECLPEAKQLAVEVVLPLGqknhatlAAFIQLDKGTHnallkekVGGDDSIArvv 242
Cdd:COG3433     97 --GGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRG-------AGVGLLLIVGA-------VAALDGLA--- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  243 flagVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASFTAQQLAEmrTSSQGPKRQPSTEAErtMQQLWA 322
Cdd:COG3433    158 ----AAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAA--ASPAPALETALTEEE--LRADVA 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  323 RVLGIEPDSIGLDDSFFRLGGDSIAAIKLVGEARRTGLQPSVADIFRHPTLAALASL 379
Cdd:COG3433    230 ELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWAL 286
PRK09274 PRK09274
peptide synthase; Provisional
4549-4949 8.48e-21

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 101.13  E-value: 8.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4549 EQARARPDTPAICAWDG----------ELTYGELDTLSSKLASHLVQLGVKPED----MVPLCFEksmwTVVAMLAVLKA 4614
Cdd:PRK09274    14 RAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMravlMVTPSLE----FFALTFALFKA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4615 GGAFVPLDPDHPASRHEHIFRQTGAQVVL--ASAQYATLWTSLG----RSVVIVSE------ASTSQLPVVTKTADPS-- 4680
Cdd:PRK09274    90 GAVPVLVDPGMGIKNLKQCLAEAQPDAFIgiPKAHLARRLFGWGkpsvRRLVTVGGrllwggTTLATLLRDGAAAPFPma 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4681 -VNPGNAAYAIFTSGSTGIPKGVVLEHK---AVVTSClghGQAFGITDHTRVLQ----FAsyTFDaciaeiittlLCCGC 4752
Cdd:PRK09274   170 dLAPDDMAAILFTSGSTGTPKGVVYTHGmfeAQIEAL---REDYGIEPGEIDLPtfplFA--LFG----------PALGM 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4753 ICV-----PS-----DSDRrnnLAKAIN-----AMDVNWALLTpsvaRMLDPCVVQ-----SLKILVLGGEQVNSADWDR 4812
Cdd:PRK09274   235 TSVipdmdPTrpatvDPAK---LFAAIErygvtNLFGSPALLE----RLGRYGEANgiklpSLRRVISAGAPVPIAVIER 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4813 W----PKSIQTINAYGPTE----CSI------CCTTYSGKQGFksGT-IGTSIVSVSWVV-----DPENH---NRLAPLG 4869
Cdd:PRK09274   308 FramlPPDAEILTPYGATEalpiSSIesreilFATRAATDNGA--GIcVGRPVDGVEVRIiaisdAPIPEwddALRLATG 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4870 SIGELLVEGPILARGYLNDMEKTEAAFIDDPAwllegyGGHSGRqgrlykTGDLVRYDADGNLVYLGRKDSQVKLRGQRV 4949
Cdd:PRK09274   386 EIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQ------GDVWHR------MGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1919-2444 9.15e-21

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 101.11  E-value: 9.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1919 WNQEVPPAIE--------RCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLV-QLGVNPEDVVPLCFEKS 1989
Cdd:PRK08751     7 WLQSYPAGVAaeidleqfRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNC 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1990 MWTVVAMLAVLKAGGAFVPLDPDHPAS--RHEDIFRQTGAQVVVTSAQHSARWIGTN---HQVVTVSAGSLEQF--STLV 2062
Cdd:PRK08751    87 LQYPIATFGVLRAGLTVVNVNPLYTPRelKHQLIDSGASVLVVIDNFGTTVQQVIADtpvKQVITTGLGDMLGFpkAALV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2063 NPV-----------------------------DLPA---KPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGV 2110
Cdd:PRK08751   167 NFVvkyvkklvpeyringairfrealalgrkhSMPTlqiEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAG 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2111 TNLLRALQ---FTAYTFDVCIAEIITTLVH---GGC---ICVPSD-----SERRDNLAKAITDMQVNWGYLTSSVArlLD 2176
Cdd:PRK08751   247 TGKLEEGCevvITALPLYHIFALTANGLVFmkiGGCnhlISNPRDmpgfvKELKKTRFTAFTGVNTLFNGLLNTPG--FD 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2177 PCLVPSLKVLVLGGEQVNSTDWGKWP--SSVQTINGYGPTECC-VFCTGYTGIQGFqSGNIGTSIASVSWVVDpENHGRL 2253
Cdd:PRK08751   325 QIDFSSLKMTLGGGMAVQRSVAERWKqvTGLTLVEAYGLTETSpAACINPLTLKEY-NGSIGLPIPSTDACIK-DDAGTV 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2254 APLGSIGELLVEGPILARGYLNDVDKTqAAFIDDPAWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVR 2333
Cdd:PRK08751   403 LAIGEIGELCIKGPQVMKGYWKRPEET-AKVMDADGWL---------------HTGDIARMDEQGFVYIVDRKKDMILVS 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2334 GQRVELGEVEHHMrKCLPEANQLAVEVVPpsGERDHAMLAAFIRLDDETRNSPLIIKYAEDNstaqivfLTGIEEelser 2413
Cdd:PRK08751   467 GFNVYPNEIEDVI-AMMPGVLEVAAVGVP--DEKSGEIVKVVIVKKDPALTAEDVKAHARAN-------LTGYKQ----- 531
                          570       580       590
                   ....*....|....*....|....*....|.
gi 1820002560 2414 lpqhmvPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:PRK08751   532 ------PRIIEFRKELPKTNVGKILRRELRD 556
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
844-1367 9.41e-21

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 100.87  E-value: 9.41e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  844 ADMPPAVDRCIHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVL 923
Cdd:PRK07059    15 AEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  924 KAGGAFVPLDPGHPASRHEEIFKQIGAQ--VVLTSSQH---AMLFASSERHQVT--------------------VSK-VS 977
Cdd:PRK07059    95 RAGYVVVNVNPLYTPRELEHQLKDSGAEaiVVLENFATtvqQVLAKTAVKHVVVasmgdllgfkghivnfvvrrVKKmVP 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  978 TSQLPTVVNF------------AKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLG----HGEAFGYTDHARVLQ 1041
Cdd:PRK07059   175 AWSLPGHVRFndalaegarqtfKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQmeawLQPAFEKKPRPDQLN 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1042 FAS----YTFDACIAEIITTLLYGGC-ICVPSESDRRnNLAKAISTMDVNC---------ALL-TPSVARLlepsavpSL 1106
Cdd:PRK07059   255 FVCalplYHIFALTVCGLLGMRTGGRnILIPNPRDIP-GFIKELKKYQVHIfpavntlynALLnNPDFDKL-------DF 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1107 KRLVLQ---GEQVSFADWNRWPGSVQT--INGYGPTECS--VCCNTYSGKQgFkSGIIGTSVAS--LSWVVDAGNHnrlA 1177
Cdd:PRK07059   327 SKLIVAnggGMAVQRPVAERWLEMTGCpiTEGYGLSETSpvATCNPVDATE-F-SGTIGLPLPSteVSIRDDDGND---L 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1178 PLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpawlleGYeghagrrgrlYKTGDLVRCDADGNLVCLGRKDSQVKVRG 1257
Cdd:PRK07059   402 PLGEPGEICIRGPQVMAGYWNRPDETAKVMTAD------GF----------FRTGDVGVMDERGYTKIVDRKKDMILVSG 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1258 QRVELGEIEHHVREClPEARQLAVeVILPSgqkEHallaafiqldkgnhnalfeekaSGEDSMAQVV----FLTgvEEEL 1333
Cdd:PRK07059   466 FNVYPNEIEEVVASH-PGVLEVAA-VGVPD---EH----------------------SGEAVKLFVVkkdpALT--EEDV 516
                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1820002560 1334 ----AKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:PRK07059   517 kafcKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
PRK07787 PRK07787
acyl-CoA synthetase; Validated
3471-3875 1.10e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 100.06  E-value: 1.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLAShlvqlGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 3550
Cdd:PRK07787    10 AAAADIADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAER 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3551 EEIFEQTGAQVVVASAQysarWTSSSCHVVTVSkalssqLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVA 3630
Cdd:PRK07787    85 RHILADSGAQAWLGPAP----DDPAGLPHVPVR------LHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3631 TS--------------CLGHGRA-FGITNL-----------SRVLQFASYTFDACIAEIIT--TLLCGgcicVPSDSDR- 3681
Cdd:PRK07787   155 ADldalaeawqwtaddVLVHGLPlFHVHGLvlgvlgplrigNRFVHTGRPTPEAYAQALSEggTLYFG----VPTVWSRi 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3682 --RNSLAKAISTmdvnwafltpsvARLLDPGLIP-----SLKILAIGGEQSssadwnrwpgsvqkIHVYGPTECCIFCtg 3754
Cdd:PRK07787   231 aaDPEAARALRG------------ARLLVSGSAAlpvpvFDRLAALTGHRP--------------VERYGMTETLITL-- 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3755 yTTKQGFE--PSTIGTSVASVSWVVDPENHNRLAPLG-SMGELLMEGPILARGYLNDVDKTEAAFIDDpAWllegypghp 3831
Cdd:PRK07787   283 -STRADGErrPGWVGLPLAGVETRLVDEDGGPVPHDGeTVGELQVRGPTLFDGYLNRPDATAAAFTAD-GW--------- 351
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 3832 grqgrlYKTGDLVQYNADGNLVYLGRKDSQ-VKVRGQRVELGEVE 3875
Cdd:PRK07787   352 ------FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIE 390
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
5624-6138 1.20e-20

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 101.03  E-value: 1.20e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5624 VHDLFTEQAKARPHAPAIcAWDGE------LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGG 5697
Cdd:cd05968     63 VEQLLDKWLADTRTRPAL-RWEGEdgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5698 AFVPL----DPDHPASRHEDT----------FRHTGAQVVVT-SAQHSARWIGTNHQVVTVSAGSLGQLSTLVNPVGLPA 5762
Cdd:cd05968    142 IVVPIfsgfGKEAAATRLQDAeakalitadgFTRRGREVNLKeEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDE 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5763 I------------PENAVYIMFTSGSTGIPKGVVLEHRAV-VTSCWGRGRAFGITNLSRV-------------LQFASYT 5816
Cdd:cd05968    222 EketagdgaerteSEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLtwftdlgwmmgpwLIFGGLI 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5817 FDAcmdeiiTTLMYGGCICVPsDSDRRNDLVKAistMDVSCALLTPSVARLLEP--------SSVPTLQMLVLQGEQVSF 5888
Cdd:cd05968    302 LGA------TMVLYDGAPDHP-KADRLWRMVED---HEITHLGLSPTLIRALKPrgdapvnaHDLSSLRVLGSTGEPWNP 371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5889 ADWNRWPASVqtingyGPTECSICcnTYSGKQGFKSGIIG-------------TSVASVSWVVDPENHDRLAPlgSIGEL 5955
Cdd:cd05968    372 EPWNWLFETV------GKGRNPII--NYSGGTEISGGILGnvlikpikpssfnGPVPGMKADVLDESGKPARP--EVGEL 441
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5956 LVEGPI--LARGylndiqktaavFIDDPAWLLEGYpghPGRQGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELG 6033
Cdd:cd05968    442 VLLAPWpgMTRG-----------FWRDEDRYLETY---WSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPA 507
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6034 EVE------HHVREClpearqLAVEVILP-SGQKDHamlaAFVQLEEGtqnalldkeasgedsmaqVVFLASVEEELAKR 6106
Cdd:cd05968    508 EIEsvlnahPAVLES------AAIGVPHPvKGEAIV----CFVVLKPG------------------VTPTEALAEELMER 559
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1820002560 6107 LPEHM----VPTVFFSLLHFPTTTSGKTDRKRLREI 6138
Cdd:cd05968    560 VADELgkplSPERILFVKDLPKTRNAKVMRRVIRAA 595
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
8260-8649 1.39e-20

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 99.33  E-value: 1.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8260 DVVPASYIQQFYIATGVRAPR-EAFNYPF-IDLSDAVDIQVLQASCSALLEHFPILRTHFVY-FQGKLYQVIprHQDLPF 8336
Cdd:pfam00668    3 DEYPLSPAQKRMWFLEKLEPHsSAYNMPAvLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVI--LEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8337 SIFEVNGALAEESQAIHIRDL----DQTSPLGLPTS----FTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQ 8408
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAfiqrDLQSPFDLEKGplfrAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8409 E------PLLSTTGFHSY-------LAYVHNQRSASinYWSRLLKGSHITNITSKLRPKLGKDT--------TIRSVKVE 8467
Cdd:pfam00668  161 LlkgeplPLPPKTPYKDYaewlqqyLQSEDYQKDAA--YWLEQLEGELPVLQLPKDYARPADRSfkgdrlsfTLDEDTEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8468 RVIRTPQLpTGLTMASLVSSAWAVVLSHISGEEDVVYGLVVAGRNSD------------LPSITEVS-----------VQ 8524
Cdd:pfam00668  239 LLRKLAKA-HGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPdiermvgmfvntLPLRIDPKggktfselikrVQ 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8525 DQYISLGESDSIGLDDIVQHCTDWPAKSE---FDSIIQHQNIEEQPEI----QFAGETTKLQWFKN---SFAVSRQLFvf 8594
Cdd:pfam00668  318 EDLLSAEPHQGYPFGDLVNDLRLPRDLSRhplFDPMFSFQNYLGQDSQeeefQLSELDLSVSSVIEeeaKYDLSLTAS-- 395
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 8595 shPRGNSLTITITGNTGILTDQCAEKLLVMLCDTISQLSDSLDTPLAACKLLLPT 8649
Cdd:pfam00668  396 --ERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDA 448
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
51-284 1.44e-20

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 99.56  E-value: 1.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   51 GYGPTECCIVCTGYTSEQDFTTGTIGTSIASVSW-VVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINnp 129
Cdd:cd05936    273 GYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVkIVD--DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVD-- 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  130 AWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECL---PEAKQLAVeVVLPLG 206
Cdd:cd05936    349 GWL---------------RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVE----EVLyehPAVAEAAV-VGVPDP 408
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560  207 QKNHATlAAFIQLDKGtHNALLKEkvggddsiarvvflagVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLR 284
Cdd:cd05936    409 YSGEAV-KAFVVLKEG-ASLTEEE----------------IIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
5648-6136 1.45e-20

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 98.95  E-value: 1.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSA 5727
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5728 qhsarwigtnhqvvtvsagslgqlstlvnpvglpaipENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGrgrAFGITNLS 5807
Cdd:cd05972     81 -------------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPT---AAYWLGLR 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5808 RV-----------LQFASYTFDACMDEIITTLMYGGcicVPSDSDRRNDLVK--AISTMdvsCAllTPSVARLL---EPS 5871
Cdd:cd05972    121 PDdihwniadpgwAKGAWSSFFGPWLLGATVFVYEG---PRFDAERILELLEryGVTSF---CG--PPTAYRMLikqDLS 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5872 S--VPTLQMLVLQGEQVSFADWNRWPASVQ-TI-NGYGPTECSICCNTYSGkQGFKSGIIGTSVASVSWVVDPENHDRLA 5947
Cdd:cd05972    193 SykFSHLRLVVSAGEPLNPEVIEWWRAATGlPIrDGYGQTETGLTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELP 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5948 PlGSIGELLVE-GPI-LARGYLNDIQKTAAVFIDDpaWllegypghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKL 6025
Cdd:cd05972    272 P-GEEGDIAIKlPPPgLFLGYVGDPEKTEASIRGD--Y---------------YLTGDRAYRDEDGYFWFVGRADDIIKS 333
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6026 RGQRVELGEVEHHVREcLPEARQLAVeVILPS---GQkdhaMLAAFVQLEEGtqnalldkeASGEDSMAqvvflasveEE 6102
Cdd:cd05972    334 SGYRIGPFEVESALLE-HPAVAEAAV-VGSPDpvrGE----VVKAFVVLTSG---------YEPSEELA---------EE 389
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 6103 LA----KRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:cd05972    390 LQghvkKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
854-1368 1.70e-20

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 101.54  E-value: 1.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCawD---GELTYGELdeLSSKLA-AHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAF 929
Cdd:PRK08633   617 LAEAWIDTAKRNWSRLAVA--DstgGELSYGKA--LTGALAlARLLKRELKDEENVGILLPPSVAGALANLALLLAGKVP 692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  930 VPLDpgHPASrhEEIFK----QIGAQVVLTS-------SQHAMLFASSERHQVT-----VSKVSTSQ----------LPT 983
Cdd:PRK08633   693 VNLN--YTAS--EAALKsaieQAQIKTVITSrkfleklKNKGFDLELPENVKVIyledlKAKISKVDkltallaarlLPA 768
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  984 --VVNFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQ----FASYTFdaciaeIITT 1057
Cdd:PRK08633   769 rlLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGL------TVTL 842
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1058 ---LLYG-GCICVPSESDRRNnLAKAISTMDVNCALLTPSVARL------LEPSAVPSLkRLVLQG-----EQVSFADWN 1122
Cdd:PRK08633   843 wlpLLEGiKVVYHPDPTDALG-IAKLVAKHRATILLGTPTFLRLylrnkkLHPLMFASL-RLVVAGaeklkPEVADAFEE 920
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1123 RWpgSVQTINGYGPTECS--VCCNT-------YSGKQGFKSG-----IIGTSVAslswVVDAGNHNRLAPlGSIGELLVE 1188
Cdd:PRK08633   921 KF--GIRILEGYGATETSpvASVNLpdvlaadFKRQTGSKEGsvgmpLPGVAVR----IVDPETFEELPP-GEDGLILIG 993
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1189 GPILARGYLNDIDKTEAAF--IDDPAWllegyeghagrrgrlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIE 1266
Cdd:PRK08633   994 GPQVMKGYLGDPEKTAEVIkdIDGIGW---------------YVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVE 1058
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1267 HHVRECLPEARQLAVEVILPSGQKEHALLaafiqldkgnhnALFEEKASGEDsmaqvvfltGVEEELAK-RLPEHMVPTI 1345
Cdd:PRK08633  1059 EELAKALGGEEVVFAVTAVPDEKKGEKLV------------VLHTCGAEDVE---------ELKRAIKEsGLPNLWKPSR 1117
                          570       580
                   ....*....|....*....|...
gi 1820002560 1346 LFTVKAMPITTSGKIDRKRLQDI 1368
Cdd:PRK08633  1118 YFKVEALPLLGSGKLDLKGLKEL 1140
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
1955-2443 1.82e-20

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 98.56  E-value: 1.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSA 2034
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2035 qhsarwigtnhqvvtvsagsleqfstlvnpvdlpakpENAAYVMFTSGSTGTPKGVVLEHRAVvtscLGHGQ-AFGVTNL 2113
Cdd:cd05972     81 -------------------------------------EDPALIYFTSGTTGLPKGVLHTHSYP----LGHIPtAAYWLGL 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2114 LRAlqftaytfDV--CIAE----------IITTLVHGgcICVPSDSERR---DNLAKAITDMQVNWGYLTSSVARLLDPC 2178
Cdd:cd05972    120 RPD--------DIhwNIADpgwakgawssFFGPWLLG--ATVFVYEGPRfdaERILELLERYGVTSFCGPPTAYRMLIKQ 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2179 LVPS-----LKVLVLGGEQVN--STDWGKWPSSVQTINGYGPTECCVFCTGYTGIQgFQSGNIGTSIAS-VSWVVDPEnh 2250
Cdd:cd05972    190 DLSSykfshLRLVVSAGEPLNpeVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMP-VKPGSMGRPTPGyDVAIIDDD-- 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2251 GRLAPLGSIGELLVE-GPI-LARGYLNDVDKTQAAFIDDpaWllegypghegrqgrlYKTGDLVRYSSDGNLVCLGRKDS 2328
Cdd:cd05972    267 GRELPPGEEGDIAIKlPPPgLFLGYVGDPEKTEASIRGD--Y---------------YLTGDRAYRDEDGYFWFVGRADD 329
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2329 QVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVPpsgerdhamlaafirldDETRNSplIIKyaednstAQIVFLTGIE- 2407
Cdd:cd05972    330 IIKSSGYRIGPFEVESALLE-HPAVAEAAVVGSP-----------------DPVRGE--VVK-------AFVVLTSGYEp 382
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 2408 -EELSERLPQHM--------VPTVFFALVHFPTTTSGKTDRKRLR 2443
Cdd:cd05972    383 sEELAEELQGHVkkvlapykYPREIEFVEELPKTISGKIRRVELR 427
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
1955-2444 2.04e-20

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 98.61  E-value: 2.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPdhpasrhedIFRQTGAQVVVTSA 2034
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILP---------FFREHELAFILRRA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2035 QhsARwigtnhqvVTVSAGSLEQFstlvNPVDLPAKPenaAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLL 2114
Cdd:cd05903     73 K--AK--------VFVVPERFRQF----DPAAMPDAV---ALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2115 RAL------QFTAYTFDVCIAEIITTLVHggcicVPSDSERRDNLAKAITDMQVNWGYLTSSVARLLD-----PCLVPSL 2183
Cdd:cd05903    136 VFLvaspmaHQTGFVYGFTLPLLLGAPVV-----LQDIWDPDKALALMREHGVTFMMGATPFLTDLLNaveeaGEPLSRL 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2184 KVLVLGGEQVNstdwGKWPSSVQTING------YGPTECCVFCTGYT-GIQGFQSGNIGTSIASVSWVVDPENHGRLAPl 2256
Cdd:cd05903    211 RTFVCGGATVP----RSLARRAAELLGakvcsaYGSTECPGAVTSITpAPEDRRLYTDGRPLPGVEIKVVDDTGATLAP- 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2257 GSIGELLVEGPILARGYLNDVDKTQAAFIDdpAWllegypghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQR 2336
Cdd:cd05903    286 GVEGELLSRGPSVFLGYLDRPDLTADAAPE--GW---------------FRTGDLARLDEDGYLRITGRSKDIIIRGGEN 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2337 VELGEVEHHMRKcLPEANQLAVEVVPPS--GERdhamLAAFIRLDDetrnspliikyaednsTAQIVFLTGIEEELSERL 2414
Cdd:cd05903    349 IPVLEVEDLLLG-HPGVIEAAVVALPDErlGER----ACAVVVTKS----------------GALLTFDELVAYLDRQGV 407
                          490       500       510
                   ....*....|....*....|....*....|
gi 1820002560 2415 PQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:cd05903    408 AKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
5648-6138 2.37e-20

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 99.66  E-value: 2.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH---PASRHEDTFRHT----GA 5720
Cdd:cd05906     40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPtydEPNARLRKLRHIwqllGS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5721 QVVVTSAQHSARWIG----TNHQVVTVSAGSLgQLSTLVNPVGLPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWG 5796
Cdd:cd05906    120 PVVLTDAELVAEFAGletlSGLPGIRVLSIEE-LLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5797 RGRAFGITNLSRVLQFASytfdacMDEIITTLMYG------GC--ICVPSDSDRRNDL--VKAISTMDVS--------CA 5858
Cdd:cd05906    199 KIQHNGLTPQDVFLNWVP------LDHVGGLVELHlravylGCqqVHVPTEEILADPLrwLDLIDRYRVTitwapnfaFA 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5859 LLTPSVARLLEPS-SVPTLQMLVLQGEQVSFADWNRW-----PASVQT---INGYGPTE-CSICcnTYSgkQGFKSGIIG 5928
Cdd:cd05906    273 LLNDLLEEIEDGTwDLSSLRYLVNAGEAVVAKTIRRLlrllePYGLPPdaiRPAFGMTEtCSGV--IYS--RSFPTYDHS 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5929 TSVASVSW----------VVDPENhdRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpAWllegypghpgrqgrl 5998
Cdd:cd05906    349 QALEFVSLgrpipgvsmrIVDDEG--QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED-GW--------------- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5999 YKTGDLVrYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQ---LAVEVILPSGQKDHamLAAFVQLEEGT 6075
Cdd:cd05906    411 FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEE-VPGVEPsftAAFAVRDPGAETEE--LAIFFVPEYDL 486
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 6076 QNALLDKEASGEDSMAQVVFLAsveeelakrlPEHMVPtvffsLLH--FPTTTSGKTDRKRLREI 6138
Cdd:cd05906    487 QDALSETLRAIRSVVSREVGVS----------PAYLIP-----LPKeeIPKTSLGKIQRSKLKAA 536
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
854-1363 2.67e-20

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 99.19  E-value: 2.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGE--LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVP 931
Cdd:PRK05852    18 IADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  932 LDPGHPASRHEEIFKQIGAQVVLTSS----QHAMLFASSERHQVTVSKVSTSQL------------PTVVNFAKSPVDPg 995
Cdd:PRK05852    98 LDPALPIAEQRVRSQAAGARVVLIDAdgphDRAEPTTRWWPLTVNVGGDSGPSGgtlsvhldaatePTPATSTPEGLRP- 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  996 NTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDH-ARVLQFASYTFDACIAEIITTLLYGGCICVPSesdrRN 1074
Cdd:PRK05852   177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRdATVAVMPLYHGHGLIAALLATLASGGAVLLPA----RG 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1075 NLAKAISTMDVNCALLTPSvarllepSAVPSLKRLVLQGEQVSFADWNR----------WPGSVQT------------IN 1132
Cdd:PRK05852   253 RFSAHTFWDDIKAVGATWY-------TAVPTIHQILLERAATEPSGRKPaalrfirscsAPLTAETaqalqtefaapvVC 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1133 GYGPTECS-------VCCNTYSGKQGFKSGIIGTSVASLSWVVDAGNHNrlAPLGSIGELLVEGPILARGYLNDIDKTEA 1205
Cdd:PRK05852   326 AFGMTEAThqvtttqIEGIGQTENPVVSTGLVGRSTGAQIRIVGSDGLP--LPAGAVGEVWLRGTTVVRGYLGDPTITAA 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1206 AFIDdpAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVElgeiehhvreclPEarqlAVEVIL 1285
Cdd:PRK05852   404 NFTD--GWL---------------RTGDLGSLSAAGDLSIRGRIKELINRGGEKIS------------PE----RVEGVL 450
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1286 PSgqkEHALLAAFIqldKGNHNALFeekasGEDSMAQVVFLTGVE---EELA----KRLPEHMVPTILFTVKAMPITTSG 1358
Cdd:PRK05852   451 AS---HPNVMEAAV---FGVPDQLY-----GEAVAAVIVPRESAPptaEELVqfcrERLAAFEIPASFQEASGLPHTAKG 519

                   ....*
gi 1820002560 1359 KIDRK 1363
Cdd:PRK05852   520 SLDRR 524
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
428-611 2.89e-20

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 93.95  E-value: 2.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  428 SPLQEGLMSLTTKRAgDYIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSElGLLQVVVEE-KMQWT------ 500
Cdd:COG4908      2 SPAQKRFLFLEPGSN-AYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDG-EPVQRIDPDaDLPLEvvdlsa 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  501 -----ESESLEEYLNEDKAASMGLGDR-LARYALIKESCGGKRwFVWTIHHALYDGWSLPLVLDAVKQVYSGAALERQPS 574
Cdd:COG4908     80 lpepeREAELEELVAEEASRPFDLARGpLLRAALIRLGEDEHV-LLLTIHHIISDGWSLGILLRELAALYAALLEGEPPP 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560  575 F----NTFIQYVSQQ-------DVKAAAAYWQTALADCEAVLfpPLPS 611
Cdd:COG4908    159 LpelpIQYADYAAWQrawlqseALEKQLEYWRQQLAGAPPVL--ELPT 204
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
4550-5057 3.11e-20

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 98.50  E-value: 3.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4550 QARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpDHPASR 4629
Cdd:PRK03640    11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLL--NTRLSR 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4630 HEHIFR--QTGAQVVLASAQYATLWTSLGRsvVIVSEASTSQLPVVTKTADPSVNpgNAAYAIFTSGSTGIPKGVVLEHK 4707
Cdd:PRK03640    89 EELLWQldDAEVKCLITDDDFEAKLIPGIS--VKFAELMNGPKEEAEIQEEFDLD--EVATIMYTSGTTGKPKGVIQTYG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4708 AVVTSCLGHGQAFGITDHTRVLQ----FASYTFDACIAEII---TTLLccgcicVPS-DSDRRNNLAK--AINAMDVNWA 4777
Cdd:PRK03640   165 NHWWSAVGSALNLGLTEDDCWLAavpiFHISGLSILMRSVIygmRVVL------VEKfDAEKINKLLQtgGVTIISVVST 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4778 LLTPSVARMLDPCVVQSLKILVLGG--------EQVNSadwdrwpKSIQTINAYGPTE-CSICCT---TYSGKqgfKSGT 4845
Cdd:PRK03640   239 MLQRLLERLGEGTYPSSFRCMLLGGgpapkpllEQCKE-------KGIPVYQSYGMTEtASQIVTlspEDALT---KLGS 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4846 IGTSIVSVSwvVDPENHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDdpAWLlegygghsgrqgrlyKTGDLVR 4925
Cdd:PRK03640   309 AGKPLFPCE--LKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD--GWF---------------KTGDIGY 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4926 YDADGNLVYLGRKDSQVKLRGQRVELGEVEH------HVREclteakqlAVEVIVPEGEGGyAMLAAFVQLGddtyntlv 4999
Cdd:PRK03640   370 LDEEGFLYVLDRRSDLIISGGENIYPAEIEEvllshpGVAE--------AGVVGVPDDKWG-QVPVAFVVKS-------- 432
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 5000 kEKAGGDSLTvqvvflDRVEEELAK-RVPEHmmlttFFTLEAMPTTTSGKIDRKRLREI 5057
Cdd:PRK03640   433 -GEVTEEELR------HFCEEKLAKyKVPKR-----FYFVEELPRNASGKLLRHELKQL 479
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
4509-5049 3.75e-20

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 99.19  E-value: 3.75e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4509 GEEKKVAGIETTTTGDRQQLWA----WNQDVPPAIERCVHDQFAEQARARPDTPAICaWDGE-------LTYGELDTLSS 4577
Cdd:cd17634     17 GEAGKILDWITPYQKVKNTSFApgapSIKWFEDATLNLAANALDRHLRENGDRTAII-YEGDdtsqsrtISYRELHREVC 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4578 KLASHLVQLGVKPED----MVPLCFEksmwTVVAMLAVLKAGGAFVPL----DPDHPASRhehIFRQTGAQVVLASAQYA 4649
Cdd:cd17634     96 RFAGTLLDLGVKKGDrvaiYMPMIPE----AAVAMLACARIGAVHSVIfggfAPEAVAGR---IIDSSSRLLITADGGVR 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4650 TlwtslGRSV---VIVSEASTSQLP------VVTKTADP-------------------------SVNPGNAAYAIFTSGS 4695
Cdd:cd17634    169 A-----GRSVplkKNVDDALNPNVTsvehviVLKRTGSDidwqegrdlwwrdliakaspehqpeAMNAEDPLFILYTSGT 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4696 TGIPKGVVLEHK----AVVTSC-----LGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPsDSDRrnnLA 4766
Cdd:cd17634    244 TGKPKGVLHTTGgylvYAATTMkyvfdYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWP-TPAR---MW 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4767 KAINAMDVNWALLTPSVARML---DPCVVQ-----SLKILVLGGEQVNSADWDRWPKSIQ-----TINAYGPTECS-ICC 4832
Cdd:cd17634    320 QVVDKHGVNILYTAPTAIRALmaaGDDAIEgtdrsSLRILGSVGEPINPEAYEWYWKKIGkekcpVVDTWWQTETGgFMI 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4833 TTYSGKQGFKSGTIGTSIVSVS-WVVDPENHNrlAPLGSIGELLVEGPI--LARGYLNDMEKTEAAFIDDpawlLEGYgg 4909
Cdd:cd17634    400 TPLPGAIELKAGSATRPVFGVQpAVVDNEGHP--QPGGTEGNLVITDPWpgQTRTLFGDHERFEQTYFST----FKGM-- 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4910 hsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEH------HVRECLTEAKQLAVEVIVPEgegGYAM 4983
Cdd:cd17634    472 --------YFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESvlvahpKVAEAAVVGIPHAIKGQAPY---AYVV 540
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 4984 LAAFVQLGDDTYNTLVkekaggdsltvqvvflDRVEEEL-AKRVPEHMMLTtfftlEAMPTTTSGKI 5049
Cdd:cd17634    541 LNHGVEPSPELYAELR----------------NWVRKEIgPLATPDVVHWV-----DSLPKTRSGKI 586
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
7607-8036 4.15e-20

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 98.35  E-value: 4.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7607 RCVHDLFAEQARARPGAPAICAWDG--ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAF 7684
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7685 VPLDPDHPASRHEEIFE---------QTGAQVVVASAQYSARWTSSSCHVVTVSKALSSQLPAvvdstNTSVRPENAAYI 7755
Cdd:cd05923     81 ALINPRLKAAELAELIErgemtaaviAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIE-----DPPREPEQPAFV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7756 IFTSGSTGVPKGVVLEHRAVATSCL-----------GHGRAFGITNLSRVLQFasytfdacIAEIITTLLCGGCICVPSD 7824
Cdd:cd05923    156 FYTSGTTGLPKGAVIPQRAAESRVLfmstqaglrhgRHNVVLGLMPLYHVIGF--------FAVLVAALALDGTYVVVEE 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7825 SDRRNSLaKAISTMDVNWAFLTPS------VARLLDPGLIPSLKILAIGGEQSSSADWNR----WPGsvQKIHVYGPTEC 7894
Cdd:cd05923    228 FDPADAL-KLIEQERVTSLFATPThldalaAAAEFAGLKLSSLRHVTFAGATMPDAVLERvnqhLPG--EKVNIYGTTEA 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7895 CIFC------TGYTTKQGFEpstigtsvASVSWVVDPENHNRLAPLGSMGELLMEGPILA--RGYLNDVDKTEAAFIDdp 7966
Cdd:cd05923    305 MNSLymrdarTGTEMRPGFF--------SEVRIVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-- 374
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 7967 awllegypghpgrqgRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvrECL---PEARQLAV 8036
Cdd:cd05923    375 ---------------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIE----RVLsrhPGVTEVVV 428
PRK06164 PRK06164
acyl-CoA synthetase; Validated
7611-8133 4.43e-20

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 98.66  E-value: 4.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVV----PLCFEksmWtVVAMLAVLKAGGAFVP 7686
Cdd:PRK06164    14 SLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVavwlPNCIE---W-VVLFLACARLGATVIA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7687 LDPDHPASRHEEIFEQTGAQVVV--------------ASAQYSARWTSSSCHVVTVS-------------KALSSQLPAV 7739
Cdd:PRK06164    90 VNTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailAAVPPDALPPLRAIAVVDDAadatpapapgarvQLFALPDPAP 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7740 VDSTNTSVRPENAAYIIFT-SGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGG- 7817
Cdd:PRK06164   170 PAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAp 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7818 CICVPS-DSDRRnslAKAISTMDVNWAFLTPSV-ARLLD----PGLIPSLKILAIGGEQSSSAD---WNRWPGSVQKiHV 7888
Cdd:PRK06164   250 LVCEPVfDAART---ARALRRHRVTHTFGNDEMlRRILDtageRADFPSARLFGFASFAPALGElaaLARARGVPLT-GL 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7889 YGPTECCIFCTGYTTKQGFEPSTIGTSV-----ASVSwVVDPENhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFI 7963
Cdd:PRK06164   326 YGSSEVQALVALQPATDPVSVRIEGGGRpaspeARVR-ARDPQD-GALLPDGESGEIEIRAPSLMRGYLDNPDATARALT 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7964 DDpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVEVILPSG 8043
Cdd:PRK06164   404 DD------GY----------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL-PGVAAAQVVGATRDG 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8044 QknhAMLAVFVQLGKGThiahleeKAGGEDSMAQvvfltgteeeLAKRLPKHMVPTVFFALLHFPMTTSG---KADRKRL 8120
Cdd:PRK06164   467 K---TVPVAFVIPTDGA-------SPDEAGLMAA----------CREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
                          570
                   ....*....|...
gi 1820002560 8121 REIGASFTAQQLA 8133
Cdd:PRK06164   527 REMAQARLAAERA 539
PLN02246 PLN02246
4-coumarate--CoA ligase
4544-5056 5.08e-20

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 98.51  E-value: 5.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4544 HDQFAEQARARPDTPaiCAWDGE----LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFV 4619
Cdd:PLN02246    26 HDYCFERLSEFSDRP--CLIDGAtgrvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4620 PLDPDHPASRHEHIFRQTGAQVVLASAQYATLWTSL--GRSVVIV---------------SEASTSQLPVVtktadpSVN 4682
Cdd:PLN02246   104 TANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLaeDDGVTVVtiddppegclhfselTQADENELPEV------EIS 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4683 PGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCL----GHGQAFGITDHTRVL----QFASYTFDaciaeiiTTLLC---CG 4751
Cdd:PLN02246   178 PDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFHSDDVILcvlpMFHIYSLN-------SVLLCglrVG 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4752 CICVPSDSDRRNNLAKAINAMDVNWALLTPSVARML--DPCV----VQSLKILVLG----GEQVNSADWDRWPKSI--Qt 4819
Cdd:PLN02246   251 AAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIakSPVVekydLSSIRMVLSGaaplGKELEDAFRAKLPNAVlgQ- 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4820 inAYGPTEC----SICCTTysGKQGF--KSGTIGTSIVSVSW-VVDPENHNRLaPLGSIGELLVEGPILARGYLNDMEKT 4892
Cdd:PLN02246   330 --GYGMTEAgpvlAMCLAF--AKEPFpvKSGSCGTVVRNAELkIVDPETGASL-PRNQPGEICIRGPQIMKGYLNDPEAT 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4893 EAAfIDDPAWLlegyggHsgrqgrlykTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE-----HHvreCLTEA-- 4965
Cdd:PLN02246   405 ANT-IDKDGWL------H---------TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEallisHP---SIADAav 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4966 ----KQLAVEVIVpegeggyamlaAFVQLGDDTYntlVKEKAGGDSLTVQVVFLDRVeeelaKRVpehmmlttFFTlEAM 5041
Cdd:PLN02246   466 vpmkDEVAGEVPV-----------AFVVRSNGSE---ITEDEIKQFVAKQVVFYKRI-----HKV--------FFV-DSI 517
                          570
                   ....*....|....*
gi 1820002560 5042 PTTTSGKIDRKRLRE 5056
Cdd:PLN02246   518 PKAPSGKILRKDLRA 532
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
5647-6036 5.52e-20

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 97.16  E-value: 5.52e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5647 ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTS 5726
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5727 AQHsarwigtnhqvvtvsagslgqlstlvnpvglpaipENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNL 5806
Cdd:cd05935     81 SEL-----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5807 SRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRNDLVKAISTMDVSCALLTPSVARLL------EPSSVPTLQMLV 5880
Cdd:cd05935    126 DVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLlatpefKTRDLSSLKVLT 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5881 LQGEQVSFADWNRWP--ASVQTINGYGPTECsiCCNTYSGKQG-FKSGIIGTSVASV-SWVVDPENHDRLAPlGSIGELL 5956
Cdd:cd05935    206 GGGAPMPPAVAEKLLklTGLRFVEGYGLTET--MSQTHTNPPLrPKLQCLGIP*FGVdARVIDIETGRELPP-NEVGEIV 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5957 VEGPILARGYLNDIQKTAAVFIDDpawllegypghPGRqgRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVE 6036
Cdd:cd05935    283 VRGPQIFKGYWNRPEETEESFIEI-----------KGR--RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE 349
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
1929-2387 5.57e-20

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 97.96  E-value: 5.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1929 RCVHDLFTEQAKARPHAPAICAWDG--ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAF 2006
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2007 VPLDPDHPASRHED---------IFRQTGAQVVVTSAQHSARWIGTNhqvVTVSAGSLEQFSTLvnPVDLPAKPENAAYV 2077
Cdd:cd05923     81 ALINPRLKAAELAEliergemtaAVIAVDAQVMDAIFQSGVRVLALS---DLVGLGEPESAGPL--IEDPPREPEQPAFV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2078 MFTSGSTGTPKGVVLEHRAVVTSCLG----HGQAFGVTNLLRALQFTAYTFDVcIAEIITTLVHGGCICVPSDsERRDNL 2153
Cdd:cd05923    156 FYTSGTTGLPKGAVIPQRAAESRVLFmstqAGLRHGRHNVVLGLMPLYHVIGF-FAVLVAALALDGTYVVVEE-FDPADA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2154 AKAITDMQVNWGYLTSS------VARLLDPCLVPSLKVLVLGGEQVNSTDWGKWPSSVQT--INGYGPTECCVFC----- 2220
Cdd:cd05923    234 LKLIEQERVTSLFATPThldalaAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGekVNIYGTTEAMNSLymrda 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2221 -TGYTGIQGFQSgnigtsiaSVSWVVDPENHGRLAPLGSIGELLVEGPILA--RGYLNDVDKTQAAFIDdpawllegypg 2297
Cdd:cd05923    314 rTGTEMRPGFFS--------EVRIVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD----------- 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2298 hegrqgRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKClPEANQLAVEVVPpsGERDHAMLAAFI- 2376
Cdd:cd05923    375 ------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRH-PGVTEVVVIGVA--DERWGQSVTACVv 445
                          490       500
                   ....*....|....*....|
gi 1820002560 2377 ---------RLDDETRNSPL 2387
Cdd:cd05923    446 pregtlsadELDQFCRASEL 465
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4567-5055 5.62e-20

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 97.20  E-value: 5.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLASA 4646
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4647 qyatlwtslgrsvvivseASTSQLpvvtkTADPSVNpgnaayaIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHT 4726
Cdd:cd05973     81 ------------------ANRHKL-----DSDPFVM-------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4727 RVLQFAS--------YTFDACIAEIITTLLCCGCICVPSDSD--RRNNLAKAINAMDVNWALLTPSVARMLDPCVvqSLK 4796
Cdd:cd05973    131 SFWNAADpgwayglyYAITGPLALGHPTILLEGGFSVESTWRviERLGVTNLAGSPTAYRLLMAAGAEVPARPKG--RLR 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4797 ILVLGGEQVNSA--DWDRWPKSIQTINAYGPTECS-ICCTTYSGKQGFKSGTIGTSIVSVSWVVDPENHNRLAPlGSIGE 4873
Cdd:cd05973    209 RVSSAGEPLTPEviRWFDAALGVPIHDHYGQTELGmVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGP-GEPGR 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4874 LLVE---GPILA-RGYLNdmekteaafIDDPAWllegygghsgrQGRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQR- 4948
Cdd:cd05973    288 LAIDianSPLMWfRGYQL---------PDTPAI-----------DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRi 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4949 ----VELGEVEH-HVREClteakqlAVeVIVPEGEGGyAMLAAFVQLGDDTYNTlvkekaggdsltvqvvflDRVEEELA 5023
Cdd:cd05973    348 gpfdVESALIEHpAVAEA-------AV-IGVPDPERT-EVVKAFVVLRGGHEGT------------------PALADELQ 400
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1820002560 5024 ----KRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLR 5055
Cdd:cd05973    401 lhvkKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
4551-5056 6.36e-20

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 98.34  E-value: 6.36e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAI--CAWDGE---LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPldPDH 4625
Cdd:cd05970     27 AKEYPDKLALvwCDDAGEeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP--ATH 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4626 PASRHEHIFRQTGAQV-----------------VLASAQYATLWTSLGRSVV--------IVSEAStsqlPVVTKTADPS 4680
Cdd:cd05970    105 QLTAKDIVYRIESADIkmivaiaednipeeiekAAPECPSKPKLVWVGDPVPegwidfrkLIKNAS----PDFERPTANS 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4681 VNPG-NAAYAIFTSGSTGIPKGVvlEHkaVVTSCLGH---GQAF-GITDHTRVLQFASYTFDACIAEIITTLLCCGCICV 4755
Cdd:cd05970    181 YPCGeDILLVYFSSGTTGMPKMV--EH--DFTYPLGHivtAKYWqNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVF 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4756 PSDSDR--RNNLAKAINAMDVNWALLTPSVARML--------DpcvVQSLKILVLGGEQVNSADWDRWPK--SIQTINAY 4823
Cdd:cd05970    257 VYDYDKfdPKALLEKLSKYGVTTFCAPPTIYRFLiredlsryD---LSSLRYCTTAGEALNPEVFNTFKEktGIKLMEGF 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4824 GPTECSICCTTYSGKQGfKSGTIGTSivSVSWVVDPENHN-RLAPLGSIGELLV---EG-PI-LARGYLNDMEKTEAAFI 4897
Cdd:cd05970    334 GQTETTLTIATFPWMEP-KPGSMGKP--APGYEIDLIDREgRSCEAGEEGEIVIrtsKGkPVgLFGGYYKDAEKTAEVWH 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4898 DdpawlleGYgghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE----HH--VRECLTEAkqlave 4971
Cdd:cd05970    411 D-------GY----------YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVEsaliQHpaVLECAVTG------ 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4972 viVPEGEGGYAMLAAFVqlgddtyntLVKEKAGGDSLTVQVvfLDRVEEELA----KRVPEHmmlttfftLEAMPTTTSG 5047
Cdd:cd05970    468 --VPDPIRGQVVKATIV---------LAKGYEPSEELKKEL--QDHVKKVTApykyPRIVEF--------VDELPKTISG 526

                   ....*....
gi 1820002560 5048 KIDRKRLRE 5056
Cdd:cd05970    527 KIRRVEIRE 535
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
1510-1717 6.86e-20

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 92.79  E-value: 6.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1510 SPLQEGLMSLTAKRAgDYIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQ---------HSELGL-LQVVIEENI 1579
Cdd:COG4908      2 SPAQKRFLFLEPGSN-AYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEedgepvqriDPDADLpLEVVDLSAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1580 QWTEPKS-LEEYLSEDKAVSVGLG-DPLARYAFVKEACGGKRwFVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQWQP-- 1655
Cdd:COG4908     81 PEPEREAeLEELVAEEASRPFDLArGPLLRAALIRLGEDEHV-LLLTIHHIISDGWSLGILLRELAALYAALLEGEPPpl 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 1656 -----SFNAFI----QYLGQQDLEATVAYWQTALADCEAVL-FPT-LPPTVTQPVADATVEYqcpPLSKATSD 1717
Cdd:COG4908    160 pelpiQYADYAawqrAWLQSEALEKQLEYWRQQLAGAPPVLeLPTdRPRPAVQTFRGATLSF---TLPAELTE 229
PRK07787 PRK07787
acyl-CoA synthetase; Validated
7614-8021 7.77e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 97.37  E-value: 7.77e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7614 AEQARARPGAPAICAWDGELTYGELDVLSSNLAGhlvqlGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPA 7693
Cdd:PRK07787     7 AAVAAAADIADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7694 SRHEEIFEQTGAQVVVASAQysarWTSSSCHVVTVSkalssqLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHR 7773
Cdd:PRK07787    82 AERRHILADSGAQAWLGPAP----DDPAGLPHVPVR------LHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRR 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7774 AVATS--------------CLGHGRA-FGITNL-----------SRVLQFASYTFDACIAEIIT--TLLCGgcicVPSDS 7825
Cdd:PRK07787   152 AIAADldalaeawqwtaddVLVHGLPlFHVHGLvlgvlgplrigNRFVHTGRPTPEAYAQALSEggTLYFG----VPTVW 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7826 DR---RNSLAKAISTmdvnwafltpsvARLLDPGLIP-----SLKILAIGGEQSssadwnrwpgsvqkIHVYGPTECCIF 7897
Cdd:PRK07787   228 SRiaaDPEAARALRG------------ARLLVSGSAAlpvpvFDRLAALTGHRP--------------VERYGMTETLIT 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7898 CtgyTTKQGFE--PSTIGTSVASVSWVVDPENHNRLAPLG-SMGELLMEGPILARGYLNDVDKTEAAFIDDpAWllegyp 7974
Cdd:PRK07787   282 L---STRADGErrPGWVGLPLAGVETRLVDEDGGPVPHDGeTVGELQVRGPTLFDGYLNRPDATAAAFTAD-GW------ 351
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 7975 ghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQ-VKVRGQRVELGEVE 8021
Cdd:PRK07787   352 ---------FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIE 390
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
5629-6138 8.75e-20

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 97.34  E-value: 8.75e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5629 TEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpdHPA 5708
Cdd:PRK03640     9 KQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN--TRL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5709 SRHEDTFR--HTGAQVVVTSAQHSARWIGtnHQVVTVSagSLGQLsTLVNPVGLPAIPENAVY-IMFTSGSTGIPKGVVL 5785
Cdd:PRK03640    87 SREELLWQldDAEVKCLITDDDFEAKLIP--GISVKFA--ELMNG-PKEEAEIQEEFDLDEVAtIMYTSGTTGKPKGVIQ 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5786 E-----HRAVVTS---------CWgrgRA----FGITNLSRVLQfasytfdacmdeiitTLMYGGCICVPS--DSDRRND 5845
Cdd:PRK03640   162 TygnhwWSAVGSAlnlglteddCW---LAavpiFHISGLSILMR---------------SVIYGMRVVLVEkfDAEKINK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5846 LVK--AISTMDVSCALLTPSVARLLE---------------PSSVPTLQMLVLQGEQVsfadwnrwpasVQTingYGPTE 5908
Cdd:PRK03640   224 LLQtgGVTIISVVSTMLQRLLERLGEgtypssfrcmllgggPAPKPLLEQCKEKGIPV-----------YQS---YGMTE 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5909 -CS-ICcnTYSGKQGF-KSGIIGTSVASVSwvVDPENHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDdpAWLl 5985
Cdd:PRK03640   290 tASqIV--TLSPEDALtKLGSAGKPLFPCE--LKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD--GWF- 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5986 egypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhHVRECLPearqlAVEVILPSGQKDH--- 6062
Cdd:PRK03640   363 --------------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE-EVLLSHP-----GVAEAGVVGVPDDkwg 422
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6063 AMLAAFVqleegtqnaLLDKEASgEDSMAQVvflasVEEELAKrlpeHMVPTVFFSLLHFPTTTSGKTDRKRLREI 6138
Cdd:PRK03640   423 QVPVAFV---------VKSGEVT-EEELRHF-----CEEKLAK----YKVPKRFYFVEELPRNASGKLLRHELKQL 479
PRK06188 PRK06188
acyl-CoA synthetase; Validated
843-1365 1.09e-19

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 97.36  E-value: 1.09e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  843 NADMPPAVDRCIH--DLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAML 920
Cdd:PRK06188     1 QATMADLLHSGATygHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  921 AVLKAGGAFVPLdpgHP-ASR--HEEIFKQIGAQVVLTssqHAMLFAssERHQVTVSKVSTsqLPTVVNFAKSPV----- 992
Cdd:PRK06188    81 AAQLAGLRRTAL---HPlGSLddHAYVLEDAGISTLIV---DPAPFV--ERALALLARVPS--LKHVLTLGPVPDgvdll 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  993 ---------------DPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQFA--SYtfdACIAEII 1055
Cdd:PRK06188   151 aaaakfgpaplvaaaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTplSH---AGGAFFL 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1056 TTLLYGGCICVPSESDRRNNLAkAISTMDVNCALLTPS-VARLLEPSAVP-----SLKrLVLQGEQ----VSFADWNRWP 1125
Cdd:PRK06188   228 PTLLRGGTVIVLAKFDPAEVLR-AIEEQRITATFLVPTmIYALLDHPDLRtrdlsSLE-TVYYGASpmspVRLAEAIERF 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1126 GSV--QTingYGPTECSVCCNTYSGKQ------------GFKsgIIGTSVASLswvvdaGNHNRLAPLGSIGELLVEGPI 1191
Cdd:PRK06188   306 GPIfaQY---YGQTEAPMVITYLRKRDhdpddpkrltscGRP--TPGLRVALL------DEDGREVAQGEVGEICVRGPL 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1192 LARGYLNDIDKTEAAFIDDpaWLlegyegHagrrgrlykTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVRE 1271
Cdd:PRK06188   375 VMDGYWNRPEETAEAFRDG--WL------H---------TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAE 437
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1272 cLPEARQLAVeVILPsgqkehallaafiqldkgnhnalfEEKAsGEDSMAQVVFLTGV---EEEL-----AKRLPEHMVP 1343
Cdd:PRK06188   438 -HPAVAQVAV-IGVP------------------------DEKW-GEAVTAVVVLRPGAavdAAELqahvkERKGSVHAPK 490
                          570       580
                   ....*....|....*....|..
gi 1820002560 1344 TILFtVKAMPITTSGKIDRKRL 1365
Cdd:PRK06188   491 QVDF-VDSLPLTALGKPDKKAL 511
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
842-1367 1.10e-19

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 97.64  E-value: 1.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  842 WNADMPPAVD--------RCIHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLV-QLGVKREDVVPLCFEKS 912
Cdd:PRK08751     7 WLQSYPAGVAaeidleqfRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNC 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  913 MWTVVAMLAVLKAGGAFVPLDPGHPAS--RHEEIFKQIGAQVVL----TSSQHAMlfASSERHQVTVSK----------- 975
Cdd:PRK08751    87 LQYPIATFGVLRAGLTVVNVNPLYTPRelKHQLIDSGASVLVVIdnfgTTVQQVI--ADTPVKQVITTGlgdmlgfpkaa 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  976 ------------VSTSQLPTVVNFAKS------------PVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAF 1031
Cdd:PRK08751   165 lvnfvvkyvkklVPEYRINGAIRFREAlalgrkhsmptlQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWL 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1032 GYTDHAR------VLQFASYTFDACIAEIITTLLYGGC---ICVPSE--------SDRRNNLAKAISTMdVNCALLTPSV 1094
Cdd:PRK08751   245 AGTGKLEegcevvITALPLYHIFALTANGLVFMKIGGCnhlISNPRDmpgfvkelKKTRFTAFTGVNTL-FNGLLNTPGF 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1095 ARLlepsAVPSLKRLVLQGEQVSFADWNRWP--GSVQTINGYGPTECS--VCCNTYSGKQgfKSGIIGTSVASLSWVVDa 1170
Cdd:PRK08751   324 DQI----DFSSLKMTLGGGMAVQRSVAERWKqvTGLTLVEAYGLTETSpaACINPLTLKE--YNGSIGLPIPSTDACIK- 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1171 GNHNRLAPLGSIGELLVEGPILARGYLNDIDKTeAAFIDDPAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKD 1250
Cdd:PRK08751   397 DDAGTVLAIGEIGELCIKGPQVMKGYWKRPEET-AKVMDADGWL---------------HTGDIARMDEQGFVYIVDRKK 460
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1251 SQVKVRGQRVELGEIEhHVRECLPEARQLAVeVILPSGQKEHALLAAFIQLDKgnhnALFEEKasgedsmaqvvfltgVE 1330
Cdd:PRK08751   461 DMILVSGFNVYPNEIE-DVIAMMPGVLEVAA-VGVPDEKSGEIVKVVIVKKDP----ALTAED---------------VK 519
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 1820002560 1331 EELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:PRK08751   520 AHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
PRK08316 PRK08316
acyl-CoA synthetase; Validated
4551-5056 1.15e-19

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 97.31  E-value: 1.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVP----LDPDHP 4626
Cdd:PRK08316    21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPvnfmLTGEEL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4627 AsrheHIFRQTGAQVVLASA----------QYATLWTSLGRSVVIVSEASTSQLPVVT-----KTADPSVNPGNAAYA-- 4689
Cdd:PRK08316   101 A----YILDHSGARAFLVDPalaptaeaalALLPVDTLILSLVLGGREAPGGWLDFADwaeagSVAEPDVELADDDLAqi 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4690 IFTSGSTGIPKGVVLEHKAVV---TSCLghgQAFGITDHTRVL---------QF-----------------ASYTFDACI 4740
Cdd:PRK08316   177 LYTSGTESLPKGAMLTHRALIaeyVSCI---VAGDMSADDIPLhalplyhcaQLdvflgpylyvgatnvilDAPDPELIL 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4741 AEI----ITTLLCCGCICVP----SDSDRRN--NLAKA---INAMDVnwalltPSVARMLdpcvvqslkilvlggeqvns 4807
Cdd:PRK08316   254 RTIeaerITSFFAPPTVWISllrhPDFDTRDlsSLRKGyygASIMPV------EVLKELR-------------------- 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4808 adwDRWPKsIQTINAYGPTECSICCTTYSGK-QGFKSGTIGTSIVSV-SWVVDpENHNRLAPlGSIGELLVEGPILARGY 4885
Cdd:PRK08316   308 ---ERLPG-LRFYNCYGQTEIAPLATVLGPEeHLRRPGSAGRPVLNVeTRVVD-DDGNDVAP-GEVGEIVHRSPQLMLGY 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4886 LNDMEKTEAAFIDDpaWLlegyggHSgrqgrlyktGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhhvrECLTEA 4965
Cdd:PRK08316   382 WDDPEKTAEAFRGG--WF------HS---------GDLGVMDEEGYITVVDRKKDMIKTGGENVASREVE----EALYTH 440
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4966 KQLA-VEVI-VPEGEGGYAMLAAFVqlgddtyntlVKEkagGDSLTVQVVfLDRVEEELA-----KRVpehmmlttFFTl 5038
Cdd:PRK08316   441 PAVAeVAVIgLPDPKWIEAVTAVVV----------PKA---GATVTEDEL-IAHCRARLAgfkvpKRV--------IFV- 497
                          570
                   ....*....|....*...
gi 1820002560 5039 EAMPTTTSGKIDRKRLRE 5056
Cdd:PRK08316   498 DELPRNPSGKILKRELRE 515
PRK06178 PRK06178
acyl-CoA synthetase; Validated
1913-2444 1.29e-19

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 97.42  E-value: 1.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1913 RQQLwAWNQEVP-----PAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVV----P 1983
Cdd:PRK06178    13 LQQA-AWPAGIPrepeyPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVavflP 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1984 LC--FeksmwtVVAMLAVLKAGGAFVPLDPdhPASRHEDIF--RQTGAQVVVT-----------SAQHSARwigtnHQVV 2048
Cdd:PRK06178    92 NCpqF------HIVFFGILKLGAVHVPVSP--LFREHELSYelNDAGAEVLLAldqlapvveqvRAETSLR-----HVIV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2049 T-----------------------VSAGSLEQFSTL----VNPVDLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSC 2101
Cdd:PRK06178   159 TsladvlpaeptlplpdslraprlAAAGAIDLLPALractAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2102 lghGQAFGVTNLLRA-LQFTAYTFDVCIAE----IITTLVHGGCICVPSdseRRDNLA--KAITDMQVNWGYLT-SSVAR 2173
Cdd:PRK06178   239 ---AAAYAVAVVGGEdSVFLSFLPEFWIAGenfgLLFPLFSGATLVLLA---RWDAVAfmAAVERYRVTRTVMLvDNAVE 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2174 LLD-PCL----VPSLKvlvlggeQVNSTD------------WGKWPSSVQTINGYGPTE---CCVFCTgytgiqGFQSGN 2233
Cdd:PRK06178   313 LMDhPRFaeydLSSLR-------QVRVVSfvkklnpdyrqrWRALTGSVLAEAAWGMTEthtCDTFTA------GFQDDD 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2234 I--------------GTSIAsvswVVDPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDdpAWLlegypghe 2299
Cdd:PRK06178   380 FdllsqpvfvglpvpGTEFK----ICDFET-GELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD--GWL-------- 444
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2300 grqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVE----HHmrkclPEAnqLAVEVVPPSGERDHAMLAAF 2375
Cdd:PRK06178   445 -------HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEallgQH-----PAV--LGSAVVGRPDPDKGQVPVAF 510
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 2376 IRLDDETRNSpliikyaednstaqivfltgiEEELSERLPQHM----VPTVFFaLVHFPTTTSGKTDRKRLRE 2444
Cdd:PRK06178   511 VQLKPGADLT---------------------AAALQAWCRENMavykVPEIRI-VDALPMTATGKVRKQDLQA 561
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
5196-5503 1.38e-19

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 95.58  E-value: 1.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5196 MYPCSPLQEG-----LMSltakRAGD-YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIvqHSElGL---LQVV-- 5264
Cdd:cd19544      1 IYPLAPLQEGilfhhLLA----EEGDpYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAI--LWE-GLsepVQVVwr 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5265 -----VEEkIQWTESKRLEEYLRE---DKAVSMGLgdRLA---RYALIKEPydGGKRWFV-WTIHHALYDGWSLPRILQA 5332
Cdd:cd19544     74 qaelpVEE-LTLDPGDDALAQLRArfdPRRYRLDL--RQApllRAHVAEDP--ANGRWLLlLLFHHLISDHTSLELLLEE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5333 VKQIYSG---AVPERQPsFNAFI-QYLGQQDLEAATLYWQTALADCKAalfPTLP--PTVTQPVADTTVEYQCPPPSQSA 5406
Cdd:cd19544    149 IQAILAGraaALPPPVP-YRNFVaQARLGASQAEHEAFFREMLGDVDE---PTAPfgLLDVQGDGSDITEARLALDAELA 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5407 TDI---------TTSTLVRAAWAIVTSRYTSSDDVVFGaTV-TGRNAPIAGVEAMVGPTIATVPLRVCLQkDQTVSTLLE 5476
Cdd:cd19544    225 QRLraqarrlgvSPASLFHLAWALVLARCSGRDDVVFG-TVlSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVR 302
                          330       340       350
                   ....*....|....*....|....*....|
gi 1820002560 5477 CLQQQSTDMIAHEQTGL---QRIAKMSPGA 5503
Cdd:cd19544    303 QTHARLAELLRHEHASLalaQRCSGVPAPT 332
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
878-1315 1.43e-19

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 96.27  E-value: 1.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPldpghpasRheeifkqiGAQVvlTSS 957
Cdd:cd17640      6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVV--------R--------GSDS--SVE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  958 QHAMLFASSErhqvtvskvstSQLPTVVNfakspvDPGNTAYIIFTSGTTGIPKGVVLQHRAVT--TSCLGHGEAFGYTD 1035
Cdd:cd17640     68 ELLYILNHSE-----------SVALVVEN------DSDDLATIIYTSGTTGNPKGVMLTHANLLhqIRSLSDIVPPQPGD 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1036 haRVLQF----------ASYTFDACiaeiittllygGCICVPSesdrrnnlakAISTMDVNCALLTP----SVARLLEP- 1100
Cdd:cd17640    131 --RFLSIlpiwhsyersAEYFIFAC-----------GCSQAYT----------SIRTLKDDLKRVKPhyivSVPRLWESl 187
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1101 --------SAVPSLKRLVLQ----GEQVSFA--DWNRWPGSVQT---------INGYGPTECS--VCCNTysgkqgFKSG 1155
Cdd:cd17640    188 ysgiqkqvSKSSPIKQFLFLfflsGGIFKFGisGGGALPPHVDTffeaigievLNGYGLTETSpvVSARR------LKCN 261
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1156 IIGTSVASLS----WVVDAGNHNRLAPlGSIGELLVEGPILARGYLNDIDKTEAAfIDDPAWLlegyeghagrrgrlyKT 1231
Cdd:cd17640    262 VRGSVGRPLPgteiKIVDPEGNVVLPP-GEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDGWF---------------NT 324
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1232 GDLVRCDADGNLVCLGR-KDSQVKVRGQRVELGEIEhhvRECLpeaRQLAVEVILPSGQKEHAlLAAFIQLDKGNHNALF 1310
Cdd:cd17640    325 GDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIE---EALM---RSPFIEQIMVVGQDQKR-LGALIVPNFEELEKWA 397

                   ....*
gi 1820002560 1311 EEKAS 1315
Cdd:cd17640    398 KESGV 402
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
4115-4422 1.44e-19

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 95.58  E-value: 1.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4115 VYPCSPLQEG-----LMSltakRAGD-YIMQTVLEL--RADVneDAFRAAWELVVQLTAVLRTRIvqHSElGL---LQVV 4183
Cdd:cd19544      1 IYPLAPLQEGilfhhLLA----EEGDpYLLRSLLAFdsRARL--DAFLAALQQVIDRHDILRTAI--LWE-GLsepVQVV 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4184 -------VEErIQWTESESLEEYPREDKAVSMGVGDR----LARYALIKEPydGGKRWFV-WTMHHALYDGWSLPRILHA 4251
Cdd:cd19544     72 wrqaelpVEE-LTLDPGDDALAQLRARFDPRRYRLDLrqapLLRAHVAEDP--ANGRWLLlLLFHHLISDHTSLELLLEE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4252 VK--QAYSGVVLERQPSFNAFI-QYLSQQDPEAAAAYWQTALVDCKAalfPTLP--PTVTQPVADTTVEYQCPPPSQSAT 4326
Cdd:cd19544    149 IQaiLAGRAAALPPPVPYRNFVaQARLGASQAEHEAFFREMLGDVDE---PTAPfgLLDVQGDGSDITEARLALDAELAQ 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4327 DI---------TTSTLARAAWAIVTSRYTSSDDVVFGaTV-TGRNAPIAGGEAIVGPTIATVPVRLRVQrDQTVFAFLQG 4396
Cdd:cd19544    226 RLraqarrlgvSPASLFHLAWALVLARCSGRDDVVFG-TVlSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQ 303
                          330       340
                   ....*....|....*....|....*....
gi 1820002560 4397 VQQQATDMIAHEQTGL---QRIAKMSPGA 4422
Cdd:cd19544    304 THARLAELLRHEHASLalaQRCSGVPAPT 332
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
4551-5056 1.50e-19

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 96.88  E-value: 1.50e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAICAWDGE--LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 4628
Cdd:PRK05852    26 ATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIA 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4629 RHEHIFRQTGAQVVLAS-------AQYATLWTSLGRSVVIVSEASTSQLPV-----VTKTADPSVNPG---NAAYAIFTS 4693
Cdd:PRK05852   106 EQRVRSQAAGARVVLIDadgphdrAEPTTRWWPLTVNVGGDSGPSGGTLSVhldaaTEPTPATSTPEGlrpDDAMIMFTG 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4694 GSTGIPKGVVLEHKAVVTSCLGHGQAFGITDH-TRVLQFASYTFDACIAEIITTLLCCGCICVPSDSD-RRNNLAKAINA 4771
Cdd:PRK05852   186 GTTGLPKMVPWTHANIASSVRAIITGYRLSPRdATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRfSAHTFWDDIKA 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4772 MDVNWALLTPSVAR-MLDPCVVQSLKILVLGGEQVNSADWDRWPKSIQT---------INAYGPTECSICCTT------- 4834
Cdd:PRK05852   266 VGATWYTAVPTIHQiLLERAATEPSGRKPAALRFIRSCSAPLTAETAQAlqtefaapvVCAFGMTEATHQVTTtqiegig 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4835 YSGKQGFKSGTIGTSIVSVSWVVDPENHNrlAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDdpAWLlegygghsgrq 4914
Cdd:PRK05852   346 QTENPVVSTGLVGRSTGAQIRIVGSDGLP--LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD--GWL----------- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4915 grlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREC--LTEAKQLAveviVPEGEGGYAMLAAFVQlgd 4992
Cdd:PRK05852   411 ----RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHpnVMEAAVFG----VPDQLYGEAVAAVIVP--- 479
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 4993 dtyntlvKEKAG--GDSLTVQvvfldrVEEELAK-RVPehmmlTTFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:PRK05852   480 -------RESAPptAEELVQF------CRERLAAfEIP-----ASFQEASGLPHTAKGSLDRRAVAE 528
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
3463-3989 1.51e-19

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 97.56  E-value: 1.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3463 VHDLFTEQAKARPHAPAIcAWDGE------LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGG 3536
Cdd:cd05968     63 VEQLLDKWLADTRTRPAL-RWEGEdgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3537 AFVPL----DPDHPASRHE----------EIFEQTGAQV-VVASAQYSARWTSSSCHVVTVSKALSSQLPAVVD------ 3595
Cdd:cd05968    142 IVVPIfsgfGKEAAATRLQdaeakalitaDGFTRRGREVnLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRdlsyde 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3596 ------STNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAV---ATSCLGHGraFGITNLSRVLQFASYTFDACIAEIITT 3666
Cdd:cd05968    222 eketagDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFplkAAQDMYFQ--FDLKPGDLLTWFTDLGWMMGPWLIFGG 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3667 LLCGGCIC----VPsDSDRRNSLAKAISTMDVNWAFLTPSVARLLDP-GLIP-------SLKILAIGGEQSSSADWN--- 3731
Cdd:cd05968    300 LILGATMVlydgAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALKPrGDAPvnahdlsSLRVLGSTGEPWNPEPWNwlf 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3732 --RWPGSVQKIHVYGPTECC--IFCtGYTTKQgFEPSTIGTSVASVSWVVDPENHNRLAPlgSMGELLMEGPI--LARGY 3805
Cdd:cd05968    379 etVGKGRNPIINYSGGTEISggILG-NVLIKP-IKPSSFNGPVPGMKADVLDESGKPARP--EVGELVLLAPWpgMTRGF 454
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3806 LNDVDKTEAAFID--DPAWLlegypgHpgrqgrlyktGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE------HH 3877
Cdd:cd05968    455 WRDEDRYLETYWSrfDNVWV------H----------GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIEsvlnahPA 518
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3878 VREClpearqLAVEVILP-SGQKDHamlaAFVQLEEGtqnalldkeaggedsmaqVVFLASVEEELAKRLPEHM----VP 3952
Cdd:cd05968    519 VLES------AAIGVPHPvKGEAIV----CFVVLKPG------------------VTPTEALAEELMERVADELgkplSP 570
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 1820002560 3953 TVFFSLLHFPTTTSGKTDRKRLReigASFTAQQLAEM 3989
Cdd:cd05968    571 ERILFVKDLPKTRNAKVMRRVIR---AAYLGKELGDL 604
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
4566-5057 2.07e-19

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 96.44  E-value: 2.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4566 ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLAS 4645
Cdd:cd17642     44 NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4646 AQyaTLWTSLG--------RSVVIVSEAS------------TSQLPVVTKTAD---PSVNPGNA-AYAIFTSGSTGIPKG 4701
Cdd:cd17642    124 KK--GLQKVLNvqkklkiiKTIIILDSKEdykgyqclytfiTQNLPPGFNEYDfkpPSFDRDEQvALIMNSSGSTGLPKG 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4702 VVLEHKAVVTScLGHGQ--AFG--ITDHTRVLQFASYTFDACIAEIITTLlCCGCICVPSDSDRRNNLAKAINAMDVNWA 4777
Cdd:cd17642    202 VQLTHKNIVAR-FSHARdpIFGnqIIPDTAILTVIPFHHGFGMFTTLGYL-ICGFRVVLMYKFEEELFLRSLQDYKVQSA 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4778 LLTPSV------ARMLDPCVVQSLKILVLGGEQVNSADWDRWPKSIQ---TINAYGPTEcsiccTTYS---GKQGF-KSG 4844
Cdd:cd17642    280 LLVPTLfaffakSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKlpgIRQGYGLTE-----TTSAiliTPEGDdKPG 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4845 TIGTSIVSVSW-VVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAfIDDPAWLlegygghsgrqgrlyKTGDL 4923
Cdd:cd17642    355 AVGKVVPFFYAkVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEATKAL-IDKDGWL---------------HSGDI 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4924 VRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVrecLTEAKQLAVEVI-VPEGEGGyAMLAAFVqlgddtyntlVKEK 5002
Cdd:cd17642    418 AYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESIL---LQHPKIFDAGVAgIPDEDAG-ELPAAVV----------VLEA 483
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 5003 agGDSLTVQVVfLDRVEEEL--AKRVPEHMMLttfftLEAMPTTTSGKIDRKRLREI 5057
Cdd:cd17642    484 --GKTMTEKEV-MDYVASQVstAKRLRGGVKF-----VDEVPKGLTGKIDRRKIREI 532
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
1919-2444 2.07e-19

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 96.76  E-value: 2.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1919 WNQEVPPAIER--------CVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQL-GVNPEDVVPLCFEKS 1989
Cdd:PRK05677     6 WKDKYPAGIAAeinpdeypNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1990 MWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSAQ--HSARWI----GTNHQVVTVSAGSLEQFS-TLV 2062
Cdd:PRK05677    86 LQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANmaHLAEKVlpktGVKHVIVTEVADMLPPLKrLLI 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2063 NPV-----------DLP---------------------AKPENAAYVMFTSGSTGTPKGVVLEHR----------AVVTS 2100
Cdd:PRK05677   166 NAVvkhvkkmvpayHLPqavkfndalakgagqpvteanPQADDVAVLQYTGGTTGVAKGAMLTHRnlvanmlqcrALMGS 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2101 CLGHGQAFGVTNLlRALQFTAYTFDvCIAEIITTlVHGGCICVPSDserrdnLAKAITDMQvNW------GYLTSSVA-- 2172
Cdd:PRK05677   246 NLNEGCEILIAPL-PLYHIYAFTFH-CMAMMLIG-NHNILISNPRD------LPAMVKELG-KWkfsgfvGLNTLFVAlc 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2173 -----RLLDpclVPSLKVLVLGGEQVNSTDWGKWP--SSVQTINGYGPTECCVFCTGyTGIQGFQSGNIGTSIASVSW-V 2244
Cdd:PRK05677   316 nneafRKLD---FSALKLTLSGGMALQLATAERWKevTGCAICEGYGMTETSPVVSV-NPSQAIQVGTIGIPVPSTLCkV 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2245 VDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFiDDPAWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLG 2324
Cdd:PRK05677   392 IDDD--GNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL-DSDGWL---------------KTGDIALIQEDGYMRIVD 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2325 RKDSQVKVRGQRVELGEVEHHMrKCLPEANQLAVEVVP--PSGErdhaMLAAFIrlddetrnsplIIKYAEDNSTAQIVf 2402
Cdd:PRK05677   454 RKKDMILVSGFNVYPNELEDVL-AALPGVLQCAAIGVPdeKSGE----AIKVFV-----------VVKPGETLTKEQVM- 516
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 2403 ltgieEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:PRK05677   517 -----EHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
PRK06164 PRK06164
acyl-CoA synthetase; Validated
1933-2455 2.21e-19

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 96.35  E-value: 2.21e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmWtVVAMLAVLKAGGAFVP 2008
Cdd:PRK06164    14 SLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVavwlPNCIE---W-VVLFLACARLGATVIA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2009 LDPDHPASRHEDIFRQTGAQVVV--------------TSAQHSARwiGTNHQVVTVSAGSLE----QFSTLVNPVDLP-- 2068
Cdd:PRK06164    90 VNTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailAAVPPDAL--PPLRAIAVVDDAADAtpapAPGARVQLFALPdp 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2069 ---------AKPENAAYVMFT-SGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTN---LLRALQFT-AYTFDVCIAeiitT 2134
Cdd:PRK06164   168 appaaagerAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPgavLLAALPFCgVFGFSTLLG----A 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2135 LVHGG-CICVPS-DSERRdnlAKAITDMQVNWGYLTSSV-ARLLD----PCLVPSLKVLvlgGEQVNSTDWGKWPSSVQT 2207
Cdd:PRK06164   244 LAGGApLVCEPVfDAART---ARALRRHRVTHTFGNDEMlRRILDtageRADFPSARLF---GFASFAPALGELAALARA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2208 ----ING-YGPTEccvfctgytgIQGFQSGNIGTSIASVSW--------------VVDPENhGRLAPLGSIGELLVEGPI 2268
Cdd:PRK06164   318 rgvpLTGlYGSSE----------VQALVALQPATDPVSVRIegggrpaspearvrARDPQD-GALLPDGESGEIEIRAPS 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2269 LARGYLNDVDKTQAAFIDDpawlleGYpghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRK 2348
Cdd:PRK06164   387 LMRGYLDNPDATARALTDD------GY----------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEA 450
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2349 CLPEANQLAVEVvppsgERD-HAMLAAFIRLDDETRNSPLIIKYAednstaqivfltgieeeLSERLPQHMVPTVFFALV 2427
Cdd:PRK06164   451 LPGVAAAQVVGA-----TRDgKTVPVAFVIPTDGASPDEAGLMAA-----------------CREALAGFKVPARVQVVE 508
                          570       580       590
                   ....*....|....*....|....*....|.
gi 1820002560 2428 HFPTTTSG---KTDRKRLREIGASFTAQQLA 2455
Cdd:PRK06164   509 AFPVTESAngaKIQKHRLREMAQARLAAERA 539
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
3022-3354 2.29e-19

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 95.20  E-value: 2.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3022 VFPCTPMQEGIL-----TSQGkdpDAYWVCFIYEViPNQETsisLARLQQAWKGVVHQHSLLRTLLVdnvpgSTGTTN-- 3094
Cdd:cd19544      1 IYPLAPLQEGILfhhllAEEG---DPYLLRSLLAF-DSRAR---LDAFLAALQQVIDRHDILRTAIL-----WEGLSEpv 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3095 -VVLKDPQPSISVFS-SEGTATIELFRSRYNPAAQR-SIGQ--LQHhLSICQ-LNNGKVYLCLDINHAIIDAHSRGILMH 3168
Cdd:cd19544     69 qVVWRQAELPVEELTlDPGDDALAQLRARFDPRRYRlDLRQapLLR-AHVAEdPANGRWLLLLLFHHLISDHTSLELLLE 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3169 DLQ--EAYDANLNPQSTSFRDFASYIKQQ-SQEEAGRYWAEYLDGVEPcffPSL--------GDsgGANTIPRTVEVPSI 3237
Cdd:cd19544    148 EIQaiLAGRAAALPPPVPYRNFVAQARLGaSQAEHEAFFREMLGDVDE---PTApfglldvqGD--GSDITEARLALDAE 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3238 DSSAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPLISILPCRIHLHkQLTVLEAL 3317
Cdd:cd19544    223 LAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAV 301
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1820002560 3318 KTVQENYASSLSFQTFPLASMHSFLGLGTSA-LFNTAL 3354
Cdd:cd19544    302 RQTHARLAELLRHEHASLALAQRCSGVPAPTpLFSALL 339
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
4567-4955 2.68e-19

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 95.50  E-value: 2.68e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTgaqvvlasa 4646
Cdd:cd17640      6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHS--------- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4647 qyatlwtslgRSVVIVSEASTSQLpvvtktadpsvnpgnaAYAIFTSGSTGIPKGVVLEHKAVVTScLGHGQAFGITDH- 4725
Cdd:cd17640     77 ----------ESVALVVENDSDDL----------------ATIIYTSGTTGNPKGVMLTHANLLHQ-IRSLSDIVPPQPg 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4726 TRVLQF----------ASYTFDAC-IAEIITTLlccgcICVPSDSDR----------------RNNLAKAINAMdvnwal 4778
Cdd:cd17640    130 DRFLSIlpiwhsyersAEYFIFACgCSQAYTSI-----RTLKDDLKRvkphyivsvprlweslYSGIQKQVSKS------ 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4779 ltPSVARMLdpcvvqsLKILVLGGE---QVNSAD-----WDRWPKS--IQTINAYGPTECS--ICCTTYSGKqgfKSGTI 4846
Cdd:cd17640    199 --SPIKQFL-------FLFFLSGGIfkfGISGGGalpphVDTFFEAigIEVLNGYGLTETSpvVSARRLKCN---VRGSV 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4847 GTSIVSVSW-VVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAfIDDPAWLlegygghsgrqgrlyKTGDLVR 4925
Cdd:cd17640    267 GRPLPGTEIkIVDPEGNVVLPP-GEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDGWF---------------NTGDLGW 329
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1820002560 4926 YDADGNLVYLGR-KDSQVKLRGQRVELGEVE 4955
Cdd:cd17640    330 LTCGGELVLTGRaKDTIVLSNGENVEPQPIE 360
PRK06188 PRK06188
acyl-CoA synthetase; Validated
7598-8122 3.39e-19

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 95.82  E-value: 3.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7598 NADVPPAIERCVH--DLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAML 7675
Cdd:PRK06188     1 QATMADLLHSGATygHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7676 AVLKAGGAFVPLdpdHP-ASR--HEEIFEQTGAQV-VVASAQYSARW------TSSSCHVVTVSKA-----LSSQLPAVV 7740
Cdd:PRK06188    81 AAQLAGLRRTAL---HPlGSLddHAYVLEDAGISTlIVDPAPFVERAlallarVPSLKHVLTLGPVpdgvdLLAAAAKFG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7741 DSTNTSV-RPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFA--SYtfdACIAEIITTLLCGG 7817
Cdd:PRK06188   158 PAPLVAAaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTplSH---AGGAFFLPTLLRGG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7818 CICVPSDSDRRNSLAkAISTMDVNWAFLTPS-VARLLD-PGL----IPSLKILAIGGEQSSSAdwnRWPGSVQKI----- 7886
Cdd:PRK06188   235 TVIVLAKFDPAEVLR-AIEEQRITATFLVPTmIYALLDhPDLrtrdLSSLETVYYGASPMSPV---RLAEAIERFgpifa 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7887 HVYGPTECCIFCTgYTTKQGFEP------STIGTSVASVSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEA 7960
Cdd:PRK06188   311 QYYGQTEAPMVIT-YLRKRDHDPddpkrlTSCGRPTPGLRVALLDEDGREVAQ-GEVGEICVRGPLVMDGYWNRPEETAE 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7961 AFIDDpaWLlegypgHpgrqgrlykTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVIL 8040
Cdd:PRK06188   389 AFRDG--WL------H---------TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAE-HPAVAQVAV-IGV 449
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8041 PSGQKNHAMLAVFV-----QLGKGTHIAHLEEKAGGEDSMAQVVFLtgteEELakrlpkhmvptvffallhfPMTTSGKA 8115
Cdd:PRK06188   450 PDEKWGEAVTAVVVlrpgaAVDAAELQAHVKERKGSVHAPKQVDFV----DSL-------------------PLTALGKP 506

                   ....*..
gi 1820002560 8116 DRKRLRE 8122
Cdd:PRK06188   507 DKKALRA 513
PLN02246 PLN02246
4-coumarate--CoA ligase
5625-6137 3.70e-19

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 95.82  E-value: 3.70e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5625 HDLFTEQAKARPHAPaiCAWDGE----LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFV 5700
Cdd:PLN02246    26 HDYCFERLSEFSDRP--CLIDGAtgrvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5701 PLDPDHPASRHEDTFRHTGAQVVVTSAQHSARWIGTNH----QVVTVSAGSLGQL--STLVNPVG--LPAI---PENAVY 5769
Cdd:PLN02246   104 TANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEddgvTVVTIDDPPEGCLhfSELTQADEneLPEVeisPDDVVA 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 IMFTSGSTGIPKGVVLEHRAVVTSCW----GRGRAFGITNLSRVL----QFASYTFDACMdeiITTLMYGGCICVPSDSD 5841
Cdd:PLN02246   184 LPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFHSDDVILcvlpMFHIYSLNSVL---LCGLRVGAAILIMPKFE 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5842 rRNDLVKAISTMDVSCALLTPSVARLLEPSSV------PTLQMlVLQG-----EQVSFADWNRWPASV--QtinGYGPTE 5908
Cdd:PLN02246   261 -IGALLELIQRHKVTIAPFVPPIVLAIAKSPVvekydlSSIRM-VLSGaaplgKELEDAFRAKLPNAVlgQ---GYGMTE 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5909 C----SICCNTysGKQGF--KSGIIGTSV--ASVSwVVDPENHDRLaPLGSIGELLVEGPILARGYLNDIQKTAAVfIDD 5980
Cdd:PLN02246   336 AgpvlAMCLAF--AKEPFpvKSGSCGTVVrnAELK-IVDPETGASL-PRNQPGEICIRGPQIMKGYLNDPEATANT-IDK 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5981 PAWLlegypgHpgrqgrlykTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVE-----HhvreclPEARQLAVevil 6055
Cdd:PLN02246   411 DGWL------H---------TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEallisH------PSIADAAV---- 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6056 pSGQKDHA---MLAAFVQLEEGTqnalldkEASGEDSMA----QVVFLasveeelaKRLpeHMvptVFFsLLHFPTTTSG 6128
Cdd:PLN02246   466 -VPMKDEVageVPVAFVVRSNGS-------EITEDEIKQfvakQVVFY--------KRI--HK---VFF-VDSIPKAPSG 523

                   ....*....
gi 1820002560 6129 KTDRKRLRE 6137
Cdd:PLN02246   524 KILRKDLRA 532
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
4534-5055 4.26e-19

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 95.86  E-value: 4.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4534 DVPPAIERCVHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLK 4613
Cdd:PRK07059    16 EIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLR 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4614 AGGAFVPLDPDHPASRHEHIFRQTGAQVVLASAQYA-TLWTSLGRS----VVIVSEAS---------------------T 4667
Cdd:PRK07059    96 AGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFAtTVQQVLAKTavkhVVVASMGDllgfkghivnfvvrrvkkmvpA 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4668 SQLPVVTKTAD------------PSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLG----HGQAFGITDHTRVLQF 4731
Cdd:PRK07059   176 WSLPGHVRFNDalaegarqtfkpVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQmeawLQPAFEKKPRPDQLNF 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4732 AS----YTFDACIAEIITTLLCCGC-ICVPSDSD----------RRNNLAKAINAMdVNwALLTPSVARMLDpcvVQSLK 4796
Cdd:PRK07059   256 VCalplYHIFALTVCGLLGMRTGGRnILIPNPRDipgfikelkkYQVHIFPAVNTL-YN-ALLNNPDFDKLD---FSKLI 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4797 ILVLGGEQVNSADWDRWPKSIQT--INAYGPTECSICCTTYSGKQGFKSGTIGTSIVSVSWVVDPENHNRLaPLGSIGEL 4874
Cdd:PRK07059   331 VANGGGMAVQRPVAERWLEMTGCpiTEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDL-PLGEPGEI 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4875 LVEGPILARGYLNDMEKTEAAFIDDpawlleGYgghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEV 4954
Cdd:PRK07059   410 CIRGPQVMAGYWNRPDETAKVMTAD------GF----------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEI 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4955 EHHVREClteAKQLAVEVI-VPEGEGGYAmLAAFVqlgddtyntlVKEKaggDSLTVQVVFLDRVEEELAKRVPEHMMLT 5033
Cdd:PRK07059   474 EEVVASH---PGVLEVAAVgVPDEHSGEA-VKLFV----------VKKD---PALTEEDVKAFCKERLTNYKRPKFVEFR 536
                          570       580
                   ....*....|....*....|..
gi 1820002560 5034 TfftleAMPTTTSGKIDRKRLR 5055
Cdd:PRK07059   537 T-----ELPKTNVGKILRRELR 553
PRK09274 PRK09274
peptide synthase; Provisional
860-1260 4.52e-19

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 95.74  E-value: 4.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  860 EQARARPDASAVCAWDG----------ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAF 929
Cdd:PRK09274    14 RAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  930 VPLDPGHPASRHEEIFKQ------IG---AQVVltssqhAMLFASSE---RHQVTVSK---------VSTSQLPTVVNFA 988
Cdd:PRK09274    94 VLVDPGMGIKNLKQCLAEaqpdafIGipkAHLA------RRLFGWGKpsvRRLVTVGGrllwggttlATLLRDGAAAPFP 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  989 KSPVDPGNTAYIIFTSGTTGIPKGVVLQHR---AVTTScLGH--GEAFGYTDHARVLQFAsyTFDACIaeiittllyGGC 1063
Cdd:PRK09274   168 MADLAPDDMAAILFTSGSTGTPKGVVYTHGmfeAQIEA-LREdyGIEPGEIDLPTFPLFA--LFGPAL---------GMT 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1064 ICVPSESDRR------NNLAKAI-----STMDVNCALLTPsVARLLEPSAV--PSLKRLVLQGEQVSFADWNRW----PG 1126
Cdd:PRK09274   236 SVIPDMDPTRpatvdpAKLFAAIerygvTNLFGSPALLER-LGRYGEANGIklPSLRRVISAGAPVPIAVIERFramlPP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1127 SVQTINGYGPTE----CSVCCNTYSGKQGFKS----GI-IGTSVASLSWVVDAGNHN---------RLAPlGSIGELLVE 1188
Cdd:PRK09274   315 DAEILTPYGATEalpiSSIESREILFATRAATdngaGIcVGRPVDGVEVRIIAISDApipewddalRLAT-GEIGEIVVA 393
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 1189 GPILARGYLNDIDKTEAAFIDDpawllegyeghaGRRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRV 1260
Cdd:PRK09274   394 GPMVTRSYYNRPEATRLAKIPD------------GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
PLN02246 PLN02246
4-coumarate--CoA ligase
862-1366 4.61e-19

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 95.43  E-value: 4.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  862 ARARPDASAVCAWDGE----LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHP 937
Cdd:PLN02246    31 ERLSEFSDRPCLIDGAtgrvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYT 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  938 ASrheEIFKQI---GAQVVLTSSQHA-MLFASSERHQVTV----------------SKVSTSQLPTVVnfakspVDPGNT 997
Cdd:PLN02246   111 PA---EIAKQAkasGAKLIITQSCYVdKLKGLAEDDGVTVvtiddppegclhfselTQADENELPEVE------ISPDDV 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  998 AYIIFTSGTTGIPKGVVLQHRAVTTSCL----GHGEAFGYTDHARVL----QFASYTFDACiaeIITTLLYGGCICVPSE 1069
Cdd:PLN02246   182 VALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFHSDDVILcvlpMFHIYSLNSV---LLCGLRVGAAILIMPK 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1070 SDrRNNLAKAISTMDVNCALLTPSVARLLEPSAVP-----SLKRLVLQG-----EQVSFADWNRWPGSV--QtinGYGPT 1137
Cdd:PLN02246   259 FE-IGALLELIQRHKVTIAPFVPPIVLAIAKSPVVekydlSSIRMVLSGaaplgKELEDAFRAKLPNAVlgQ---GYGMT 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1138 EC----SVCCNTysGKQGF--KSGIIGTSV--ASLSwVVDAGNHNRLaPLGSIGELLVEGPILARGYLNDIDKTEAAfID 1209
Cdd:PLN02246   335 EAgpvlAMCLAF--AKEPFpvKSGSCGTVVrnAELK-IVDPETGASL-PRNQPGEICIRGPQIMKGYLNDPEATANT-ID 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1210 DPAWLlegyegHagrrgrlykTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIE-----HhvreclPEARQLAVevi 1284
Cdd:PLN02246   410 KDGWL------H---------TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEallisH------PSIADAAV--- 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1285 lpSGQKEHA---LLAAFIQLDKGNhnalfeeKASGEDSMA----QVVFLtgveeelaKRLpeHMVptilFTVKAMPITTS 1357
Cdd:PLN02246   466 --VPMKDEVageVPVAFVVRSNGS-------EITEDEIKQfvakQVVFY--------KRI--HKV----FFVDSIPKAPS 522

                   ....*....
gi 1820002560 1358 GKIDRKRLQ 1366
Cdd:PLN02246   523 GKILRKDLR 531
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1955-2443 6.83e-19

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 94.12  E-value: 6.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL----DPdhPASRHEdiFRQTGAQVV 2030
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLftafGP--KAIEHR--LRTSGARLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2031 VTSAQHSARwigtnhqvvtVSAGSLeqfstlvnpvdlpakpenaaYVMFTSGSTGTPKGVVLEHRAVVTscLGHGQAFGV 2110
Cdd:cd05973     77 VTDAANRHK----------LDSDPF--------------------VMMFTSGTTGLPKGVPVPLRALAA--FGAYLRDAV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2111 tNLLRALQF-------TAYTFDVCIAE-----IITTLVHGGcICVPS--DSERR---DNLAKAITdmqVNWGYLTSSVAR 2173
Cdd:cd05973    125 -DLRPEDSFwnaadpgWAYGLYYAITGplalgHPTILLEGG-FSVEStwRVIERlgvTNLAGSPT---AYRLLMAAGAEV 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2174 LLDPCLvpSLKVLVLGGEQVNS--TDWGKWPSSVQTINGYGPTECCVFCTGYTGIQG-FQSGNIGTSIASVSWVVDPENH 2250
Cdd:cd05973    200 PARPKG--RLRRVSSAGEPLTPevIRWFDAALGVPIHDHYGQTELGMVLANHHALEHpVHAGSAGRAMPGWRVAVLDDDG 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2251 GRLAPlGSIGELLVegpilargylnDVDKTqaafiddPAWLLEGY--PGHEGRQGRLYKTGDLVRYSSDGNLVCLGRKDS 2328
Cdd:cd05973    278 DELGP-GEPGRLAI-----------DIANS-------PLMWFRGYqlPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADD 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2329 QVKVRGQRVELGEVEHHMRKcLPEANQLAVeVVPPSGERDHaMLAAFIRLDDETRNSPliikyaednstaqivfltGIEE 2408
Cdd:cd05973    339 VITMSGYRIGPFDVESALIE-HPAVAEAAV-IGVPDPERTE-VVKAFVVLRGGHEGTP------------------ALAD 397
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 2409 ELS----ERLPQHMVP-TVFFaLVHFPTTTSGKTDRKRLR 2443
Cdd:cd05973    398 ELQlhvkKRLSAHAYPrTIHF-VDELPKTPSGKIQRFLLR 436
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
4536-5064 7.04e-19

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 94.83  E-value: 7.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4536 PPAiERCVHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAG 4615
Cdd:PRK06155    17 PPS-ERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLG 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4616 GAFVPLDPDHPASRHEHIFRQTGAQVVLASAQYATLWTSL------GRSVVIVSEA---------STSQLPVVTKTADP- 4679
Cdd:PRK06155    96 AIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAAdpgdlpLPAVWLLDAPasvsvpagwSTAPLPPLDAPAPAa 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4680 SVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITD-----------HTRVLqfasytfdaciAEIITTLL 4748
Cdd:PRK06155   176 AVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGAddvlyttlplfHTNAL-----------NAFFQALL 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4749 cCGCICVPS---------DSDRRNNlAKA---INAMdVNWALLTPSVARMLDpcvvQSLKILVLGGEQVNSADWDRWPKS 4816
Cdd:PRK06155   245 -AGATYVLEprfsasgfwPAVRRHG-ATVtylLGAM-VSILLSQPARESDRA----HRVRVALGPGVPAALHAAFRERFG 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4817 IQTINAYGPTECSICCTTYSGKQgfKSGTIGtSIVS--VSWVVDpeNHNRLAPLGSIGELLV---EGPILARGYLNDMEK 4891
Cdd:PRK06155   318 VDLLDGYGSTETNFVIAVTHGSQ--RPGSMG-RLAPgfEARVVD--EHDQELPDGEPGELLLradEPFAFATGYFGMPEK 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4892 TEAAFIDdpAWllegygghsgrqgrlYKTGDLVRYDADGNLVYLGR-KDSqVKLRGQRVELGEVEhhvRECLTEAKQLAV 4970
Cdd:PRK06155   393 TVEAWRN--LW---------------FHTGDRVVRDADGWFRFVDRiKDA-IRRRGENISSFEVE---QVLLSHPAVAAA 451
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4971 EVI-VPEGEGGYAMLAAFVqlgddtyntlVKEkagGDSLTVQVVfLDRVEEELAK-RVPEHMMLttfftLEAMPTTTSGK 5048
Cdd:PRK06155   452 AVFpVPSELGEDEVMAAVV----------LRD---GTALEPVAL-VRHCEPRLAYfAVPRYVEF-----VAALPKTENGK 512
                          570
                   ....*....|....*.
gi 1820002560 5049 IDRKRLREIGasFTAQ 5064
Cdd:PRK06155   513 VQKFVLREQG--VTAD 526
PRK06164 PRK06164
acyl-CoA synthetase; Validated
4548-5067 7.55e-19

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 94.81  E-value: 7.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4548 AEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMV----PLCFEksmWtVVAMLAVLKAGGAFVPLDP 4623
Cdd:PRK06164    17 DAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVavwlPNCIE---W-VVLFLACARLGATVIAVNT 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4624 DHPASRHEHIFRQTGAQVV--------------LASAQYATLWT-----------------SLGRSVVIVSEASTSQLPV 4672
Cdd:PRK06164    93 RYRSHEVAHILGRGRARWLvvwpgfkgidfaaiLAAVPPDALPPlraiavvddaadatpapAPGARVQLFALPDPAPPAA 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4673 VTKTADPsvnPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYtfdaCIAEIITTLLC--- 4749
Cdd:PRK06164   173 AGERAAD---PDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPF----CGVFGFSTLLGala 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4750 --CGCICVPS-DSDRRnnlAKAINAMDVNWALLTPSV-ARMLD----PCVVQSLKILVLGGEQVNSADWDRWPKS--IQT 4819
Cdd:PRK06164   246 ggAPLVCEPVfDAART---ARALRRHRVTHTFGNDEMlRRILDtageRADFPSARLFGFASFAPALGELAALARArgVPL 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4820 INAYGPTECsiccttysgkQGFKSGTIGTSIVSVSW--------------VVDPENhNRLAPLGSIGELLVEGPILARGY 4885
Cdd:PRK06164   323 TGLYGSSEV----------QALVALQPATDPVSVRIegggrpaspearvrARDPQD-GALLPDGESGEIEIRAPSLMRGY 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4886 LNDMEKTEAAFIDDpawlleGYgghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREC--LT 4963
Cdd:PRK06164   392 LDNPDATARALTDD------GY----------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALpgVA 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4964 EAKQLAVEVivpegeGGYAMLAAFVQLGDdtyntlvkekagGDSLTVQVVfLDRVEEELAK-RVPehmmlTTFFTLEAMP 5042
Cdd:PRK06164   456 AAQVVGATR------DGKTVPVAFVIPTD------------GASPDEAGL-MAACREALAGfKVP-----ARVQVVEAFP 511
                          570       580
                   ....*....|....*....|....*...
gi 1820002560 5043 TTTSG---KIDRKRLREIGASFTAQQLA 5067
Cdd:PRK06164   512 VTESAngaKIQKHRLREMAQARLAAERA 539
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
4531-5057 7.98e-19

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 94.89  E-value: 7.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4531 WNQDVPPAIE--------RCVHDQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQ-LGVKPEDMVPLCFEKS 4601
Cdd:PRK12492     6 WNDKRPAGVPstidlaayKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4602 MWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGA-------------QVVLA--------SAQYATLWTSL-GRSV 4659
Cdd:PRK12492    86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGAralvylnmfgklvQEVLPdtgieyliEAKMGDLLPAAkGWLV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4660 VIVSEASTSQLP------------VVTKTADPSVNP-----GNAAYAIFTSGSTGIPKGVVLEHKAVVT------SCLGH 4716
Cdd:PRK12492   166 NTVVDKVKKMVPayhlpqavpfkqALRQGRGLSLKPvpvglDDIAVLQYTGGTTGLAKGAMLTHGNLVAnmlqvrACLSQ 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4717 GQAFG---ITDHTRVL-----QFASYTFDACiaeiittllcCGCICVpsdSDRRNNLAKaiNAMDVN--------W---A 4777
Cdd:PRK12492   246 LGPDGqplMKEGQEVMiaplpLYHIYAFTAN----------CMCMMV---SGNHNVLIT--NPRDIPgfikelgkWrfsA 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4778 LL---TPSVARMLDPCVVQ----SLKILVLGGEQVNSADWDRWPK--SIQTINAYGPTECS-ICCTTYSGKQGfKSGTIG 4847
Cdd:PRK12492   311 LLglnTLFVALMDHPGFKDldfsALKLTNSGGTALVKATAERWEQltGCTIVEGYGLTETSpVASTNPYGELA-RLGTVG 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4848 TSIVSVSWVVDPENHNRLaPLGSIGELLVEGPILARGYLNDMEKTEAAfIDDPAWLlegygghsgrqgrlyKTGDLVRYD 4927
Cdd:PRK12492   390 IPVPGTALKVIDDDGNEL-PLGERGELCIKGPQVMKGYWQQPEATAEA-LDAEGWF---------------KTGDIAVID 452
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4928 ADGNLVYLGRKDSQVKLRGQRVELGEVEHHVrecLTEAKQLAVEVI-VPEGEGGYAmlaafVQLgddtyntLVKEKAGGD 5006
Cdd:PRK12492   453 PDGFVRIVDRKKDLIIVSGFNVYPNEIEDVV---MAHPKVANCAAIgVPDERSGEA-----VKL-------FVVARDPGL 517
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 5007 SLTVQVVFLDrvEEELAKRVPEHMMLTtfftlEAMPTTTSGKIDRKRLREI 5057
Cdd:PRK12492   518 SVEELKAYCK--ENFTGYKVPKHIVLR-----DSLPMTPVGKILRRELRDI 561
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
19-283 8.11e-19

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 93.69  E-value: 8.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   19 SHIPSLRILVMGGEQ-----VNSAdWDRWPSSVQTINGYGPTECCIVCTGYTSEQDFTTGTIGTSI-ASVSWVVDPKDHG 92
Cdd:cd17654    235 SATSSLRVLALGGEPfpslvILSS-WRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLlGTVIEVRDQNGSE 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   93 rlaplgSVGELLVEGPILaRGYLSDPEKTAavfinnpawlleghggyagrQGRLYKTGDLVRYDaDGNLVCLGRKDSQVK 172
Cdd:cd17654    314 ------GTGQVFLGGLNR-VCILDDEVTVP--------------------KGTMRATGDFVTVK-DGELFFLGRKDSQIK 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  173 LRGQRVELGEVEHHVRECLPEakqLAVEVVLPLGQKnhatLAAFI---QLDKGTHNALLKEKvggddsiarvvflagvee 249
Cdd:cd17654    366 RRGKRINLDLIQQVIESCLGV---ESCAVTLSDQQR----LIAFIvgeSSSSRIHKELQLTL------------------ 420
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1820002560  250 elakrLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd17654    421 -----LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
5770-6132 9.17e-19

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 91.94  E-value: 9.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 IMFTSGSTGIPKGVVLEHRAVVTSCWGRGRA-FGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRNDLVK 5848
Cdd:cd17635      6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKSLFK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5849 AISTMDVSCALLTPSVARLLEP------SSVPTLQMLVLQGE-----QVSFADWNRwpaSVQTINGYGPTECSICCNTYS 5917
Cdd:cd17635     86 ILTTNAVTTTCLVPTLLSKLVSelksanATVPSLRLIGYGGSraiaaDVRFIEATG---LTNTAQVYGLSETGTALCLPT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5918 GKQGFKSGIIGTSVASVSwvVDPENHDRLA-PLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpaWLlegypghpgrqg 5996
Cdd:cd17635    163 DDDSIEINAVGRPYPGVD--VYLAATDGIAgPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG--WV------------ 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5997 rlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhHVRECLPEARQLAVEVIlpsgqkDHAMLAAFVQLEEgTQ 6076
Cdd:cd17635    227 ---NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECACYEI------SDEEFGELVGLAV-VA 295
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6077 NALLDKEAsgedsmaqvvfLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDR 6132
Cdd:cd17635    296 SAELDENA-----------IRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
7186-7402 9.37e-19

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 89.71  E-value: 9.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7186 SPLQEGLISLTAKRAgDYIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSElGLLQVVVEE-KIQWT------ 7258
Cdd:COG4908      2 SPAQKRFLFLEPGSN-AYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDG-EPVQRIDPDaDLPLEvvdlsa 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7259 -----ESEALEEYLKEDKAVSMGLG-DPLAHYALVKEAWGGKRwFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQP- 7331
Cdd:COG4908     80 lpepeREAELEELVAEEASRPFDLArGPLLRAALIRLGEDEHV-LLLTIHHIISDGWSLGILLRELAALYAALLEGEPPp 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7332 ------SFNAFI----QYLGQQDLEATAAYWQTALSDCEAVL-FP---PLPSTVTQPVADTTVeyqcpplskaTLDTTTS 7397
Cdd:COG4908    159 lpelpiQYADYAawqrAWLQSEALEKQLEYWRQQLAGAPPVLeLPtdrPRPAVQTFRGATLSF----------TLPAELT 228

                   ....*
gi 1820002560 7398 TLIRA 7402
Cdd:COG4908    229 EALKA 233
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
23-286 1.05e-18

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 94.41  E-value: 1.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRWPSSVQT--INGYGPTECCIVCTGYTSEQDFTTGTIGT-----SIAsvswVVDpkDHGRLA 95
Cdd:COG0365    307 SLRLLGSAGEPLNPEVWEWWYEAVGVpiVDGWGQTETGGIFISNLPGLPVKPGSMGKpvpgyDVA----VVD--EDGNPV 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   96 PLGSVGELLVEGPI--LARGYLSDPEKTAAVFinnpawllegHGGYAGrqgrLYKTGDLVRYDADGNLVCLGRKDSQVKL 173
Cdd:COG0365    381 PPGEEGELVIKGPWpgMFRGYWNDPERYRETY----------FGRFPG----WYRTGDGARRDEDGYFWILGRSDDVINV 446
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  174 RGQRVELGEVE-----HH-VREClpeakqlAVeVVLPLGQKNHAtLAAFIQldkgthnalLKEKVGGDDSIARVVFlagv 247
Cdd:COG0365    447 SGHRIGTAEIEsalvsHPaVAEA-------AV-VGVPDEIRGQV-VKAFVV---------LKPGVEPSDELAKELQ---- 504
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1820002560  248 eEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREI 286
Cdd:COG0365    505 -AHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKI 542
PRK07788 PRK07788
acyl-CoA synthetase; Validated
3471-3977 1.07e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 94.22  E-value: 1.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 3550
Cdd:PRK07788    59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3551 EEIFEQTGAQVVVASAQYSA----------RWTSSSCHVVTVSKALSS--QLPAVVDSTNTSVRP---ENAAYIIFTSGS 3615
Cdd:PRK07788   139 AEVAAREGVKALVYDDEFTDllsalppdlgRLRAWGGNPDDDEPSGSTdeTLDDLIAGSSTAPLPkppKPGGIVILTSGT 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3616 TGVPKGVVLEHravaTSCLGHGRAFgitnLSRV-------LQFASYTFDA---CIAEIITTLlcGGCICVPSDSDRRNSL 3685
Cdd:PRK07788   219 TGTPKGAPRPE----PSPLAPLAGL----LSRVpfragetTLLPAPMFHAtgwAHLTLAMAL--GSTVVLRRRFDPEATL 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3686 AkAISTMDVNWAFLTPS-VARLLDpgLIP---------SLKILAIGGEQSSsadwnrwPGSVQKIH---------VYGPT 3746
Cdd:PRK07788   289 E-DIAKHKATALVVVPVmLSRILD--LGPevlakydtsSLKIIFVSGSALS-------PELATRALeafgpvlynLYGST 358
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3747 ECCiFCTGYTTKQ-GFEPSTIGTSVASVSWVVDPENHNRLaPLGSMGEllmegpILARGYLndvdkteaafiddpawLLE 3825
Cdd:PRK07788   359 EVA-FATIATPEDlAEAPGTVGRPPKGVTVKILDENGNEV-PRGVVGR------IFVGNGF----------------PFE 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3826 GY--PGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVevilpSGQKDHAM 3903
Cdd:PRK07788   415 GYtdGRDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVE-DLLAGHPDVVEAAV-----IGVDDEEF 488
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 3904 ---LAAFVQLEEGTQnalLDKEAggedsmaqvvflasVEEELAKRLPEHMVP--TVFFSLLhfPTTTSGKTDRKRLREI 3977
Cdd:PRK07788   489 gqrLRAFVVKAPGAA---LDEDA--------------IKDYVRDNLARYKVPrdVVFLDEL--PRNPTGKVLKRELREM 548
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1933-2444 1.11e-18

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 94.18  E-value: 1.11e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDGE--LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 2010
Cdd:PRK05852    20 DLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLD 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2011 PDHPASRHEDIFRQTGAQVVVTS-------AQHSARWIGTnhqVVTVSAGSLEQFSTLVNPVDLPAKPENA--------- 2074
Cdd:PRK05852   100 PALPIAEQRVRSQAAGARVVLIDadgphdrAEPTTRWWPL---TVNVGGDSGPSGGTLSVHLDAATEPTPAtstpeglrp 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2075 --AYVMFTSGSTGTPKGVVLEHRAVVTSC--------LGHGQAFGVTNLLralqftaYTFDVCIAEIITTLVHGGCICVP 2144
Cdd:PRK05852   177 ddAMIMFTGGTTGLPKMVPWTHANIASSVraiitgyrLSPRDATVAVMPL-------YHGHGLIAALLATLASGGAVLLP 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2145 SDSE-RRDNLAKAITDMQVNWGYLTSSVARLL--------DPCLVPSLKVlvlggeqVNSTDWGKWPSSVQT-------- 2207
Cdd:PRK05852   250 ARGRfSAHTFWDDIKAVGATWYTAVPTIHQILleraatepSGRKPAALRF-------IRSCSAPLTAETAQAlqtefaap 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2208 -INGYGPTECCVFCTGyTGIQGF--------QSGNIGTSIASVSWVVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVD 2278
Cdd:PRK05852   323 vVCAFGMTEATHQVTT-TQIEGIgqtenpvvSTGLVGRSTGAQIRIVGSD--GLPLPAGAVGEVWLRGTTVVRGYLGDPT 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2279 KTQAAFIDdpAWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKClPEANQLAV 2358
Cdd:PRK05852   400 ITAANFTD--GWL---------------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASH-PNVMEAAV 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2359 EVVPPS--GERDHAmlaafirlddetrnspLIIKYAEDNSTAQivfltGIEEELSERLPQHMVPTVFFALVHFPTTTSGK 2436
Cdd:PRK05852   462 FGVPDQlyGEAVAA----------------VIVPRESAPPTAE-----ELVQFCRERLAAFEIPASFQEASGLPHTAKGS 520

                   ....*...
gi 1820002560 2437 TDRKRLRE 2444
Cdd:PRK05852   521 LDRRAVAE 528
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
5624-6137 1.13e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 94.44  E-value: 1.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5624 VHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQL-GVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL 5702
Cdd:PRK05677    26 IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNT 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5703 DPDHPASRHEDTFRHTGAQVVVTSAQ--HSARWI----GTNHQVVTVSAGSLGQLS-TLVNPV-----------GLP-AI 5763
Cdd:PRK05677   106 NPLYTAREMEHQFNDSGAKALVCLANmaHLAEKVlpktGVKHVIVTEVADMLPPLKrLLINAVvkhvkkmvpayHLPqAV 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5764 PENAVY--------------------IMFTSGSTGIPKGVVLEHR----------AVVTSCWGRGRAFGITNLSrVLQFA 5813
Cdd:PRK05677   186 KFNDALakgagqpvteanpqaddvavLQYTGGTTGVAKGAMLTHRnlvanmlqcrALMGSNLNEGCEILIAPLP-LYHIY 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5814 SYTFDaCMdeiITTLMYGGCICVPSDSDRRNdLVKAISTMDVS--CALLTPSVA-------RLLEPSSvptLQMLVLQGE 5884
Cdd:PRK05677   265 AFTFH-CM---AMMLIGNHNILISNPRDLPA-MVKELGKWKFSgfVGLNTLFVAlcnneafRKLDFSA---LKLTLSGGM 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5885 QVSFADWNRWPA--SVQTINGYGPTECS--ICCNTYSGKQgfkSGIIGTSVASVSW-VVDPENHDrlAPLGSIGELLVEG 5959
Cdd:PRK05677   337 ALQLATAERWKEvtGCAICEGYGMTETSpvVSVNPSQAIQ---VGTIGIPVPSTLCkVIDDDGNE--LPLGEVGELCVKG 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5960 PILARGYLNDIQKTAAVFiDDPAWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhHV 6039
Cdd:PRK05677   412 PQVMKGYWQRPEATDEIL-DSDGWL---------------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELE-DV 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6040 RECLPEARQLAveVILPSGQKDHAMLAAFVQLEEGtqnALLDKEAsgedsmaqvvflasVEEELAKRLPEHMVPTVFFSL 6119
Cdd:PRK05677   475 LAALPGVLQCA--AIGVPDEKSGEAIKVFVVVKPG---ETLTKEQ--------------VMEHMRANLTGYKVPKAVEFR 535
                          570
                   ....*....|....*...
gi 1820002560 6120 LHFPTTTSGKTDRKRLRE 6137
Cdd:PRK05677   536 DELPTTNVGKILRRELRD 553
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
854-1363 1.17e-18

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 94.48  E-value: 1.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVcAWDGE------LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGG 927
Cdd:cd05968     63 VEQLLDKWLADTRTRPAL-RWEGEdgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  928 AFVPL----DPGHPASRHE----------EIFKQIGAQVVLT-SSQHAMLFASSERHQVTVSKVSTSQLPTVVNFAKSP- 991
Cdd:cd05968    142 IVVPIfsgfGKEAAATRLQdaeakalitaDGFTRRGREVNLKeEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDe 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  992 -----------VDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSC---------LGHGE-AFGYTDHARV----LQFASYT 1046
Cdd:cd05968    222 eketagdgaerTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAaqdmyfqfdLKPGDlLTWFTDLGWMmgpwLIFGGLI 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1047 FDAciaeiiTTLLYGGcicVPsESDRRNNLAKAISTMDVNCALLTPSVARLL-----EPSAVPSLKRLVLQGEQVSFADW 1121
Cdd:cd05968    302 LGA------TMVLYDG---AP-DHPKADRLWRMVEDHEITHLGLSPTLIRALkprgdAPVNAHDLSSLRVLGSTGEPWNP 371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1122 NRWPGSVQTIngyGPTECSVCcnTYSGKQGFKSGIIG-------------TSVASLSWVV--DAGNHNRlaplGSIGELL 1186
Cdd:cd05968    372 EPWNWLFETV---GKGRNPII--NYSGGTEISGGILGnvlikpikpssfnGPVPGMKADVldESGKPAR----PEVGELV 442
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1187 VEGPI--LARGylndidkteaaFIDDPAWLLEGYeghAGRRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGE 1264
Cdd:cd05968    443 LLAPWpgMTRG-----------FWRDEDRYLETY---WSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAE 508
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1265 IE------HHVREClpearqLAVEVILP-SGQKEHallaAFIQLDKGnhnalfeekasgedsmaqVVFLTGVEEELAKRL 1337
Cdd:cd05968    509 IEsvlnahPAVLES------AAIGVPHPvKGEAIV----CFVVLKPG------------------VTPTEALAEELMERV 560
                          570       580       590
                   ....*....|....*....|....*....|
gi 1820002560 1338 PEHM----VPTILFTVKAMPITTSGKIDRK 1363
Cdd:cd05968    561 ADELgkplSPERILFVKDLPKTRNAKVMRR 590
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
5648-6138 1.19e-18

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 93.34  E-value: 1.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL----DPDHPASRHEDTfrhtGAQVV 5723
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLfsafGPEAIRDRLENS----EAKVL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5724 VTSAQHSARwigtnhqvvtvsagslgqlstlvnpvglpAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTScWGRGRafgi 5803
Cdd:cd05969     77 ITTEELYER-----------------------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFY-YFTGK---- 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5804 tnlsrvlqfasYTFDACMDEI---------ITTLMYG-------GCICVpSDSDR--RNDLVKAISTMDVSCALLTPSVA 5865
Cdd:cd05969    123 -----------YVLDLHPDDIywctadpgwVTGTVYGiwapwlnGVTNV-VYEGRfdAESWYGIIERVKVTVWYTAPTAI 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5866 RLLEPSSV--------PTLQMLVLQGEQVSfADWNRWPASVQTI---NGYGPTEC-SICCNTYSGkQGFKSGIIGTSVAS 5933
Cdd:cd05969    191 RMLMKEGDelarkydlSSLRFIHSVGEPLN-PEAIRWGMEVFGVpihDTWWQTETgSIMIANYPC-MPIKPGSMGKPLPG 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5934 VSWVVDPENHDRLAPlGSIGELLVEG--PILARGYLNDIQKTAAVFIDdpawlleGYpghpgrqgrlYKTGDLVRYDANG 6011
Cdd:cd05969    269 VKAAVVDENGNELPP-GTKGILALKPgwPSMFRGIWNDEERYKNSFID-------GW----------YLTGDLAYRDEDG 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6012 NLVCLGRKDSQVKLRGQRVELGEVEhhvrECLPEARQLA-VEVIlpsGQKD---HAMLAAFVQLEEGTqnalldkEASGE 6087
Cdd:cd05969    331 YFWFVGRADDIIKTSGHRVGPFEVE----SALMEHPAVAeAGVI---GKPDplrGEIIKAFISLKEGF-------EPSDE 396
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 6088 dsmaqvvflasVEEELAKRLPEHMVPTVFFSLLHF----PTTTSGKTDRKRLREI 6138
Cdd:cd05969    397 -----------LKEEIINFVRQKLGAHVAPREIEFvdnlPKTRSGKIMRRVLKAK 440
PRK06164 PRK06164
acyl-CoA synthetase; Validated
5626-6148 1.35e-18

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 94.04  E-value: 1.35e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMV----PLCFEksmWtVVAMLAVLKAGGAFVP 5701
Cdd:PRK06164    14 SLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVavwlPNCIE---W-VVLFLACARLGATVIA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5702 LDPDHPASRHEDTFRHTGAQVVV---------------------------------TSAQHSARWIGTNHQVVTVSAGSL 5748
Cdd:PRK06164    90 VNTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailaavppdalpplraiavvddAADATPAPAPGARVQLFALPDPAP 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5749 GQLStlvnpvGLPAIPENAVYIMFT-SGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITT 5827
Cdd:PRK06164   170 PAAA------GERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGA 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5828 LMYGG-CICVPS-DSDRRndlVKAISTMDVSCALLTPSVARLL-----EPSSVPTLQMLvlqgeqvSFAD----WNRWPA 5896
Cdd:PRK06164   244 LAGGApLVCEPVfDAART---ARALRRHRVTHTFGNDEMLRRIldtagERADFPSARLF-------GFASfapaLGELAA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5897 SVQT----ING-YGPTECsiccntysgkQGFKSGIIGTSVASVSW--------------VVDPENhDRLAPLGSIGELLV 5957
Cdd:PRK06164   314 LARArgvpLTGlYGSSEV----------QALVALQPATDPVSVRIegggrpaspearvrARDPQD-GALLPDGESGEIEI 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5958 EGPILARGYLNDIQKTAAVFIDDpawlleGYpghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEH 6037
Cdd:PRK06164   383 RAPSLMRGYLDNPDATARALTDD------GY----------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEH 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6038 HVREClPEARQLAVEVILPSGQkdhAMLAAFVQLEEGTQnalldkeASGEDSMAQvvflasveeeLAKRLPEHMVPTVFF 6117
Cdd:PRK06164   447 ALEAL-PGVAAAQVVGATRDGK---TVPVAFVIPTDGAS-------PDEAGLMAA----------CREALAGFKVPARVQ 505
                          570       580       590
                   ....*....|....*....|....*....|....
gi 1820002560 6118 SLLHFPTTTSG---KTDRKRLREIGASFTAQQIA 6148
Cdd:PRK06164   506 VVEAFPVTESAngaKIQKHRLREMAQARLAAERA 539
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
1945-2443 1.47e-18

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 92.93  E-value: 1.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1945 APAICAWDGELTYGELDALSSKLASHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFR 2023
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2024 QTGAQVVVTSAQHSARwigtnhqvvtvsagsleqfstlvnpvdlpakpENAAYVMFTSGSTGTPKGVVLEHRAVVTSClg 2103
Cdd:cd05958     81 KARITVALCAHALTAS--------------------------------DDICILAFTSGTTGAPKATMHFHRDPLASA-- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2104 hgQAFGVtNLLR--------ALQFTAYTFDVCIAEIITTLVHGGCICVPSDSErrDNLAKAITDMQ----VNWGYLTSSV 2171
Cdd:cd05958    127 --DRYAV-NVLRlreddrfvGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATP--DLLLSAIARYKptvlFTAPTAYRAM 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2172 ARLLDPC--LVPSLKVLVLGGEQVNSTDWGKWPSS--VQTINGYGPTECC-VFCTGYTGiqGFQSGNIGTSIASV-SWVV 2245
Cdd:cd05958    202 LAHPDAAgpDLSSLRKCVSAGEALPAALHRAWKEAtgIPIIDGIGSTEMFhIFISARPG--DARPGATGKPVPGYeAKVV 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2246 DPEnhGRLAPLGSIGELLVEGPIlarGYLNDVDKTQAAFIDDpAWLLegypghegrqgrlykTGDLVRYSSDGNLVCLGR 2325
Cdd:cd05958    280 DDE--GNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQG-GWNI---------------TGDTYSRDPDGYFRHQGR 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2326 KDSQVKVRGQRVELGEVEhhmrKCL---PEANQLAVeVVPPSGERDhAMLAAFIRLDDETRNSPLIIkyaednstaqivf 2402
Cdd:cd05958    339 SDDMIVSGGYNIAPPEVE----DVLlqhPAVAECAV-VGHPDESRG-VVVKAFVVLRPGVIPGPVLA------------- 399
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 2403 ltgieEELSERLPQHMVPTVFFALVHF----PTTTSGKTDRKRLR 2443
Cdd:cd05958    400 -----RELQDHAKAHIAPYKYPRAIEFvtelPRTATGKLQRFALR 439
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
3487-3975 1.53e-18

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 92.79  E-value: 1.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP----LDPDHPASRheeiFEQTGAQVV 3562
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPlttlLGPKDIEYR----LEAAGAKAI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3563 VASAqysarwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVLEHRAVatscLGHGR-AFG 3641
Cdd:cd05972     77 VTDA-------------------------------------EDPALIYFTSGTTGLPKGVLHTHSYP----LGHIPtAAY 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3642 ITNLSRV-----------LQFASYTFDACIAEIITTLLCGGCICVPsdsdrRNSLaKAISTMDVNWAFLTPSVARLL--- 3707
Cdd:cd05972    116 WLGLRPDdihwniadpgwAKGAWSSFFGPWLLGATVFVYEGPRFDA-----ERIL-ELLERYGVTSFCGPPTAYRMLikq 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3708 --DPGLIPSLKILAIGGEQSSSADWNRWPGSVQ-KIH-VYGPTECCIFCTGYTTkQGFEPSTIGTSVASVSWVVDPENHN 3783
Cdd:cd05972    190 dlSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGlPIRdGYGQTETGLTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGR 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3784 RLAPlGSMGEL-LMEGPI-LARGYLNDVDKTEAAFIDDpaWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQ 3861
Cdd:cd05972    269 ELPP-GEEGDIaIKLPPPgLFLGYVGDPEKTEASIRGD--Y---------------YLTGDRAYRDEDGYFWFVGRADDI 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3862 VKVRGQRVELGEVEHHVREcLPEARQLAVeVILPS---GQkdhaMLAAFVQLEEGtqnalldkeAGGEDSMAqvvflasv 3938
Cdd:cd05972    331 IKSSGYRIGPFEVESALLE-HPAVAEAAV-VGSPDpvrGE----VVKAFVVLTSG---------YEPSEELA-------- 387
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 3939 eEELA----KRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd05972    388 -EELQghvkKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
7633-8121 1.59e-18

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 92.97  E-value: 1.59e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdhpasrheeiFEQTGAQVVvasa 7712
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPL------------FTAFGPKAI---- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7713 qySARWTSSSCHVVtvskalssqlpaVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLS 7792
Cdd:cd05973     65 --EHRLRTSGARLV------------VTDAANRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7793 RVLQFAS--------YTFDACIAEIITTLLCGGCICVPSDSDrrnslakAISTMDVNWAFLTPSVARLLDPGLIPSLKIL 7864
Cdd:cd05973    131 SFWNAADpgwayglyYAITGPLALGHPTILLEGGFSVESTWR-------VIERLGVTNLAGSPTAYRLLMAAGAEVPARP 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7865 AIGGEQSSSA------DWNRWPGSVQKIHV---YGPTECCIF-CTGYTTKQGFEPSTIGTSVASVSWVVDPENHNRLAPl 7934
Cdd:cd05973    204 KGRLRRVSSAgepltpEVIRWFDAALGVPIhdhYGQTELGMVlANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGP- 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7935 GSMGELLMegpilargylnDVDKTeaafiddPAWLLEGY--PGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRG 8012
Cdd:cd05973    283 GEPGRLAI-----------DIANS-------PLMWFRGYqlPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSG 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8013 QRVELGEVEHHVREcLPEARQLAVeVILPSGQKNHAMLAvFVQLGKGThiahlEEKAGGEDSMAQVVfltgteeelAKRL 8092
Cdd:cd05973    345 YRIGPFDVESALIE-HPAVAEAAV-IGVPDPERTEVVKA-FVVLRGGH-----EGTPALADELQLHV---------KKRL 407
                          490       500       510
                   ....*....|....*....|....*....|
gi 1820002560 8093 PKHMVP-TVFFaLLHFPMTTSGKADRKRLR 8121
Cdd:cd05973    408 SAHAYPrTIHF-VDELPKTPSGKIQRFLLR 436
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
4690-5051 1.60e-18

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 91.17  E-value: 1.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4690 IFTSGSTGIPKGVVLEHKAVVTS---CLGHGQAFGITDHTRVLQFASYTFDacIAEIITTLLCCGCICVPSDSDRRNNLA 4766
Cdd:cd17635      7 IFTSGTTGEPKAVLLANKTFFAVpdiLQKEGLNWVVGDVTYLPLPATHIGG--LWWILTCLIHGGLCVTGGENTTYKSLF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4767 KAINAMDVNWALLTPS----VARMLDPCV--VQSLKILVLGGEQVNSAD--WDRWPKSIQTINAYGPTECSICCTTYSGK 4838
Cdd:cd17635     85 KILTTNAVTTTCLVPTllskLVSELKSANatVPSLRLIGYGGSRAIAADvrFIEATGLTNTAQVYGLSETGTALCLPTDD 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4839 QGFKSGTIGTSIVSVSWVVdPENHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpaWLlegygghsgrqgrly 4918
Cdd:cd17635    165 DSIEINAVGRPYPGVDVYL-AATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG--WV--------------- 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4919 KTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhHVRECLTEAKQLAVEVIvPEGEGGYAMLAAFVQLGDDTYNTL 4998
Cdd:cd17635    227 NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECACYEI-SDEEFGELVGLAVVASAELDENAI 304
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 4999 VKEKaggdsltvqvvfldrveEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDR 5051
Cdd:cd17635    305 RALK-----------------HTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
3487-3977 1.71e-18

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 93.89  E-value: 1.71e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD--PDHPASRHEE-----IFEQTGA 3559
Cdd:cd05906     40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvpPTYDEPNARLrklrhIWQLLGS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3560 QVVVASAQ---------YSARWTSSSCHVVTVSKALSSQLPAVVdstntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVA 3630
Cdd:cd05906    120 PVVLTDAElvaefagleTLSGLPGIRVLSIEELLDTAADHDLPQ------SRPDDLALLMLTSGSTGFPKAVPLTHRNIL 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3631 TSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGC--ICVPSDSDRRNSLA--KAIST--MDVNWA--FLTPS 3702
Cdd:cd05906    194 ARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCqqVHVPTEEILADPLRwlDLIDRyrVTITWApnFAFAL 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3703 VARLLD-----PGLIPSLKILAIGGEQSSSADWNRWPGSVQK-------IH-VYGPTECC---IFCTG---YTTKQGFEP 3763
Cdd:cd05906    274 LNDLLEeiedgTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPyglppdaIRpAFGMTETCsgvIYSRSfptYDHSQALEF 353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3764 STIGTSVASVSW-VVDPEnhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpAWllegypghpgrqgrlYKTGD 3842
Cdd:cd05906    354 VSLGRPIPGVSMrIVDDE--GQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED-GW---------------FRTGD 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3843 LvQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQ---LAVEVILPSGQKDHamLAAFVQLEEGTQNALL 3919
Cdd:cd05906    416 L-GFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEE-VPGVEPsftAAFAVRDPGAETEE--LAIFFVPEYDLQDALS 491
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3920 DKEAGGEDSMAQVVFLAsveeelakrlPEHMVPtvffsLLH--FPTTTSGKTDRKRLREI 3977
Cdd:cd05906    492 ETLRAIRSVVSREVGVS----------PAYLIP-----LPKeeIPKTSLGKIQRSKLKAA 536
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
3775-4068 1.73e-18

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 90.19  E-value: 1.73e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3775 WVVDPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAwlleGYPGHPGRQGRLYKTGDLVQYNADGNLVY 3854
Cdd:COG3433     23 AIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPF----IPVPYPAQPGRQADDLRLLLRRGLGPGGG 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3855 LGRkdsQVKVRGQRVELGEVEHHVRECLPEARQLAVEvilpsgqkdhamlaafvqLEEGTQNALLDKEAGGEDSMAQVvf 3934
Cdd:COG3433     99 LER---LVQQVVIRAERGEEEELLLVLRAAAVVRVAV------------------LAALRGAGVGLLLIVGAVAALDG-- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3935 lASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGASFTAQQLAEmrTSSQGPKRQPSTEAEqtMQQLWAQ 4014
Cdd:COG3433    156 -LAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAA--ASPAPALETALTEEE--LRADVAE 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 4015 VLSLGADIIGLDDSFFRLGGDSIAAMKLVGEARRMGLHLSVADIFRHPKLADFA 4068
Cdd:COG3433    231 LLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWW 284
PRK09274 PRK09274
peptide synthase; Provisional
1935-2337 1.74e-18

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 93.81  E-value: 1.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1935 FTEQAKARPHAPAICAWDG----------ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGG 2004
Cdd:PRK09274    12 LPRAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2005 AFVPLDPDHPASRHEDIFRQTGAQVVVTSAQ-HSARWI-----GTNHQVVTVSAG------SLEQFSTLVNPVDLP---A 2069
Cdd:PRK09274    92 VPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKaHLARRLfgwgkPSVRRLVTVGGRllwggtTLATLLRDGAAAPFPmadL 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2070 KPENAAYVMFTSGSTGTPKGVVLEHR---AVVTScLGH--GQAFGVTNL----LRALqftaytFDVCIaeiittlvhGGC 2140
Cdd:PRK09274   172 APDDMAAILFTSGSTGTPKGVVYTHGmfeAQIEA-LREdyGIEPGEIDLptfpLFAL------FGPAL---------GMT 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2141 ICVP---------SDSERrdnLAKAITDMQVNwgylTSSVA-----RLLDPCL-----VPSLKVLVLGGEQVNSTDWGKW 2201
Cdd:PRK09274   236 SVIPdmdptrpatVDPAK---LFAAIERYGVT----NLFGSpalleRLGRYGEangikLPSLRRVISAGAPVPIAVIERF 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2202 ----PSSVQTINGYGPTECCVFCT-------GYTGIQGFQSGNI--GTSIASVSWVV-----DPENH---GRLAPLGSIG 2260
Cdd:PRK09274   309 ramlPPDAEILTPYGATEALPISSiesreilFATRAATDNGAGIcvGRPVDGVEVRIiaisdAPIPEwddALRLATGEIG 388
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 2261 ELLVEGPILARGYLNDVDKTQAAFIDDPAwllegyPGHEGRqgrlykTGDLVRYSSDGNLVCLGRKDSQVKVRGQRV 2337
Cdd:PRK09274   389 EIVVAGPMVTRSYYNRPEATRLAKIPDGQ------GDVWHR------MGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
3604-3971 1.77e-18

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 91.17  E-value: 1.77e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3604 ENAAYIIFTSGSTGVPKGVVLEHR---AVATSCLGHGRAFGITNLSRVLQFASYTFDacIAEIITTLLCGGCICVPSDSD 3680
Cdd:cd17635      1 EDPLAVIFTSGTTGEPKAVLLANKtffAVPDILQKEGLNWVVGDVTYLPLPATHIGG--LWWILTCLIHGGLCVTGGENT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3681 RRNSLAKAISTMDVNWAFLTPSVARLLDPGL------IPSLKILAIGGEQSSSADWN--RWPGSVQKIHVYGPTECCIFC 3752
Cdd:cd17635     79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELksanatVPSLRLIGYGGSRAIAADVRfiEATGLTNTAQVYGLSETGTAL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3753 TGYTTKQGFEPSTIGTSVASVSWVVdPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLlegypghpg 3832
Cdd:cd17635    159 CLPTDDDSIEINAVGRPYPGVDVYL-AATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG--WV--------- 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3833 rqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVEVIlpsgqkDHAMLAAFVQLEE 3912
Cdd:cd17635    227 ------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECACYEI------SDEEFGELVGLAV 293
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 3913 gTQNALLDKEAggedsmaqvvfLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDR 3971
Cdd:cd17635    294 -VASAELDENA-----------IRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
7633-8123 1.84e-18

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 92.57  E-value: 1.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL----DPDHPASRheeiFEQTGAQVV 7708
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLfsafGPEAIRDR----LENSEAKVL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7709 VASAQYSARWTssschvvtvskalssqlpavvdstntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGhgrafgi 7788
Cdd:cd05969     77 ITTEELYERTD-----------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFT------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7789 tnlsrvlqfASYTFDA-------CIAE----------IITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFLTPSVAR 7851
Cdd:cd05969    121 ---------GKYVLDLhpddiywCTADpgwvtgtvygIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIR 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7852 LL-DPGLIP-------SLKILAIGGEqSSSADWNRWPGSVQK--IH-VYGPTECCIFCTGYTTKQGFEPSTIGTSVASVS 7920
Cdd:cd05969    192 MLmKEGDELarkydlsSLRFIHSVGE-PLNPEAIRWGMEVFGvpIHdTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVK 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7921 WVVDPENHNRLAPlGSMGELLMEG--PILARGYLNDVDKTEAAFIDdpawlleGYpghpgrqgrlYKTGDLVQYNADGNL 7998
Cdd:cd05969    271 AAVVDENGNELPP-GTKGILALKPgwPSMFRGIWNDEERYKNSFID-------GW----------YLTGDLAYRDEDGYF 332
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7999 VYLGRKDSQVKVRGQRVELGEVEhhvreclpearqlavevilpSGQKNHAMLAVFVQLGKgthiahlEEKAGGEDSMAQV 8078
Cdd:cd05969    333 WFVGRADDIIKTSGHRVGPFEVE--------------------SALMEHPAVAEAGVIGK-------PDPLRGEIIKAFI 385
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 8079 VFLTGTE------EELAKRLPKHMVPTVFFALLHF----PMTTSGKADRKRLREI 8123
Cdd:cd05969    386 SLKEGFEpsdelkEEIINFVRQKLGAHVAPREIEFvdnlPKTRSGKIMRRVLKAK 440
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
46-255 1.89e-18

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 92.66  E-value: 1.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   46 VQTINGYGPTECCIVCTgYTSEQDFTTGTIGTSIasvswvvdPKDHGRLAPlgsVGELLVEGPILARGYLSDPEKTAAVF 125
Cdd:cd05907    236 IPVYEGYGLTETSAVVT-LNPPGDNRIGTVGKPL--------PGVEVRIAD---DGEILVRGPNVMLGYYKNPEATAEAL 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  126 INNPaWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGR-KDSQVKLRGQRVELGEVEHHVREClpeakqLAVEVVLP 204
Cdd:cd05907    304 DADG-WL---------------HTGDLGEIDEDGFLHITGRkKDLIITSGGKNISPEPIENALKAS------PLISQAVV 361
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  205 LGQKNHAtLAAFIQLDKGTHNALLKEKVGGDDSIARVVFLAGVEEELAKRL 255
Cdd:cd05907    362 IGDGRPF-LVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRAEIEAAV 411
PRK05857 PRK05857
fatty acid--CoA ligase;
1922-2343 1.89e-18

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 93.53  E-value: 1.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1922 EVPPAI-ERCVhdlftEQAKARPHAPAICAWDG--ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLA 1998
Cdd:PRK05857    11 QLPSTVlDRVF-----EQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1999 VLKAGGAFVPLDPDHPA---SRHEDIFRQTGAQVVVTSAQHSARWIGTNHQV--VTVSAGSLEQFSTLVNPVDLPAK--- 2070
Cdd:PRK05857    86 CAKLGAIAVMADGNLPIaaiERFCQITDPAAALVAPGSKMASSAVPEALHSIpvIAVDIAAVTRESEHSLDAASLAGnad 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2071 --PENAAYVMFTSGSTGTPKGVVLEHRAVvtsclghgqaFGVTNLLRA--LQFTAY-----TFDVCIAE-------IITT 2134
Cdd:PRK05857   166 qgSEDPLAMIFTSGTTGEPKAVLLANRTF----------FAVPDILQKegLNWVTWvvgetTYSPLPAThigglwwILTC 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2135 LVHGG-CIcvpSDSERRDNLAKAITDMQVNWG-----YLTSSVARL-LDPCLVPSLKVLVLGGEQVNSTDWGKWPSS-VQ 2206
Cdd:PRK05857   236 LMHGGlCV---TGGENTTSLLEILTTNAVATTclvptLLSKLVSELkSANATVPSLRLVGYGGSRAIAADVRFIEATgVR 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2207 TINGYGPTE--CCVFC--TGYTGIQGFQSGNIGTSIASVSWVVDPENHG-----RLAPLGSIGELLVEGPILARGYLNDV 2277
Cdd:PRK05857   313 TAQVYGLSEtgCTALClpTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIgptapGAGPSASFGTLWIKSPANMLGYWNNP 392
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 2278 DKTQAAFIDdpAWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVE 2343
Cdd:PRK05857   393 ERTAEVLID--GWV---------------NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD 441
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
4551-4930 2.05e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 93.49  E-value: 2.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAICAWDGELTYGELDTLSSKLASHLVQ-LGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 4629
Cdd:PRK08314    20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4630 HEHIFRQTGAQVVLASAQY----ATLWTSLGRSVVIV-------SEASTSQLPVVTKTADPSVNPGNAAY---------- 4688
Cdd:PRK08314   100 LAHYVTDSGARVAIVGSELapkvAPAVGNLRLRHVIVaqysdylPAEPEIAVPAWLRAEPPLQALAPGGVvawkealaag 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4689 -------------AI--FTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYtFDaciaeiITTLLCC--- 4750
Cdd:PRK08314   180 lappphtagpddlAVlpYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FH------VTGMVHSmna 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4751 -----GCICVPSDSDRRnnLAK------------AINAMDVNWaLLTPSVARMlDpcvVQSLKILVLGG----EQVNSAD 4809
Cdd:PRK08314   253 piyagATVVLMPRWDRE--AAArlieryrvthwtNIPTMVVDF-LASPGLAER-D---LSSLRYIGGGGaampEAVAERL 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4810 WDRWpkSIQTINAYGPTEcSICCTTYSGKQGFKSGTIGTSIVSV-SWVVDPENHNRLAPlGSIGELLVEGPILARGYLND 4888
Cdd:PRK08314   326 KELT--GLDYVEGYGLTE-TMAQTHSNPPDRPKLQCLGIPTFGVdARVIDPETLEELPP-GEVGEIVVHGPQVFKGYWNR 401
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 4889 MEKTEAAFIDdpawlLEGygghsgrqGRLYKTGDLVRYDADG 4930
Cdd:PRK08314   402 PEATAEAFIE-----IDG--------KRFFRTGDLGRMDEEG 430
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
855-1367 2.21e-18

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 93.33  E-value: 2.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  855 HDLFAEQARARPDASAV--CAWDGE---LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAF 929
Cdd:cd05970     20 YDVVDAMAKEYPDKLALvwCDDAGEeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  930 VPldPGHPASRHEEIFKQIGAQVvltssqhAMLFASSERHQVTVSKVSTSQLPTV--------------VNFAK------ 989
Cdd:cd05970    100 IP--ATHQLTAKDIVYRIESADI-------KMIVAIAEDNIPEEIEKAAPECPSKpklvwvgdpvpegwIDFRKliknas 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  990 -------SPVDPGN--TAYIIFTSGTTGIPKGVVLQHravtTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLY 1060
Cdd:cd05970    171 pdferptANSYPCGedILLVYFSSGTTGMPKMVEHDF----TYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIY 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1061 G----GCICVPSESDR--RNNLAKAISTMDVNCALLTPSVARLL-----EPSAVPSLKRLVLQGEQVSFADWNRWPG--S 1127
Cdd:cd05970    247 GqwiaGAAVFVYDYDKfdPKALLEKLSKYGVTTFCAPPTIYRFLiredlSRYDLSSLRYCTTAGEALNPEVFNTFKEktG 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1128 VQTINGYGPTECSVCCNTYSGKQGfKSGIIGTSvaSLSWVVDAGNHN-RLAPLGSIGELLV---EG-PI-LARGYLNDID 1201
Cdd:cd05970    327 IKLMEGFGQTETTLTIATFPWMEP-KPGSMGKP--APGYEIDLIDREgRSCEAGEEGEIVIrtsKGkPVgLFGGYYKDAE 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1202 KTEAAFIDdpawlleGYeghagrrgrlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhhvreclpearqlav 1281
Cdd:cd05970    404 KTAEVWHD-------GY----------YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVE--------------- 451
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1282 evilpsgqkehallAAFIQldkgnHNALFEEKASG--EDSMAQVVFLTGV-------EEELAKRLPEHM--------VPT 1344
Cdd:cd05970    452 --------------SALIQ-----HPAVLECAVTGvpDPIRGQVVKATIVlakgyepSEELKKELQDHVkkvtapykYPR 512
                          570       580
                   ....*....|....*....|...
gi 1820002560 1345 ILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:cd05970    513 IVEFVDELPKTISGKIRRVEIRE 535
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
5612-6137 2.43e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 93.56  E-value: 2.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5612 WNQNVPPAIERCV-HDL-----FTEQAKAR-PHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMW 5684
Cdd:PRK06710     7 WLKSYPEEIPSTIsYDIqplhkYVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5685 TVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVV---------VTSAQHSARwigTNHQVVTVSAGSLGQLSTLV 5755
Cdd:PRK06710    87 AVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlcldlvfprVTNVQSATK---IEHVIVTRIADFLPFPKNLL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5756 NP--------------------------------VGLPAIPENAVYIM-FTSGSTGIPKGVVLEHRAVVTSC-----WGR 5797
Cdd:PRK06710   164 YPfvqkkqsnlvvkvsesetihlwnsvekevntgVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTlmgvqWLY 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5798 GRAFGITNLSRVLQFAS-YTFDACMDeiiTTLMYGGCICVPSDSDRRNdLVKAISTMDVSCALLTPSVARLLEPSsvPTL 5876
Cdd:PRK06710   244 NCKEGEEVVLGVLPFFHvYGMTAVMN---LSIMQGYKMVLIPKFDMKM-VFEAIKKHKVTLFPGAPTIYIALLNS--PLL 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5877 QMLVLQGEQVSFADWNRWPASVQT----------INGYGPTECSICCNTYSGKQGFKSGIIGtsvasVSW------VVDP 5940
Cdd:PRK06710   318 KEYDISSIRACISGSAPLPVEVQEkfetvtggklVEGYGLTESSPVTHSNFLWEKRVPGSIG-----VPWpdteamIMSL 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5941 ENHDRLAPlGSIGELLVEGPILARGYLNDIQKTAAVFIDdpAWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKD 6020
Cdd:PRK06710   393 ETGEALPP-GEIGEIVVKGPQIMKGYWNKPEETAAVLQD--GWL---------------HTGDVGYMDEDGFFYVKDRKK 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6021 SQVKLRGQRVELGEVEHHVREclPEARQLAVEVILPSGQKDHAmLAAFVQLEEGTQNAlldkeasgedsmaqvvflasvE 6100
Cdd:PRK06710   455 DMIVASGFNVYPREVEEVLYE--HEKVQEVVTIGVPDPYRGET-VKAFVVLKEGTECS---------------------E 510
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 6101 EEL----AKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:PRK06710   511 EELnqfaRKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
PRK05691 PRK05691
peptide synthase; Validated
7889-8511 2.59e-18

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 94.85  E-value: 2.59e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7889 YGPTECCIFCTGYTTKQGF---------------EPSTiGTSVASVSW--------VVDPENHNRLAPlGSMGELLMEGP 7945
Cdd:PRK05691   328 YGLAEATLFVSGGRRGQGIpaleldaealarnraEPGT-GSVLMSCGRsqpghavlIVDPQSLEVLGD-NRVGEIWASGP 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7946 ILARGYLNDVDKTEAAFI--DDPAWLlegypghpgrqgrlyKTGDLvQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHH 8023
Cdd:PRK05691   406 SIAHGYWRNPEASAKTFVehDGRTWL---------------RTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKT 469
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8024 VRECLPEARQLAVevilpsgqknhAMLAVFVQLGKGTHIAhleekAGGEDSMAQVVfltgTEEELAKRLPK------HMV 8097
Cdd:PRK05691   470 VEREVEVVRKGRV-----------AAFAVNHQGEEGIGIA-----AEISRSVQKIL----PPQALIKSIRQavaeacQEA 529
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8098 PTVFfALLH---FPMTTSGKADRK--RLR-EIG-----ASFTAQQLAETQTSSQGPkrqplTEAEQTMQQLWARVLGIDA 8166
Cdd:PRK05691   530 PSVV-LLLNpgaLPKTSSGKLQRSacRLRlADGsldsyALFPALQAVEAAQTAASG-----DELQARIAAIWCEQLKVEQ 603
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8167 diIGLDDSFFRLGGDSIAAMKLVGEARRT-GLQLSVADIFRHPRLIDLASLKSTFcnsVVEEVPAFSLLSPVMKDAMFsv 8245
Cdd:PRK05691   604 --VAADDHFFLLGGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAAFSAAVARQ---LAGGGAAQAAIARLPRGQAL-- 676
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8246 tepfgpslridditdvvPASYIQQFYIATGVRAPRE-AFNYPF-IDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGK 8323
Cdd:PRK05691   677 -----------------PQSLAQNRLWLLWQLDPQSaAYNIPGgLHLRGELDEAALRASFQRLVERHESLRTRFYERDGV 739
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8324 LYQVIPRHQDLPFSIFEVNGALAEE--SQAIHIRDLDQTSPLGLPTS----FTLVRNASGMNRLIIRLSHAQYDGVCMPV 8397
Cdd:PRK05691   740 ALQRIDAQGEFALQRIDLSDLPEAEreARAAQIREEEARQPFDLEKGpllrVTLVRLDDEEHQLLVTLHHIVADGWSLNI 819
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8398 IWASLASIYQ-----QEPLLSTTGFHsYLAYVHNQR--------SASINYWSRLLKGSHITNITSKLRPKLGKDT----- 8459
Cdd:PRK05691   820 LLDEFSRLYAaacqgQTAELAPLPLG-YADYGAWQRqwlaqgeaARQLAYWKAQLGDEQPVLELATDHPRSARQAhsaar 898
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 8460 -TIR-SVKVERVIRTPQLPTGLTMASLVSSAWAVVLSHISGEEDVVYGLVVAGR 8511
Cdd:PRK05691   899 ySLRvDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANR 952
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1938-2445 2.93e-18

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 92.62  E-value: 2.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1938 QAKARPHAPAICAWDGELTYGELDALSSKLASHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 2016
Cdd:PRK06839    11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2017 RHEDIFRQTGAQVVVTSAQHSA------RWIGTNHQVVTVSAGSLEQFStlvnPVDLPAKPENAAYVM-FTSGSTGTPKG 2089
Cdd:PRK06839    91 ELIFQLKDSGTTVLFVEKTFQNmalsmqKVSYVQRVISITSLKEIEDRK----IDNFVEKNESASFIIcYTSGTTGKPKG 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2090 VVLEHRAVVtsclghgqaFGVTNLLRALQFTAYtfDVCIAEI------------ITTLVHGGCICVPsdseRRDNLAKAI 2157
Cdd:PRK06839   167 AVLTQENMF---------WNALNNTFAIDLTMH--DRSIVLLplfhiggiglfaFPTLFAGGVIIVP----RKFEPTKAL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2158 TDMQvnwgylTSSVARLLDpclVPSLKVLVLGGEQVNSTD-----W---GKWPSSVQTI-----------NGYGPTECC- 2217
Cdd:PRK06839   232 SMIE------KHKVTVVMG---VPTIHQALINCSKFETTNlqsvrWfynGGAPCPEELMrefidrgflfgQGFGMTETSp 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2218 -VFCTGYTGIQGfQSGNIGTSIASVSWVVDPENHGRLAPlGSIGELLVEGPILARGYLNDVDKTQAAFiddpawllegyp 2296
Cdd:PRK06839   303 tVFMLSEEDARR-KVGSIGKPVLFCDYELIDENKNKVEV-GEVGELLIRGPNVMKEYWNRPDATEETI------------ 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2297 ghegRQGRLYkTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVPPS--GERDHamlaA 2374
Cdd:PRK06839   369 ----QDGWLC-TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINK-LSDVYEVAVVGRQHVkwGEIPI----A 438
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 2375 FIRLDdetrnspliikyaednSTAQIvfltgIEEELSE----RLPQHMVPTVFFALVHFPTTTSGKTDRKRLREI 2445
Cdd:PRK06839   439 FIVKK----------------SSSVL-----IEKDVIEhcrlFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
5631-6138 2.99e-18

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 92.62  E-value: 2.99e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5631 QAKARPHAPAICAWDGELTYGELDALSSKLAGHL-TQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 5709
Cdd:PRK06839    11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5710 RHEDTFRHTGAQVVVTSAQHSA------RWIGTNHQVVTVSAGSLGQLStlvnPVGLPAIPENAVYIM-FTSGSTGIPKG 5782
Cdd:PRK06839    91 ELIFQLKDSGTTVLFVEKTFQNmalsmqKVSYVQRVISITSLKEIEDRK----IDNFVEKNESASFIIcYTSGTTGKPKG 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5783 VVLEHravVTSCWGrgrafGITNLsrvlqfasYTFDACMDEI-----------------ITTLMYGGCICVPsdsdRRND 5845
Cdd:PRK06839   167 AVLTQ---ENMFWN-----ALNNT--------FAIDLTMHDRsivllplfhiggiglfaFPTLFAGGVIIVP----RKFE 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5846 LVKAISTMDvscallTPSVARLLepsSVPTLQMLVLQGEQVSFADWN--RW------PASVQTI-----------NGYGP 5906
Cdd:PRK06839   227 PTKALSMIE------KHKVTVVM---GVPTIHQALINCSKFETTNLQsvRWfynggaPCPEELMrefidrgflfgQGFGM 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5907 TECSICCNTYSgKQGF--KSGIIGTSVASVSW-VVDPENHDrlAPLGSIGELLVEGPILARGYLNDIQKTAAVFiddpaw 5983
Cdd:PRK06839   298 TETSPTVFMLS-EEDArrKVGSIGKPVLFCDYeLIDENKNK--VEVGEVGELLIRGPNVMKEYWNRPDATEETI------ 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5984 llegypghpgRQGRLYkTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAVeVILPS---GQK 6060
Cdd:PRK06839   369 ----------QDGWLC-TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINK-LSDVYEVAV-VGRQHvkwGEI 435
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 6061 DHamlaAFVQLEEGTqnalldkeasgedsmaqVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREI 6138
Cdd:PRK06839   436 PI----AFIVKKSSS-----------------VLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
5632-6011 3.31e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 92.72  E-value: 3.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGELTYGELDALSSKLAGHLTQ-LGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPdhpaSR 5710
Cdd:PRK08314    20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP----MN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5711 HEDTFRH----TGAQVVVTSAQHSAR------WIGTNHQVVTVSAGSLGQLSTLVNPVGL------PAIPENAVY----- 5769
Cdd:PRK08314    96 REEELAHyvtdSGARVAIVGSELAPKvapavgNLRLRHVIVAQYSDYLPAEPEIAVPAWLraepplQALAPGGVVawkea 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 -------------------IMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASY----TFDACMDeiiT 5826
Cdd:PRK08314   176 laaglappphtagpddlavLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLfhvtGMVHSMN---A 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5827 TLMYGGCICVPSDSDRR--NDLVK--------AISTMDVScALLTPSvarlLEPSSVPTLQMLVLQGEQVsfadwnrwPA 5896
Cdd:PRK08314   253 PIYAGATVVLMPRWDREaaARLIEryrvthwtNIPTMVVD-FLASPG----LAERDLSSLRYIGGGGAAM--------PE 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5897 SV------QT----INGYGPTEcsiccnTYSG-----KQGFKSGIIGTSVASV-SWVVDPENHDRLAPlGSIGELLVEGP 5960
Cdd:PRK08314   320 AVaerlkeLTgldyVEGYGLTE------TMAQthsnpPDRPKLQCLGIPTFGVdARVIDPETLEELPP-GEVGEIVVHGP 392
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 5961 ILARGYLNDIQKTAAVFIDdpawlLEGypghpgrqGRLYKTGDLVRYDANG 6011
Cdd:PRK08314   393 QVFKGYWNRPEATAEAFIE-----IDG--------KRFFRTGDLGRMDEEG 430
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
5648-6036 3.75e-18

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 92.04  E-value: 3.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSa 5727
Cdd:cd17640      6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5728 qhsarwigtNHqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKGVVLEHRAVVtscwgrgraFGITNLS 5807
Cdd:cd17640     85 ---------ND-------------------------SDDLATIIYTSGTTGNPKGVMLTHANLL---------HQIRSLS 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5808 ---------RVLQF----------ASYTFDACmdeiittlmygGCICVPSdsdrrndlvkAISTMDVSCALLTP----SV 5864
Cdd:cd17640    122 divppqpgdRFLSIlpiwhsyersAEYFIFAC-----------GCSQAYT----------SIRTLKDDLKRVKPhyivSV 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5865 ARLLEP----------SSVPTLQMLV---LQGEQVSFA--DWNRWPASVQT---------INGYGPTECS--ICCNTYSG 5918
Cdd:cd17640    181 PRLWESlysgiqkqvsKSSPIKQFLFlffLSGGIFKFGisGGGALPPHVDTffeaigievLNGYGLTETSpvVSARRLKC 260
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5919 KqgfKSGIIGTSVASVSW-VVDPENHDRLAPlGSIGELLVEGPILARGYLNDIQKTAAVfIDDPAWLlegypghpgrqgr 5997
Cdd:cd17640    261 N---VRGSVGRPLPGTEIkIVDPEGNVVLPP-GEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDGWF------------- 322
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1820002560 5998 lyKTGDLVRYDANGNLVCLGR-KDSQVKLRGQRVELGEVE 6036
Cdd:cd17640    323 --NTGDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIE 360
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
861-1365 3.90e-18

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 91.95  E-value: 3.90e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  861 QARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpghpaSR 940
Cdd:PRK03640    11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN-----TR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  941 --HEEIFKQI---GAQVVLTSSQhamlFASSER--HQVTVSKVStsQLPTVVNFAKSPVDPGNTAYIIFTSGTTGIPKGV 1013
Cdd:PRK03640    86 lsREELLWQLddaEVKCLITDDD----FEAKLIpgISVKFAELM--NGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1014 VLQHRAVTTSCLGHGEAFGYTDHARVLqfasytfdACI--------AEIITTLLYGGCICVPS--ESDRRNNLAK--AIS 1081
Cdd:PRK03640   160 IQTYGNHWWSAVGSALNLGLTEDDCWL--------AAVpifhisglSILMRSVIYGMRVVLVEkfDAEKINKLLQtgGVT 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1082 TMDVNCALLTPSVARLLEPSAVPSLKRLVLQGEQVSFA------DWNrwpgsVQTINGYGPTE-CSVCCN---TYSGKqg 1151
Cdd:PRK03640   232 IISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPlleqckEKG-----IPVYQSYGMTEtASQIVTlspEDALT-- 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1152 fKSGIIGTSVASLSwvVDAGNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDdpAWLlegyeghagrrgrlyKT 1231
Cdd:PRK03640   305 -KLGSAGKPLFPCE--LKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD--GWF---------------KT 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1232 GDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEH------HVREclpearqlaVEVILPSGQKEHALLAAFIQLDkgn 1305
Cdd:PRK03640   365 GDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEvllshpGVAE---------AGVVGVPDDKWGQVPVAFVVKS--- 432
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1306 hnalfeEKASgEDSMAQVvfltgVEEELAKrlpeHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:PRK03640   433 ------GEVT-EEELRHF-----CEEKLAK----YKVPKRFYFVEELPRNASGKLLRHEL 476
PRK07787 PRK07787
acyl-CoA synthetase; Validated
5632-6036 4.34e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 91.97  E-value: 4.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGELTYGELDALSSKLAGhltqlGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 5711
Cdd:PRK07787    10 AAAADIADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAER 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5712 EDTFRHTGAQVVVTSAQHSARwiGTNHQVVTVSAGSLGQLStlvnpvglPAIPENAVYIMFTSGSTGIPKGVVLEHRAVV 5791
Cdd:PRK07787    85 RHILADSGAQAWLGPAPDDPA--GLPHVPVRLHARSWHRYP--------EPDPDAPALIVYTSGTTGPPKGVVLSRRAIA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5792 TSCWGRGRAFGIT---------------NL-----------SRVLQFASYTFDACMDEIIT--TLMYGgcicVPSDSDR- 5842
Cdd:PRK07787   155 ADLDALAEAWQWTaddvlvhglplfhvhGLvlgvlgplrigNRFVHTGRPTPEAYAQALSEggTLYFG----VPTVWSRi 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5843 --RNDLVKAISTmdvscalltpsvARLL----EPSSVPTLQMLV-LQGEQVsfadwnrwpasvqtINGYGPTECSICCNT 5915
Cdd:PRK07787   231 aaDPEAARALRG------------ARLLvsgsAALPVPVFDRLAaLTGHRP--------------VERYGMTETLITLST 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5916 Y-SGKQgfKSGIIGTSVASVSWVVDPENHDRLAPLG-SIGELLVEGPILARGYLNDIQKTAAVFIDDpAWllegypghpg 5993
Cdd:PRK07787   285 RaDGER--RPGWVGLPLAGVETRLVDEDGGPVPHDGeTVGELQVRGPTLFDGYLNRPDATAAAFTAD-GW---------- 351
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 5994 rqgrlYKTGDLVRYDANGNLVCLGRKDSQ-VKLRGQRVELGEVE 6036
Cdd:PRK07787   352 -----FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIE 390
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
4566-5056 5.51e-18

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 90.87  E-value: 5.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4566 ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDhpASRHEHIFRQTGAQVVLAS 4645
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR--LTPNELAFQLKDSDVKLDD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4646 AqyATLwtslgrsvvivseastsqlpvvtktadpsvnpgnaayaIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDH 4725
Cdd:cd05912     79 I--ATI--------------------------------------MYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4726 TR--------------------VLQFASYTFDACIAEIITTLLccgcicvpsdSDRRnnlakaINAMDVNWALLTPSVAR 4785
Cdd:cd05912    119 DNwlcalplfhisglsilmrsvIYGMTVYLVDKFDAEQVLHLI----------NSGK------VTIISVVPTMLQRLLEI 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4786 MLDPCVvQSLKILVLGG--------EQVNSadwdrwpKSIQTINAYGPTE-CSICCTTYSGKQGFKSGTIGTSIVSVSW- 4855
Cdd:cd05912    183 LGEGYP-NNLRCILLGGgpapkpllEQCKE-------KGIPVYQSYGMTEtCSQIVTLSPEDALNKIGSAGKPLFPVELk 254
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4856 VVDPENhnrlaPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpaWLlegygghsgrqgrlyKTGDLVRYDADGNLVYL 4935
Cdd:cd05912    255 IEDDGQ-----PPYEVGEILLKGPNVTKGYLNRPDATEESFENG--WF---------------KTGDIGYLDEEGFLYVL 312
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4936 GRKDSQVKLRGQRVELGEVEHHVREcLTEAKQLAVeVIVPEGEGGYAMLAAFVQLGDDTYNTLVkekaggdsltvqvvfl 5015
Cdd:cd05912    313 DRRSDLIISGGENIYPAEIEEVLLS-HPAIKEAGV-VGIPDDKWGQVPVAFVVSERPISEEELI---------------- 374
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 5016 DRVEEELAK-RVPEHmmlttFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:cd05912    375 AYCSEKLAKyKVPKK-----IYFVDELPRTASGKLLRHELKQ 411
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
4532-5059 5.67e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 92.14  E-value: 5.67e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4532 NQDVPPAIErCVHDQFAEQARARPDTPAICAWDGEL--TYGELDTLSSKLASHLVQLGVKPEDMV----PLCFEksmWTV 4605
Cdd:PRK12583    10 GGDKPLLTQ-TIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVgiwaPNCAE---WLL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4606 VAMlAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLASAQYAT---------LWTSLG---------------RSVVI 4661
Cdd:PRK12583    86 TQF-ATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTsdyhamlqeLLPGLAegqpgalacerlpelRGVVS 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4662 VSEASTSQL---PVVTKTAD-----------PSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTR 4727
Cdd:PRK12583   165 LAPAPPPGFlawHELQARGEtvsrealaerqASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDR 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4728 VLqfASYTFDACIAEIITTLLCC---GCICVPSDSDRRNNLAKAINAMDVN--WALLTPSVARMLDPCV----VQSLKIL 4798
Cdd:PRK12583   245 LC--VPVPLYHCFGMVLANLGCMtvgACLVYPNEAFDPLATLQAVEEERCTalYGVPTMFIAELDHPQRgnfdLSSLRTG 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4799 VLGG------------EQVNSADwdrwpksIQTinAYGPTECS--ICCTTYSGKQGFKSGTIGTSIVSV-SWVVDPENHN 4863
Cdd:PRK12583   323 IMAGapcpievmrrvmDEMHMAE-------VQI--AYGMTETSpvSLQTTAADDLERRVETVGRTQPHLeVKVVDPDGAT 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4864 rlAPLGSIGELLVEGPILARGYLNDMEKTEAAfIDDPAWLlegygghsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQVK 4943
Cdd:PRK12583   394 --VPRGEIGELCTRGYSVMKGYWNNPEATAES-IDEDGWM---------------HTGDLATMDEQGYVRIVGRSKDMII 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4944 LRGQRVELGEVEHHVrecLTEAKQLAVEVI-VPEGEGGyAMLAAFVQLgddtyntlvkekAGGDSLTvqvvfldrvEEEL 5022
Cdd:PRK12583   456 RGGENIYPREIEEFL---FTHPAVADVQVFgVPDEKYG-EEIVAWVRL------------HPGHAAS---------EEEL 510
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 5023 AK---------RVPEHmmlttFFTLEAMPTTTSGKIDRKRLREIGA 5059
Cdd:PRK12583   511 REfckariahfKVPRY-----FRFVDEFPMTVTGKVQKFRMREISI 551
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
13-208 5.94e-18

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 91.62  E-value: 5.94e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   13 ARLLEPSHIPSLRILVMGGEQVNSADWDRWPSS--VQTINGYGPTECCIVCTGYTSEQDFTTGTIGTSIASVSWVVDPKD 90
Cdd:cd05909    252 ARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVE 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   91 HGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinnpawllegHGGYagrqgrlYKTGDLVRYDADGNLVCLGRKDSQ 170
Cdd:cd05909    332 THEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF----------GDGW-------YDTGDIGKIDGEGFLTITGRLSRF 394
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1820002560  171 VKLRGQRVELGEVEHHVRECLPEAKQLAVeVVLPLGQK 208
Cdd:cd05909    395 AKIAGEMVSLEAIEDILSEILPEDNEVAV-VSVPDGRK 431
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
848-1371 7.28e-18

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 91.74  E-value: 7.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  848 PAVDRCIHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGG 927
Cdd:PRK06155    17 PPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  928 AFVPLDPGHPASRHEEIFKQIGAQVVLTSS------QHAMLFASSERHQVTVSKVSTSQLPTVVNFAKSP---------- 991
Cdd:PRK06155    97 IAVPINTALRGPQLEHILRNSGARLLVVEAallaalEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPpldapapaaa 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  992 VDPGNTAYIIFTSGTTGIPKGVvlqhravttsCLGHGEAFGYTDH-ARVLQFAS----YTF-----DACIAEIITTLLYG 1061
Cdd:PRK06155   177 VQPGDTAAILYTSGTTGPSKGV----------CCPHAQFYWWGRNsAEDLEIGAddvlYTTlplfhTNALNAFFQALLAG 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1062 GCICVP---SESDRRNNLAKAISTMDVncaLLTPSVARLLEPSAVPS-----LKRLVLQGEQVSFADWNRWPGSVQTING 1133
Cdd:PRK06155   247 ATYVLEprfSASGFWPAVRRHGATVTY---LLGAMVSILLSQPARESdrahrVRVALGPGVPAALHAAFRERFGVDLLDG 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1134 YGPTECSVCCNTYSGKQgfKSGIIGTSVASL-SWVVDagNHNRLAPLGSIGELLV---EGPILARGYLNDIDKTEAafid 1209
Cdd:PRK06155   324 YGSTETNFVIAVTHGSQ--RPGSMGRLAPGFeARVVD--EHDQELPDGEPGELLLradEPFAFATGYFGMPEKTVE---- 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1210 dpAWllegyeghagrRGRLYKTGDLVRCDADGNLVCLGR-KDSqVKVRGQRVELGEIEhhvreclpearqlavEVILpsg 1288
Cdd:PRK06155   396 --AW-----------RNLWFHTGDRVVRDADGWFRFVDRiKDA-IRRRGENISSFEVE---------------QVLL--- 443
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1289 qkEHALLAAFiqldkgnhnALFEEKAS-GEDS-MAQVVFLTGVE---EELAK----RLPEHMVPTILFTVKAMPITTSGK 1359
Cdd:PRK06155   444 --SHPAVAAA---------AVFPVPSElGEDEvMAAVVLRDGTAlepVALVRhcepRLAYFAVPRYVEFVAALPKTENGK 512
                          570
                   ....*....|..
gi 1820002560 1360 IDRKRLQDIGAS 1371
Cdd:PRK06155   513 VQKFVLREQGVT 524
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
5617-6145 7.35e-18

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 91.74  E-value: 7.35e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5617 PPAiERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAG 5696
Cdd:PRK06155    17 PPS-ERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLG 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5697 GAFVPLDPDHPASRHEDTFRHTGAQVVVTSAQHSAR--------------WI----GTNHQVVTVSAGSLGQLSTLVNPV 5758
Cdd:PRK06155    96 AIAVPINTALRGPQLEHILRNSGARLLVVEAALLAAleaadpgdlplpavWLldapASVSVPAGWSTAPLPPLDAPAPAA 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5759 glPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTscWGR--GRAFGI-------TNLSRVLQFASYTFdacmdeiITTLM 5829
Cdd:PRK06155   176 --AVQPGDTAAILYTSGTTGPSKGVCCPHAQFYW--WGRnsAEDLEIgaddvlyTTLPLFHTNALNAF-------FQALL 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5830 YGGCICVP---SDSDRRNDLVKAISTMD------VSCALLTPSVARllepSSVPTLQMLVLQGEQVSFADWNRWPASVQT 5900
Cdd:PRK06155   245 AGATYVLEprfSASGFWPAVRRHGATVTyllgamVSILLSQPARES----DRAHRVRVALGPGVPAALHAAFRERFGVDL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5901 INGYGPTECSICCNTYSGKQgfKSGIIGTSVASV-SWVVDpeNHDRLAPLGSIGELLV---EGPILARGYLNDIQKTAAv 5976
Cdd:PRK06155   321 LDGYGSTETNFVIAVTHGSQ--RPGSMGRLAPGFeARVVD--EHDQELPDGEPGELLLradEPFAFATGYFGMPEKTVE- 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5977 fiddpAWllegypghpgrQGRLYKTGDLVRYDANGNLVCLGR-KDSqVKLRGQRVELGEVEHHVREcLPEARQLAVeVIL 6055
Cdd:PRK06155   396 -----AW-----------RNLWFHTGDRVVRDADGWFRFVDRiKDA-IRRRGENISSFEVEQVLLS-HPAVAAAAV-FPV 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6056 PSGQKDHAMLAAFVqLEEGTQnalLDkeasgedsmaqvvFLASVEEELAkRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:PRK06155   457 PSELGEDEVMAAVV-LRDGTA---LE-------------PVALVRHCEP-RLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
                          570
                   ....*....|
gi 1820002560 6136 REIGasFTAQ 6145
Cdd:PRK06155   519 REQG--VTAD 526
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
5612-6137 8.22e-18

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 91.86  E-value: 8.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5612 WNQNVPPAIE--------RCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLT-QLGVKPEDMVPLCFEKS 5682
Cdd:PRK08751     7 WLQSYPAGVAaeidleqfRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNC 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5683 MWTVVAMLAVLKAGGAFVPLDPDHPAS--RHEDTFRHTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLGQL-----STLV 5755
Cdd:PRK08751    87 LQYPIATFGVLRAGLTVVNVNPLYTPRelKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMlgfpkAALV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5756 NPV-----------------------------GLPAI---PENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGI 5803
Cdd:PRK08751   167 NFVvkyvkklvpeyringairfrealalgrkhSMPTLqiePDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAG 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5804 TNLSR------VLQFASYTFDACMDEIITTLMYGGC---ICVPSD--------SDRRNDLVKAISTMdVSCALLTPSVAR 5866
Cdd:PRK08751   247 TGKLEegcevvITALPLYHIFALTANGLVFMKIGGCnhlISNPRDmpgfvkelKKTRFTAFTGVNTL-FNGLLNTPGFDQ 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5867 LlepsSVPTLQMLVLQGEQVSFADWNRWP--ASVQTINGYGPTECS--ICCNTYSGKQgfKSGIIGTSVASVSWVVDpEN 5942
Cdd:PRK08751   326 I----DFSSLKMTLGGGMAVQRSVAERWKqvTGLTLVEAYGLTETSpaACINPLTLKE--YNGSIGLPIPSTDACIK-DD 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5943 HDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVfIDDPAWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQ 6022
Cdd:PRK08751   399 AGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKV-MDADGWL---------------HTGDIARMDEQGFVYIVDRKKDM 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6023 VKLRGQRVELGEVEhHVRECLPEARQLAVeVILPSGQKDHAMLAAFVQleegtqnalLDKEASGEDsmaqvvflasVEEE 6102
Cdd:PRK08751   463 ILVSGFNVYPNEIE-DVIAMMPGVLEVAA-VGVPDEKSGEIVKVVIVK---------KDPALTAED----------VKAH 521
                          570       580       590
                   ....*....|....*....|....*....|....*
gi 1820002560 6103 LAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:PRK08751   522 ARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
4854-5148 8.71e-18

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 88.27  E-value: 8.71e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4854 SWVVDPENHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAWllegygghSGRQGRLYKTGDLVRYDADGNLV 4933
Cdd:COG3433     23 AIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIP--------VPYPAQPGRQADDLRLLLRRGLG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4934 YLGRKDSQVKLRGQRVELGEVEHHVRECLTEAKQLAVEVIVPEGEGGyamlaafvqlgDDTYNTLVKEKAGGDSLTVQVV 5013
Cdd:COG3433     95 PGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGV-----------GLLLIVGAVAALDGLAAAAALA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5014 FLDRVeeelakrvpeHMMLTTFFTLEAMPTTTSGKIDRKRLREIGASFTAQQLAEmrTSSQGPKRQPSTEAErtMQQLWT 5093
Cdd:COG3433    164 ALDKV----------PPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAA--ASPAPALETALTEEE--LRADVA 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 5094 RVLGIELNGIGLDDSFFRLGGDSIAAMKLVGEARRTGLQLSVADVFRHPRLVDLA 5148
Cdd:COG3433    230 ELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWW 284
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
859-1387 9.76e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 91.38  E-value: 9.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  859 AEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPA 938
Cdd:PRK07786    24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  939 SRHEEIFKQIGAQVVLTSSQHAMLfASSERHQV----TVSKVSTSQLPTVVNF---------AKSPVD-PGNT-AYIIFT 1003
Cdd:PRK07786   104 PEIAFLVSDCGAHVVVTEAALAPV-ATAVRDIVpllsTVVVAGGSSDDSVLGYedllaeagpAHAPVDiPNDSpALIMYT 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1004 SGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFD-ACIAEIITTLLYGGCICV-PSESDRRNNLAKAIS 1081
Cdd:PRK07786   183 SGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHiAGIGSMLPGLLLGAPTVIyPLGAFDPGQLLDVLE 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1082 TMDVNCALLTPS--VARLLEPSAVP-SLKRLVLQgeqvsfadWNRWPGS-------------VQTINGYGPTECSVCCNT 1145
Cdd:PRK07786   263 AEKVTGIFLVPAqwQAVCAEQQARPrDLALRVLS--------WGAAPASdtllrqmaatfpeAQILAAFGQTEMSPVTCM 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1146 YSGKQGF-KSGIIGTSVASLSWVVDAGNHNRLAPlGSIGELLVEGPILARGYLNDIDKTEAAFidDPAWllegyeghagr 1224
Cdd:PRK07786   335 LLGEDAIrKLGSVGKVIPTVAARVVDENMNDVPV-GEVGEIVYRAPTLMSGYWNNPEATAEAF--AGGW----------- 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1225 rgrlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhHVRECLPEARQLAveVILPSGQKEHALLAAFIQLDKG 1304
Cdd:PRK07786   401 ----FHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVE-NVLASHPDIVEVA--VIGRADEKWGEVPVAVAAVRND 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1305 NHNALFEEKASgedsmaqvvFLTGveeelakRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDigaSFTVQQLAEMRTSS 1384
Cdd:PRK07786   474 DAALTLEDLAE---------FLTD-------RLARYKHPKALEIVDALPRNPAGKVLKTELRE---RYGACVNVERRSAS 534

                   ...
gi 1820002560 1385 QGP 1387
Cdd:PRK07786   535 AGF 537
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5764-6136 9.81e-18

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 88.87  E-value: 9.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5764 PENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRV-LQFASYTFDACMDEIITTLMYGGCICVPSDSDR 5842
Cdd:cd05917      1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcIPVPLFHCFGSVLGVLACLTHGATMVFPSPSFD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5843 RNDLVKAIS-----------TMdvSCALLTPSVARLLEPSSVPTLqmlVLQGEQVSFADWNRwpaSVQTIN------GYG 5905
Cdd:cd05917     81 PLAVLEAIEkekctalhgvpTM--FIAELEHPDFDKFDLSSLRTG---IMAGAPCPPELMKR---VIEVMNmkdvtiAYG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5906 PTECSICCNtysgkQGFKSGIIGTSVASV--------SWVVDPENhDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVf 5977
Cdd:cd05917    153 MTETSPVST-----QTRTDDSIEKRVNTVgrimphteAKIVDPEG-GIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA- 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5978 IDDPAWllegypghpgrqgrlYKTGDLVRYDANGNLVCLGR-KDSQVKlRGQRVELGEVEhhvrECL---PEARQlaVEV 6053
Cdd:cd05917    226 IDGDGW---------------LHTGDLAVMDEDGYCRIVGRiKDMIIR-GGENIYPREIE----EFLhthPKVSD--VQV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6054 IlpsGQKDHAM---LAAFVQLEEGtqnalldKEASGEDsmaqvvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKT 6130
Cdd:cd05917    284 V---GVPDERYgeeVCAWIRLKEG-------AELTEED----------IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKI 343

                   ....*.
gi 1820002560 6131 DRKRLR 6136
Cdd:cd05917    344 QKFKLR 349
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
7750-8117 9.95e-18

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 88.86  E-value: 9.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7750 ENAAYIIFTSGSTGVPKGVVLEHR---AVATSCLGHGRAFGITNLSRVLQFASYTFDacIAEIITTLLCGGCICVPSDSD 7826
Cdd:cd17635      1 EDPLAVIFTSGTTGEPKAVLLANKtffAVPDILQKEGLNWVVGDVTYLPLPATHIGG--LWWILTCLIHGGLCVTGGENT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7827 RRNSLAKAISTMDVNWAFLTPSVARLLDPGL------IPSLKILAIGGEQSSSADWN--RWPGSVQKIHVYGPTECCIFC 7898
Cdd:cd17635     79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELksanatVPSLRLIGYGGSRAIAADVRfiEATGLTNTAQVYGLSETGTAL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7899 TGYTTKQGFEPSTIGTSVASVSWVVdPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLlegypghpg 7978
Cdd:cd17635    159 CLPTDDDSIEINAVGRPYPGVDVYL-AATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG--WV--------- 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7979 rqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVEVIlpsgqkNHAMLAVFVQlgk 8058
Cdd:cd17635    227 ------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECACYEI------SDEEFGELVG--- 290
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 8059 gthiahLEEKAGGEDSMAQVvflTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADR 8117
Cdd:cd17635    291 ------LAVVASAELDENAI---RALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK07788 PRK07788
acyl-CoA synthetase; Validated
4551-5057 1.02e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 91.14  E-value: 1.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 4630
Cdd:PRK07788    59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4631 EHIFRQTGAQVVLASAQYATLW----TSLGRSVVIVSEASTSQLPVVT-----------KTADPSVNPGNAAYAIFTSGS 4695
Cdd:PRK07788   139 AEVAAREGVKALVYDDEFTDLLsalpPDLGRLRAWGGNPDDDEPSGSTdetlddliagsSTAPLPKPPKPGGIVILTSGT 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4696 TGIPKGVVLEHKAVVTScLGhgqafGITDHT-----RVLQFASYTFDA---CIAEIITTLlccGCICVPSdsdRRNNLAK 4767
Cdd:PRK07788   219 TGTPKGAPRPEPSPLAP-LA-----GLLSRVpfragETTLLPAPMFHAtgwAHLTLAMAL---GSTVVLR---RRFDPEA 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4768 AINAMD---VNWALLTPS-VARMLD--PCVVQ-----SLKILVLGGEQVNSADWDRWPKSIQTI--NAYGPTECSICCTT 4834
Cdd:PRK07788   287 TLEDIAkhkATALVVVPVmLSRILDlgPEVLAkydtsSLKIIFVSGSALSPELATRALEAFGPVlyNLYGSTEVAFATIA 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4835 YSGKQGFKSGTIGTSIVSVSWVVDPENHNRLaPLGSIGELLVEGPILARGYLNdmekteaafiddpawllegyGGHSGRQ 4914
Cdd:PRK07788   367 TPEDLAEAPGTVGRPPKGVTVKILDENGNEV-PRGVVGRIFVGNGFPFEGYTD--------------------GRDKQII 425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4915 GRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhHVRECLTEAKQLAVeVIVPEGEGGyAMLAAFVqlgddt 4994
Cdd:PRK07788   426 DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVE-DLLAGHPDVVEAAV-IGVDDEEFG-QRLRAFV------ 496
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 4995 yntlVKEKagGDSLTVQVVfLDRVEEELAK-RVPEHMmltTFftLEAMPTTTSGKIDRKRLREI 5057
Cdd:PRK07788   497 ----VKAP--GAALDEDAI-KDYVRDNLARyKVPRDV---VF--LDELPRNPTGKVLKRELREM 548
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
1902-2436 1.05e-17

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 91.48  E-value: 1.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1902 VSDIETTTPEDRQQLWA------WNQEVPPAIERCVHDLFTEQAKARPHAPAICaWDGE-------LTYGELDALSSKLA 1968
Cdd:cd17634     20 GKILDWITPYQKVKNTSfapgapSIKWFEDATLNLAANALDRHLRENGDRTAII-YEGDdtsqsrtISYRELHREVCRFA 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1969 SHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAGGAFVPL----DPDHPASRHEDifrqTGAQVVVTSAQHSARw 2040
Cdd:cd17634     99 GTLLDLGVKKGDRVaiymPMIPE----AAVAMLACARIGAVHSVIfggfAPEAVAGRIID----SSSRLLITADGGVRA- 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2041 iGTNHQVVTVSAGSLEQFSTLVNPV----------------DL----------------PAKPENAAYVMFTSGSTGTPK 2088
Cdd:cd17634    170 -GRSVPLKKNVDDALNPNVTSVEHVivlkrtgsdidwqegrDLwwrdliakaspehqpeAMNAEDPLFILYTSGTTGKPK 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2089 GVVLEHRavvtsclGHgqafgvtnLLRALQFTAYTFDVCIAEIITT------------LVHGGCIC---------VPsDS 2147
Cdd:cd17634    249 GVLHTTG-------GY--------LVYAATTMKYVFDYGPGDIYWCtadvgwvtghsyLLYGPLACgattllyegVP-NW 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2148 ERRDNLAKAITDMQVNWGYLTSSVARLLDPC--------LVPSLKVLVLGGEQVNSTDWgKWPSSV------QTINGYGP 2213
Cdd:cd17634    313 PTPARMWQVVDKHGVNILYTAPTAIRALMAAgddaiegtDRSSLRILGSVGEPINPEAY-EWYWKKigkekcPVVDTWWQ 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2214 TECCVFCTgyTGIQGFQSGNIGTSIASV----SWVVDpeNHGRLAPLGSIGELLVEGPILArgylndvdKTQAAFIDDPA 2289
Cdd:cd17634    392 TETGGFMI--TPLPGAIELKAGSATRPVfgvqPAVVD--NEGHPQPGGTEGNLVITDPWPG--------QTRTLFGDHER 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2290 WLLEGYPGHEGrqgrLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMrKCLPEANQLAVEVVPPS--GER 2367
Cdd:cd17634    460 FEQTYFSTFKG----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVL-VAHPKVAEAAVVGIPHAikGQA 534
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 2368 dhamLAAFIRLDDETRNSPliikyaednstaqivfltGIEEELSERLPQHMVPTVFFALVHF----PTTTSGK 2436
Cdd:cd17634    535 ----PYAYVVLNHGVEPSP------------------ELYAELRNWVRKEIGPLATPDVVHWvdslPKTRSGK 585
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
991-1366 1.41e-17

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 88.49  E-value: 1.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  991 PVDPGNtayIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARV-LQFASYTFDACIAEIITTLLYGGCICVPSE 1069
Cdd:cd05917      1 PDDVIN---IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcIPVPLFHCFGSVLGVLACLTHGATMVFPSP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1070 S-DRRNNLAkAIStmDVNCALL--TPS--VARLLEP-----------------SAVPS--LKRLVlqgEQVSFADWnrwp 1125
Cdd:cd05917     78 SfDPLAVLE-AIE--KEKCTALhgVPTmfIAELEHPdfdkfdlsslrtgimagAPCPPelMKRVI---EVMNMKDV---- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1126 gsvqTInGYGPTECS-VCCNTYSGKQGFKSGiigTSVASL-----SWVVDAGNhNRLAPLGSIGELLVEGPILARGYLND 1199
Cdd:cd05917    148 ----TI-AYGMTETSpVSTQTRTDDSIEKRV---NTVGRImphteAKIVDPEG-GIVPPVGVPGELCIRGYSVMKGYWND 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1200 IDKTEAAfIDDPAWllegyeghagrrgrlYKTGDLVRCDADGNLVCLGR-KDsqVKVRG-QRVELGEIEhhvrECL---P 1274
Cdd:cd05917    219 PEKTAEA-IDGDGW---------------LHTGDLAVMDEDGYCRIVGRiKD--MIIRGgENIYPREIE----EFLhthP 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1275 EARQlaVEVIlpsGQKEHAL---LAAFIQLDKGnhnalfeEKASGEDSMAqvvFLTGveeelakRLPEHMVPTILFTVKA 1351
Cdd:cd05917    277 KVSD--VQVV---GVPDERYgeeVCAWIRLKEG-------AELTEEDIKA---YCKG-------KIAHYKVPRYVFFVDE 334
                          410
                   ....*....|....*
gi 1820002560 1352 MPITTSGKIDRKRLQ 1366
Cdd:cd05917    335 FPLTVSGKIQKFKLR 349
PRK06188 PRK06188
acyl-CoA synthetase; Validated
3452-3976 1.48e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 90.82  E-value: 1.48e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3452 NADVPPAIERCVH--DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAML 3529
Cdd:PRK06188     1 QATMADLLHSGATygHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3530 AVLKAGGAFVPLdpdHP-ASR--HEEIFEQTGAQV-VVASAQYSARW------TSSSCHVVTVSKA-----LSSQLPAVV 3594
Cdd:PRK06188    81 AAQLAGLRRTAL---HPlGSLddHAYVLEDAGISTlIVDPAPFVERAlallarVPSLKHVLTLGPVpdgvdLLAAAAKFG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3595 DSTNTSV-RPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFA--SYtfdACIAEIITTLLCGG 3671
Cdd:PRK06188   158 PAPLVAAaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTplSH---AGGAFFLPTLLRGG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3672 CICVPSDSDRRNSLAkAISTMDVNWAFLTPS-VARLLD-PGL----IPSLKILAIGGEQSSSAdwnRWPGSVQKI----- 3740
Cdd:PRK06188   235 TVIVLAKFDPAEVLR-AIEEQRITATFLVPTmIYALLDhPDLrtrdLSSLETVYYGASPMSPV---RLAEAIERFgpifa 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3741 HVYGPTECCIFCTgYTTKQGFEP------STIGTSVASVSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEA 3814
Cdd:PRK06188   311 QYYGQTEAPMVIT-YLRKRDHDPddpkrlTSCGRPTPGLRVALLDEDGREVAQ-GEVGEICVRGPLVMDGYWNRPEETAE 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3815 AFIDDpaWLlegypgHpgrqgrlykTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAV---- 3890
Cdd:PRK06188   389 AFRDG--WL------H---------TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAE-HPAVAQVAVigvp 450
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3891 -----E-----VILPSGQK-DHAMLAAFVQLEEGTQNAlldkeaggedsMAQVVFLASVeeelakrlpehmvptvffsll 3959
Cdd:PRK06188   451 dekwgEavtavVVLRPGAAvDAAELQAHVKERKGSVHA-----------PKQVDFVDSL--------------------- 498
                          570
                   ....*....|....*..
gi 1820002560 3960 hfPTTTSGKTDRKRLRE 3976
Cdd:PRK06188   499 --PLTALGKPDKKALRA 513
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
3486-3977 1.54e-17

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 90.66  E-value: 1.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3486 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVAS 3565
Cdd:cd17642     44 NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3566 AQYSARWTSSSCHVVTVSKAL------------------SSQLPAVVDS----TNTSVRPENAAYIIFTSGSTGVPKGVV 3623
Cdd:cd17642    124 KKGLQKVLNVQKKLKIIKTIIildskedykgyqclytfiTQNLPPGFNEydfkPPSFDRDEQVALIMNSSGSTGLPKGVQ 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3624 LEHRAVATScLGHGR--AFG--ITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLaKAISTMDVNWAFL 3699
Cdd:cd17642    204 LTHKNIVAR-FSHARdpIFGnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFL-RSLQDYKVQSALL 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3700 TPSV------ARLLDPGLIPSLKILAIGGEQSSS------ADWNRWPGSVQKihvYGPTECCIfcTGYTTKQGF-EPSTI 3766
Cdd:cd17642    282 VPTLfaffakSTLVDKYDLSNLHEIASGGAPLSKevgeavAKRFKLPGIRQG---YGLTETTS--AILITPEGDdKPGAV 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3767 GTSVASVSW-VVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTGDLVQ 3845
Cdd:cd17642    357 GKVVPFFYAkVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEATKAL-IDKDGWL---------------HSGDIAY 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3846 YNADGNLVYLGRKDSQVKVRGQRVELGEVE----HHvreclPEARQLAVevilpSGQKDHA---MLAAFVQLEEGTQnaL 3918
Cdd:cd17642    420 YDEDGHFFIVDRLKSLIKYKGYQVPPAELEsillQH-----PKIFDAGV-----AGIPDEDageLPAAVVVLEAGKT--M 487
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 3919 LDKEaggedsmaqVVFLASVEEELAKRLPEhmvpTVFFsLLHFPTTTSGKTDRKRLREI 3977
Cdd:cd17642    488 TEKE---------VMDYVASQVSTAKRLRG----GVKF-VDEVPKGLTGKIDRRKIREI 532
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
4119-4303 1.63e-17

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 85.86  E-value: 1.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4119 SPLQEGLMSLTAKRAgDYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSElGLLQVVVE------ERIQWTE 4192
Cdd:COG4908      2 SPAQKRFLFLEPGSN-AYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDG-EPVQRIDPdadlplEVVDLSA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4193 ------SESLEEYPREDKAVSMGVGDR-LARYALIKEPYDGGkrWFVWTMHHALYDGWSLPRILHAVKQAYSGVVLERQP 4265
Cdd:COG4908     80 lpeperEAELEELVAEEASRPFDLARGpLLRAALIRLGEDEH--VLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4266 -------SFNAFI----QYLSQQDPEAAAAYWQTALVDCKAAL-FPTLPP 4303
Cdd:COG4908    158 plpelpiQYADYAawqrAWLQSEALEKQLEYWRQQLAGAPPVLeLPTDRP 207
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
4543-5069 1.64e-17

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 91.01  E-value: 1.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4543 VHDQFAEQARARPDTPAIcAWDGE------LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGG 4616
Cdd:cd05968     63 VEQLLDKWLADTRTRPAL-RWEGEdgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4617 AFVPL----DPDHPASRHEH-----IFRQTG-----------AQVVLASAQYATLwtslgRSVVIVSEASTSQLPV---- 4672
Cdd:cd05968    142 IVVPIfsgfGKEAAATRLQDaeakaLITADGftrrgrevnlkEEADKACAQCPTV-----EKVVVVRHLGNDFTPAkgrd 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4673 -----VTKTADP---SVNPGNAAYAIFTSGSTGIPKGVVLEH-----KAVVTscLGHGqaFGITDHTRVLQFASYTFDAC 4739
Cdd:cd05968    217 lsydeEKETAGDgaeRTESEDPLMIIYTSGTTGKPKGTVHVHagfplKAAQD--MYFQ--FDLKPGDLLTWFTDLGWMMG 292
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4740 IAEIITTLLCCGCIC----VPsDSDRRNNLAKAINAMDVNWALLTPSVARML-----DPCVVQSLKIL-VLG--GEQVNS 4807
Cdd:cd05968    293 PWLIFGGLILGATMVlydgAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALkprgdAPVNAHDLSSLrVLGstGEPWNP 371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4808 ADWdRWpksiqTINAYGPTECSICctTYSGKQGFKSGTIG-------------TSIVSVSWVVDPENHNRLAPlgSIGEL 4874
Cdd:cd05968    372 EPW-NW-----LFETVGKGRNPII--NYSGGTEISGGILGnvlikpikpssfnGPVPGMKADVLDESGKPARP--EVGEL 441
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4875 LVEGPILArgylndMEKteaAFIDDPAWLLEGYGghsGRQGRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEV 4954
Cdd:cd05968    442 VLLAPWPG------MTR---GFWRDEDRYLETYW---SRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEI 509
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4955 E------HHVRECLTeakqlaveVIVPEGEGGYAMLaAFVQLGDDtyntlvkekaggdsltvqVVFLDRVEEELAKRVPE 5028
Cdd:cd05968    510 EsvlnahPAVLESAA--------IGVPHPVKGEAIV-CFVVLKPG------------------VTPTEALAEELMERVAD 562
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 5029 HM----MLTTFFTLEAMPTTTSGKIDRKRLReigASFTAQQLAEM 5069
Cdd:cd05968    563 ELgkplSPERILFVKDLPKTRNAKVMRRVIR---AAYLGKELGDL 604
PRK07798 PRK07798
acyl-CoA synthetase; Validated
3465-3915 1.80e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 90.33  E-value: 1.80e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 3544
Cdd:PRK07798     7 DLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3545 HPASRHEEIFEQTGAQVVVASAQYSARW------TSSSCHVVTVSKALSSQLP--------AVVDSTNTSVRPENAA--- 3607
Cdd:PRK07798    87 YVEDELRYLLDDSDAVALVYEREFAPRVaevlprLPKLRTLVVVEDGSGNDLLpgavdyedALAAGSPERDFGERSPddl 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3608 YIIFTSGSTGVPKGVVLEHRAVATSCLGhGRAFG----ITNLSRVLQFA-----SYTFDAC-------IAEIITTLLCGG 3671
Cdd:PRK07798   167 YLLYTGGTTGMPKGVMWRQEDIFRVLLG-GRDFAtgepIEDEEELAKRAaagpgMRRFPAPplmhgagQWAAFAALFSGQ 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3672 CICVPSDS--DRRNSLA-----KAISTMDVNWAFLTPSVARLLDPG--LIPSLKILAIGGEQSSSADWNRWPGSVQKIHV 3742
Cdd:PRK07798   246 TVVLLPDVrfDADEVWRtiereKVNVITIVGDAMARPLLDALEARGpyDLSSLFAIASGGALFSPSVKEALLELLPNVVL 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3743 ---YGPTEccifcTGY----TTKQGFEPSTIGTSVASVSWVVDPENHNRLAPlGS--MGELLMEGPIlARGYLNDVDKTE 3813
Cdd:PRK07798   326 tdsIGSSE-----TGFggsgTVAKGAVHTGGPRFTIGPRTVVLDEDGNPVEP-GSgeIGWIARRGHI-PLGYYKDPEKTA 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3814 AAFiddpawllegypghPGRQGRLYK-TGDLVQYNADGNLVYLGRkDSQ-VKVRGQRVELGEVEhhvrECLpeARQLAVE 3891
Cdd:PRK07798   399 ETF--------------PTIDGVRYAiPGDRARVEADGTITLLGR-GSVcINTGGEKVFPEEVE----EAL--KAHPDVA 457
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1820002560 3892 ----VILPS---GQKdhamLAAFVQLEEGTQ 3915
Cdd:PRK07798   458 dalvVGVPDerwGQE----VVAVVQLREGAR 484
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
7617-8021 1.82e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 90.40  E-value: 1.82e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQ-LGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 7695
Cdd:PRK08314    20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7696 HEEIFEQTGAQVVVASAQYSAR--------------------------------WTSSSCH--------VVTVSKALSSQ 7735
Cdd:PRK08314   100 LAHYVTDSGARVAIVGSELAPKvapavgnlrlrhvivaqysdylpaepeiavpaWLRAEPPlqalapggVVAWKEALAAG 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7736 LPAvvdsTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYtFD--ACIAEIITTL 7813
Cdd:PRK08314   180 LAP----PPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHvtGMVHSMNAPI 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7814 LCGGCICVPSDSDRRnSLAKAISTMDV-NWAFLTPSVARLL-DPGL----IPSLKILAIGGEQSSSADWNRWPG--SVQK 7885
Cdd:PRK08314   255 YAGATVVLMPRWDRE-AAARLIERYRVtHWTNIPTMVVDFLaSPGLaerdLSSLRYIGGGGAAMPEAVAERLKEltGLDY 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7886 IHVYGPTECCIFcTGYTTKQGFEPSTIGTSVASV-SWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFID 7964
Cdd:PRK08314   334 VEGYGLTETMAQ-THSNPPDRPKLQCLGIPTFGVdARVIDPETLEELPP-GEVGEIVVHGPQVFKGYWNRPEATAEAFIE 411
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 7965 dpawlLEGypghpgrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 8021
Cdd:PRK08314   412 -----IDG--------KRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE 455
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
5632-6051 1.85e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 90.61  E-value: 1.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 5711
Cdd:PRK07786    27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5712 EDTFRHTGAQVVVTSA-----QHSARWIGTNHQVVTVSAGS-----LGqLSTLVNPVGLPA----IPENA-VYIMFTSGS 5776
Cdd:PRK07786   107 AFLVSDCGAHVVVTEAalapvATAVRDIVPLLSTVVVAGGSsddsvLG-YEDLLAEAGPAHapvdIPNDSpALIMYTSGT 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5777 TGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFD-ACMDEIITTLMYGGCICV-PSDSDRRNDLVKAISTMD 5854
Cdd:PRK07786   186 TGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHiAGIGSMLPGLLLGAPTVIyPLGAFDPGQLLDVLEAEK 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5855 VSCALLTPS--VARLLEPSSVP-TLQMLVLQgeqvsfadWNRWPAS-------------VQTINGYGPTECSICCNTYSG 5918
Cdd:PRK07786   266 VTGIFLVPAqwQAVCAEQQARPrDLALRVLS--------WGAAPASdtllrqmaatfpeAQILAAFGQTEMSPVTCMLLG 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5919 KQGF-KSGIIGTSVASVSW-VVDPENHDrlAPLGSIGELLVEGPILARGYLNDIQKTAAVFiddpawllegypghpgrQG 5996
Cdd:PRK07786   338 EDAIrKLGSVGKVIPTVAArVVDENMND--VPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-----------------AG 398
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 5997 RLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhHVRECLPEARQLAV 6051
Cdd:PRK07786   399 GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVE-NVLASHPDIVEVAV 452
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
3470-3977 1.94e-17

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 89.92  E-value: 1.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3470 QAKARPHAPAICAWDGELTYGELDALSSKLASHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 3548
Cdd:PRK06839    11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3549 RHEEIFEQTGAQVVVASAQYSA-----RWTSSSCHVVTVS--KALSSQLPAVVDSTNtsvrpENAAYII-FTSGSTGVPK 3620
Cdd:PRK06839    91 ELIFQLKDSGTTVLFVEKTFQNmalsmQKVSYVQRVISITslKEIEDRKIDNFVEKN-----ESASFIIcYTSGTTGKPK 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3621 GVVLE---------HRAVATSCLGHGRAFGITNLSRVLQFASYTFdaciaeiiTTLLCGGCICVPSDSDRRNSLaKAIST 3691
Cdd:PRK06839   166 GAVLTqenmfwnalNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAF--------PTLFAGGVIIVPRKFEPTKAL-SMIEK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3692 MDVNWAFLTPSVARlldpGLIPSLKILaiggeqSSSADWNRW------PGSVQKIHVYGPteccifcTGYTTKQGF---- 3761
Cdd:PRK06839   237 HKVTVVMGVPTIHQ----ALINCSKFE------TTNLQSVRWfynggaPCPEELMREFID-------RGFLFGQGFgmte 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3762 ---------------EPSTIGTSVASVSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFiddpawlleg 3826
Cdd:PRK06839   300 tsptvfmlseedarrKVGSIGKPVLFCDYELIDENKNKVEV-GEVGELLIRGPNVMKEYWNRPDATEETI---------- 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3827 ypghpgRQGRLYkTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPS---GQKDHam 3903
Cdd:PRK06839   369 ------QDGWLC-TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINK-LSDVYEVAV-VGRQHvkwGEIPI-- 437
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 3904 laAFVQLEEGTqnalldkeaggedsmaqVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREI 3977
Cdd:PRK06839   438 --AFIVKKSSS-----------------VLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
5935-6231 2.26e-17

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 87.11  E-value: 2.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5935 SWVVDPENHDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPAWLLEGYPGHPGRQGRlyktgdlvRYDANGNLV 6014
Cdd:COG3433     23 AIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDL--------RLLLRRGLG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6015 CLGRKDSQVKLRGQRVELGEVEHHVRECLPEARQLAVEvilpsgqkdhamlaafvqLEEGTQNALLDKEASGEDSMAQVV 6094
Cdd:COG3433     95 PGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAV------------------LAALRGAGVGLLLIVGAVAALDGL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6095 FLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLreigasfTAQQIANMQTSSQDPKRQPSTEAEQTMQKLWA 6174
Cdd:COG3433    157 AAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAP-------ALAAAEALLAAASPAPALETALTEEELRADVA 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 6175 QVLGIELNGIGLDDSFFRLGGDSIAAMKLVGEARRIGLQLSVADIFRYARLVDLASL 6231
Cdd:COG3433    230 ELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWAL 286
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
3464-3968 2.34e-17

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 90.33  E-value: 2.34e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3464 HDLFTEQAKARPHAPAICaWDGE-------LTYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVL 3532
Cdd:cd17634     56 ANALDRHLRENGDRTAII-YEGDdtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVaiymPMIPE----AAVAMLACA 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3533 KAGGAFVPL----DPDHPASRheeiFEQTGAQVVVASAQYSARWTSSSCHVVtVSKALSSQLPA-----VVDSTNTSVR- 3602
Cdd:cd17634    131 RIGAVHSVIfggfAPEAVAGR----IIDSSSRLLITADGGVRAGRSVPLKKN-VDDALNPNVTSvehviVLKRTGSDIDw 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3603 -------------------------PENAAYIIFTSGSTGVPKGVVLEHRavatsclGHgrafgitnLSRVLQFASYTFD 3657
Cdd:cd17634    206 qegrdlwwrdliakaspehqpeamnAEDPLFILYTSGTTGKPKGVLHTTG-------GY--------LVYAATTMKYVFD 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3658 ACIAEIITT------------LLCGGCIC---------VPS--DSDRrnsLAKAISTMDVNWAFLTPSVARLLDPGL--- 3711
Cdd:cd17634    271 YGPGDIYWCtadvgwvtghsyLLYGPLACgattllyegVPNwpTPAR---MWQVVDKHGVNILYTAPTAIRALMAAGdda 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3712 -----IPSLKILAIGGEQSSSADWnRW------PGSVQKIHVYGPTECCIFCTgyTTKQGFEPSTIGTSVASV----SWV 3776
Cdd:cd17634    348 iegtdRSSLRILGSVGEPINPEAY-EWywkkigKEKCPVVDTWWQTETGGFMI--TPLPGAIELKAGSATRPVfgvqPAV 424
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3777 VDPENHNrlAPLGSMGELLMEGPI--LARGYLNDVDKTEAAFIDDpawlLEGYpghpgrqgrlYKTGDLVQYNADGNLVY 3854
Cdd:cd17634    425 VDNEGHP--QPGGTEGNLVITDPWpgQTRTLFGDHERFEQTYFST----FKGM----------YFSGDGARRDEDGYYWI 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3855 LGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVeVILPSGQKDHAmLAAFVQLeegtqnalldkEAGGEDSmaqvvf 3934
Cdd:cd17634    489 TGRSDDVINVAGHRLGTAEIE-SVLVAHPKVAEAAV-VGIPHAIKGQA-PYAYVVL-----------NHGVEPS------ 548
                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1820002560 3935 lASVEEELAKRLPEHMVPTVFFSLLHF----PTTTSGK 3968
Cdd:cd17634    549 -PELYAELRNWVRKEIGPLATPDVVHWvdslPKTRSGK 585
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
1931-2464 2.37e-17

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 90.63  E-value: 2.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1931 VHDLFTEQAKARPHAPAIcAWDGE------LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGG 2004
Cdd:cd05968     63 VEQLLDKWLADTRTRPAL-RWEGEdgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2005 AFVPL----DPDHPASRHE----------DIFRQTGAQVVVT-SAQHSARWIGTNHQVVTVSAGSLEQFSTLVNPVDLP- 2068
Cdd:cd05968    142 IVVPIfsgfGKEAAATRLQdaeakalitaDGFTRRGREVNLKeEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDe 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2069 -----------AKPENAAYVMFTSGSTGTPKGVVLEHRAV-VTSCLGHGQAFGVTNLLRALQFTAYTFDVCIAEIITTLV 2136
Cdd:cd05968    222 eketagdgaerTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLI 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2137 HGGCIC----VPsDSERRDNLAKAITDMQVNWGYLTSSVARLL-----DPCLVPSLKVL-VLG--GEQVNSTDWgKW--- 2201
Cdd:cd05968    302 LGATMVlydgAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALkprgdAPVNAHDLSSLrVLGstGEPWNPEPW-NWlfe 379
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2202 ---PSSVQTINGYGPTE------CCVFCTGYTGIqGFQSGNIGTSIAsvswVVDPEnhGRLAPlGSIGELLVEGPI--LA 2270
Cdd:cd05968    380 tvgKGRNPIINYSGGTEisggilGNVLIKPIKPS-SFNGPVPGMKAD----VLDES--GKPAR-PEVGELVLLAPWpgMT 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2271 RGYLNDVDKTQAAFID--DPAWLlegypgHegrqgrlyktGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRK 2348
Cdd:cd05968    452 RGFWRDEDRYLETYWSrfDNVWV------H----------GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNA 515
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2349 CLPEANQLAVEVVPP-SGERDHamlaAFIRLDDETRNSPliikyaednstaqivfltGIEEELSERLPQHM----VPTVF 2423
Cdd:cd05968    516 HPAVLESAAIGVPHPvKGEAIV----CFVVLKPGVTPTE------------------ALAEELMERVADELgkplSPERI 573
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 2424 FALVHFPTTTSGKTDRKRLReigASFTAQQLAEMrTSSEGP 2464
Cdd:cd05968    574 LFVKDLPKTRNAKVMRRVIR---AAYLGKELGDL-SSLENP 610
PRK09274 PRK09274
peptide synthase; Provisional
3467-3869 2.40e-17

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 89.96  E-value: 2.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3467 FTEQAKARPHAPAICAWDG----------ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGG 3536
Cdd:PRK09274    12 LPRAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3537 AFVPLDPDHPASRHEEIFEQTGAQVVV--ASAQYSARW----TSSSCHVVTVSKALS------SQLPAVVDSTNTSVR-- 3602
Cdd:PRK09274    92 VPVLVDPGMGIKNLKQCLAEAQPDAFIgiPKAHLARRLfgwgKPSVRRLVTVGGRLLwggttlATLLRDGAAAPFPMAdl 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3603 -PENAAYIIFTSGSTGVPKGVVLEHR---AVATScLGHgrAFGITNLSRVLQ----FAsyTFDACiaeiittllCGGCIC 3674
Cdd:PRK09274   172 aPDDMAAILFTSGSTGTPKGVVYTHGmfeAQIEA-LRE--DYGIEPGEIDLPtfplFA--LFGPA---------LGMTSV 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3675 VP---------SDSDRrnsLAKAISTMDVNWAFLTPSV-ARLLDPGL-----IPSLKILAIGGEQSSSADWNRW----PG 3735
Cdd:PRK09274   238 IPdmdptrpatVDPAK---LFAAIERYGVTNLFGSPALlERLGRYGEangikLPSLRRVISAGAPVPIAVIERFramlPP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3736 SVQKIHVYGPTEC----------CIFCTGYTTKQGfEPSTIGTSVASVSWVV-----DPENH---NRLAPLGSMGELLME 3797
Cdd:PRK09274   315 DAEILTPYGATEAlpissiesreILFATRAATDNG-AGICVGRPVDGVEVRIiaisdAPIPEwddALRLATGEIGEIVVA 393
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 3798 GPILARGYLNDVDKTEAAFIDDpawllegypghpGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRV 3869
Cdd:PRK09274   394 GPMVTRSYYNRPEATRLAKIPD------------GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
7580-8114 2.64e-17

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 90.33  E-value: 2.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7580 VADIDTTTPEDRQQLWA------WNADVPPAIERCVHDLFAEQARARPGAPAICaWDGE-------LTYGELDVLSSNLA 7646
Cdd:cd17634     20 GKILDWITPYQKVKNTSfapgapSIKWFEDATLNLAANALDRHLRENGDRTAII-YEGDdtsqsrtISYRELHREVCRFA 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7647 GHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAGGAFVPL----DPDHPASRheeiFEQTGAQVVVASAQYSARW 7718
Cdd:cd17634     99 GTLLDLGVKKGDRVaiymPMIPE----AAVAMLACARIGAVHSVIfggfAPEAVAGR----IIDSSSRLLITADGGVRAG 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7719 TSSSCHVVtVSKALSSQLPA-----VVDSTNTSVR--------------------------PENAAYIIFTSGSTGVPKG 7767
Cdd:cd17634    171 RSVPLKKN-VDDALNPNVTSvehviVLKRTGSDIDwqegrdlwwrdliakaspehqpeamnAEDPLFILYTSGTTGKPKG 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7768 VVLEHRavatsclGHgrafgitnLSRVLQFASYTFDACIAEIITT------------LLCGGCIC---------VPS--D 7824
Cdd:cd17634    250 VLHTTG-------GY--------LVYAATTMKYVFDYGPGDIYWCtadvgwvtghsyLLYGPLACgattllyegVPNwpT 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7825 SDRrnsLAKAISTMDVNWAFLTPSVARLLDPGL--------IPSLKILAIGGEQSSSADWnRW------PGSVQKIHVYG 7890
Cdd:cd17634    315 PAR---MWQVVDKHGVNILYTAPTAIRALMAAGddaiegtdRSSLRILGSVGEPINPEAY-EWywkkigKEKCPVVDTWW 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7891 PTECCIFCTgyTTKQGFEPSTIGTSVASV----SWVVDPENHNrlAPLGSMGELLMEGPI--LARGYLNDVDKTEAAFID 7964
Cdd:cd17634    391 QTETGGFMI--TPLPGAIELKAGSATRPVfgvqPAVVDNEGHP--QPGGTEGNLVITDPWpgQTRTLFGDHERFEQTYFS 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7965 DpawlLEGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVeVILPSGQ 8044
Cdd:cd17634    467 T----FKGM----------YFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIE-SVLVAHPKVAEAAV-VGIPHAI 530
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 8045 KNHAMLAvFVQLgkgthiahleeKAGGEDSmaqvvflTGTEEELAKRLPKHMVPTVFFALLHF----PMTTSGK 8114
Cdd:cd17634    531 KGQAPYA-YVVL-----------NHGVEPS-------PELYAELRNWVRKEIGPLATPDVVHWvdslPKTRSGK 585
PRK07787 PRK07787
acyl-CoA synthetase; Validated
1939-2343 3.40e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 88.89  E-value: 3.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGELTYGELDALSSKLAShlvqlGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 2018
Cdd:PRK07787    10 AAAADIADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAER 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2019 EDIFRQTGAQVVVTSAQHSARwiGTNHQVVTVSAGSLEQFStlvnpvdlPAKPENAAYVMFTSGSTGTPKGVVLEHRAvV 2098
Cdd:PRK07787    85 RHILADSGAQAWLGPAPDDPA--GLPHVPVRLHARSWHRYP--------EPDPDAPALIVYTSGTTGPPKGVVLSRRA-I 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2099 TSCLG-----------------------HGQAFGVTNLLR---ALQFTAYTFDVCIAEIIT---TLVHGgcicVPSDSER 2149
Cdd:PRK07787   154 AADLDalaeawqwtaddvlvhglplfhvHGLVLGVLGPLRignRFVHTGRPTPEAYAQALSeggTLYFG----VPTVWSR 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2150 --RD-NLAKAITDmqvnwgyltssvARLL----DPCLVPSLKVLV-LGGEQVnstdwgkwpssvqtINGYGPTECCVFCT 2221
Cdd:PRK07787   230 iaADpEAARALRG------------ARLLvsgsAALPVPVFDRLAaLTGHRP--------------VERYGMTETLITLS 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2222 gyTGIQG-FQSGNIGTSIASVSWVVDPENHGRLAPLG-SIGELLVEGPILARGYLNDVDKTQAAFIDDpAWllegypghe 2299
Cdd:PRK07787   284 --TRADGeRRPGWVGLPLAGVETRLVDEDGGPVPHDGeTVGELQVRGPTLFDGYLNRPDATAAAFTAD-GW--------- 351
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 2300 grqgrlYKTGDLVRYSSDGNLVCLGRKDSQ-VKVRGQRVELGEVE 2343
Cdd:PRK07787   352 ------FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIE 390
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
1508-1897 3.61e-17

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 88.59  E-value: 3.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1508 PCSPLQEGLMSLTAKRAGD--YIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQV----------VI 1575
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGpaYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEilppgpapleVR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1576 EENIQWTEPKS-LEEYLSEDKAVSVGL-GDPLARyAFVKEACGGKRWFVWTIHHAVYDGWSLPLI--------------- 1638
Cdd:cd19539     83 DLSDPDSDRERrLEELLRERESRGFDLdEEPPIR-AVLGRFDPDDHVLVLVAHHTAFDAWSLDVFardlaalyaarrkgp 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1639 ---LHAVKQVYsGGVLQWQPsfnafiQYLGQQDLEATVAYWQTALADCEAVLFPTLPP---------TVTQPVADATVEY 1706
Cdd:cd19539    162 aapLPELRQQY-KEYAAWQR------EALAAPRAAELLDFWRRRLRGAEPTALPTDRPrpagfpypgADLRFELDAELVA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1707 QCPPLSKATSDTTTSTLIrAAWAIVTSRYTTSDDVVFGTTVTGRNTPvtGVEAMVGPTIATVPVRLRVQRDQTVFAFLQG 1786
Cdd:cd19539    235 ALRELAKRARSSLFMVLL-AAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLIAR 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1787 LQQQATDMIAHEQTGLQRIAKmGQGPQHACS----FQTLLVVQPV-DDVLDNTLG-EWRDHSELQEFTTYTLMLQCMLAA 1860
Cdd:cd19539    312 VRKALVDAQRHQELPFQQLVA-ELPVDRDAGrhplVQIVFQVTNApAGELELAGGlSYTEGSDIPDGAKFDLNLTVTEEG 390
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1820002560 1861 EGVQITASFDTRVIEKWVVEKMLRQFSFIMQQLAEAG 1897
Cdd:cd19539    391 TGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
1507-1832 3.83e-17

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 88.20  E-value: 3.83e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1507 YPCSPLQEGlMSLTAKRAGD---YIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHsELGLLQVVIEEN----- 1578
Cdd:cd19533      2 LPLTSAQRG-VWFAEQLDPEgsiYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWIDPYTpvpir 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1579 -IQWTEP----KSLEEYLSEDKAVSVGL-GDPLARYAFVKeaCGGKRWFVW-TIHHAVYDGWSLPLILHAVKQVY----S 1647
Cdd:cd19533     80 hIDLSGDpdpeGAAQQWMQEDLRKPLPLdNDPLFRHALFT--LGDNRHFWYqRVHHIVMDGFSFALFGQRVAEIYtallK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1648 GGVLQWQP--SFNAFI----QYLGQQDLEATVAYWQTALADC-EAVLFPT---------------LPPTVTQPVADAtve 1705
Cdd:cd19533    158 GRPAPPAPfgSFLDLVeeeqAYRQSERFERDRAFWTEQFEDLpEPVSLARrapgrslaflrrtaeLPPELTRTLLEA--- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1706 yqcpplSKATSDTTTSTLIrAAWAIVTSRYTTSDDVVFGTTVTGRntpvTGVEA--MVGPTIATVPVRLRVQRDQTVFAF 1783
Cdd:cd19533    235 ------AEAHGASWPSFFI-ALVAAYLHRLTGANDVVLGVPVMGR----LGAAArqTPGMVANTLPLRLTVDPQQTFAEL 303
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 1784 LQGLQQQATDMIAHEQ---TGLQRIAKMGQGPQHAcsFQTLLVVQPVDDVLD 1832
Cdd:cd19533    304 VAQVSRELRSLLRHQRyryEDLRRDLGLTGELHPL--FGPTVNYMPFDYGLD 353
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
1527-1899 3.94e-17

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 88.18  E-value: 3.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1527 YIMQSVLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSElGLLQVVIEE---NIQWTEPKSLEEYLSEDKAVSVG--- 1600
Cdd:cd19531     24 YNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDG-EPVQVILPPlplPLPVVDLSGLPEAEREAEAQRLAree 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1601 ------LG-DPLARYAFVKeaCGGKRW-FVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQWQPSFNAF-IQY-------- 1663
Cdd:cd19531    103 arrpfdLArGPLLRATLLR--LGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPPLpIQYadyavwqr 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1664 --LGQQDLEATVAYWQTALADCEAVL-FPT-LPPTVTQPVADATVEYQCPP--------LSKATsDTTTSTLIRAAWAIV 1731
Cdd:cd19531    181 ewLQGEVLERQLAYWREQLAGAPPVLeLPTdRPRPAVQSFRGARVRFTLPAeltaalraLARRE-GATLFMTLLAAFQVL 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1732 TSRYTTSDDVVFGTTVTGRNTPvtGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAH---------EQTGL 1802
Cdd:cd19531    260 LHRYSGQDDIVVGTPVAGRNRA--ELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAYAHqdlpfeklvEALQP 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1803 QRiaKMGQGPQhacsFQTLLVVQPVDDVLDNTLGewrDHSELQEFTTYT----LMLQCMLAAEGVQITASFDTRVIEKWV 1878
Cdd:cd19531    338 ER--DLSRSPL----FQVMFVLQNAPAAALELPG---LTVEPLEVDSGTakfdLTLSLTETDGGLRGSLEYNTDLFDAAT 408
                          410       420
                   ....*....|....*....|.
gi 1820002560 1879 VEKMLRQFsfimQQLAEAGAE 1899
Cdd:cd19531    409 IERMAGHF----QTLLEAIVA 425
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
5198-5590 4.09e-17

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 88.21  E-value: 4.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5198 PCSPLQEGLMSLTAKRAGD--YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQV----------VV 5265
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGpaYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEilppgpapleVR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5266 EEKIQWTESKR-LEEYLREdkavSMGLGDRLARYALIKE---PYDGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGA- 5340
Cdd:cd19539     83 DLSDPDSDRERrLEELLRE----RESRGFDLDEEPPIRAvlgRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARr 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5341 ------VPERQPSFNAFI----QYLGQQDLEAATLYWQTALADCKAALFPTLPPTVTQPVADTTVEYQCPPPS------- 5403
Cdd:cd19539    159 kgpaapLPELRQQYKEYAawqrEALAAPRAAELLDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAElvaalre 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5404 -QSATDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQS 5482
Cdd:cd19539    239 lAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKAL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5483 TDMIAHEQTGLQRIAK-----MSPGARHAcgFQTLLVVQPTDDVLGSDDMLGEWRSYSEMQDFTTYALMVQCTLAKDRVE 5557
Cdd:cd19539    317 VDAQRHQELPFQQLVAelpvdRDAGRHPL--VQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLR 394
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1820002560 5558 VTASFDARVIEQWVVEKMLRQFGFVMQQLAEAG 5590
Cdd:cd19539    395 GSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
PRK05857 PRK05857
fatty acid--CoA ligase;
3453-3889 4.32e-17

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 89.30  E-value: 4.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3453 ADVPPAI-ERCVhdlftEQAKARPHAPAICAWDG--ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAML 3529
Cdd:PRK05857    10 PQLPSTVlDRVF-----EQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3530 AVLKAGGAFVPLDPDHPA---SRHEEIFEQTGAQV-----VVASAQYSARWTSSSCHVVTVSKALSSQLPAVVD--STNT 3599
Cdd:PRK05857    85 ACAKLGAIAVMADGNLPIaaiERFCQITDPAAALVapgskMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAAslAGNA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3600 SVRPENAAYIIFTSGSTGVPKGVVLEHR---AVATSClghgRAFGITNLSRVLQFASY-----TFDACIAEIITTLLCGG 3671
Cdd:PRK05857   165 DQGSEDPLAMIFTSGTTGEPKAVLLANRtffAVPDIL----QKEGLNWVTWVVGETTYsplpaTHIGGLWWILTCLMHGG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3672 -CIcvpSDSDRRNSLAKAISTMDVNWAFLTPSVARLLDPGL------IPSLKILAIGGEQSSSADWnRW--PGSVQKIHV 3742
Cdd:PRK05857   241 lCV---TGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELksanatVPSLRLVGYGGSRAIAADV-RFieATGVRTAQV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3743 YGPTE--CCIFC--TGYTTKQGFEPSTIGTSVASVSWVVDPENHN-----RLAPLGSMGELLMEGPILARGYLNDVDKTE 3813
Cdd:PRK05857   317 YGLSEtgCTALClpTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIgptapGAGPSASFGTLWIKSPANMLGYWNNPERTA 396
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 3814 AAFIDdpAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLA 3889
Cdd:PRK05857   397 EVLID--GWV---------------NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGVSGVREAA 454
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
3471-3875 4.54e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 89.25  E-value: 4.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQ-LGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 3549
Cdd:PRK08314    20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3550 HEEIFEQTGAQVVVASAQYSAR--------------------------------WTSSSCH--------VVTVSKALSSQ 3589
Cdd:PRK08314   100 LAHYVTDSGARVAIVGSELAPKvapavgnlrlrhvivaqysdylpaepeiavpaWLRAEPPlqalapggVVAWKEALAAG 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3590 LPAvvdsTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYtFD--ACIAEIITTL 3667
Cdd:PRK08314   180 LAP----PPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHvtGMVHSMNAPI 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3668 LCGGCICVPSDSDRRnSLAKAISTMDV-NWAFLTPSVARLL-DPGL----IPSLKILAIGGEQSSSADWNRWPG--SVQK 3739
Cdd:PRK08314   255 YAGATVVLMPRWDRE-AAARLIERYRVtHWTNIPTMVVDFLaSPGLaerdLSSLRYIGGGGAAMPEAVAERLKEltGLDY 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3740 IHVYGPTECCIFcTGYTTKQGFEPSTIGTSVASV-SWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFID 3818
Cdd:PRK08314   334 VEGYGLTETMAQ-THSNPPDRPKLQCLGIPTFGVdARVIDPETLEELPP-GEVGEIVVHGPQVFKGYWNRPEATAEAFIE 411
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 3819 dpawlLEGypghpgrqGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 3875
Cdd:PRK08314   412 -----IDG--------KRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE 455
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
3487-3976 4.54e-17

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 88.21  E-value: 4.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHPASRHEE---IFEQTGAQVVV 3563
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFREHElafILRRAKAKVFV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3564 AsaqysarwtssschvvtvskalssqlPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGIT 3643
Cdd:cd05903     79 V--------------------------PERFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3644 NLSRVLQFASYtfdACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFL----TPSVARLLD-----PGLIPS 3714
Cdd:cd05903    133 PGDVFLVASPM---AHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFmmgaTPFLTDLLNaveeaGEPLSR 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3715 LKILAIGG--------EQSSSAdwnrwpGSVQKIHVYGPTECCIFCTGYT-TKQGFEPSTIGTSVASVSWVVDPENHNRL 3785
Cdd:cd05903    210 LRTFVCGGatvprslaRRAAEL------LGAKVCSAYGSTECPGAVTSITpAPEDRRLYTDGRPLPGVEIKVVDDTGATL 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3786 APlGSMGELLMEGPILARGYLNDVDKTEAAFIDdpAWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVR 3865
Cdd:cd05903    284 AP-GVEGELLSRGPSVFLGYLDRPDLTADAAPE--GW---------------FRTGDLARLDEDGYLRITGRSKDIIIRG 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3866 GQRVELGEVEhhvrECL---PEARQLAVeVILPS---GQKdhamLAAFVQLEEGtqnALLDKEAGGEdsmaqvvFLASVe 3939
Cdd:cd05903    346 GENIPVLEVE----DLLlghPGVIEAAV-VALPDerlGER----ACAVVVTKSG---ALLTFDELVA-------YLDRQ- 405
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 3940 eELAK-RLPEHMVptvffSLLHFPTTTSGKTDRKRLRE 3976
Cdd:cd05903    406 -GVAKqYWPERLV-----HVDDLPRTPSGKVQKFRLRE 437
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
428-723 4.55e-17

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 87.88  E-value: 4.55e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  428 SPLQEG-----LMSlttkRAGD-YIMQDVLEL--RADVDehAFRAAWEYVVQSIAVLRTRIvqHSElGL---LQVV---- 492
Cdd:cd19544      5 APLQEGilfhhLLA----EEGDpYLLRSLLAFdsRARLD--AFLAALQQVIDRHDILRTAI--LWE-GLsepVQVVwrqa 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  493 ---VEEkMQWTESESLEEYLNEDKAASMGLGDrLARYALIK----ESCGGKRWFV-WTIHHALYDGWSLPLVLDAVKQVY 564
Cdd:cd19544     76 elpVEE-LTLDPGDDALAQLRARFDPRRYRLD-LRQAPLLRahvaEDPANGRWLLlLLFHHLISDHTSLELLLEEIQAIL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  565 SG--AALERQPSFNTFIQYV-SQQDVKAAAAYWQTALADceavlfpplpstVTQPVA-----------DTTVKYQCPPSP 630
Cdd:cd19544    154 AGraAALPPPVPYRNFVAQArLGASQAEHEAFFREMLGD------------VDEPTApfglldvqgdgSDITEARLALDA 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  631 EVTSS--------NITTSTLIRAAWAIIASRYTSSEDIVFGTTVTGRNAPITGVEAMVGPTIATVPLRVRpRKGQTVSAF 702
Cdd:cd19544    222 ELAQRlraqarrlGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVR-LGGRSVREA 300
                          330       340
                   ....*....|....*....|....
gi 1820002560  703 LENLQQQATEMIAYEQTGL---QR 723
Cdd:cd19544    301 VRQTHARLAELLRHEHASLalaQR 324
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
1939-2395 4.58e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 89.25  E-value: 4.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQ-LGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 2017
Cdd:PRK08314    20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2018 HEDIFRQTGAQVVVTSAQHSAR------WIGTNHQVVTVSAGSLEQFSTLVNPVDLPAKPENAAY--------------- 2076
Cdd:PRK08314   100 LAHYVTDSGARVAIVGSELAPKvapavgNLRLRHVIVAQYSDYLPAEPEIAVPAWLRAEPPLQALapggvvawkealaag 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2077 --------------VM-FTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVT---NLLRALQFtaytFDVciaeiiTTLVH- 2137
Cdd:PRK08314   180 lappphtagpddlaVLpYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTpesVVLAVLPL----FHV------TGMVHs 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2138 -------GGCICVPSDSErRDNLAKAITDMQV-NWGYLTSSVARLL-DPCL----VPSLKVLVLGGEQVnstdwgkwPSS 2204
Cdd:PRK08314   250 mnapiyaGATVVLMPRWD-REAAARLIERYRVtHWTNIPTMVVDFLaSPGLaerdLSSLRYIGGGGAAM--------PEA 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2205 V------QT----INGYGPTE---------------CCVfctgytGIQGFqsgniGTSiasvSWVVDPENhGRLAPLGSI 2259
Cdd:PRK08314   321 VaerlkeLTgldyVEGYGLTEtmaqthsnppdrpklQCL------GIPTF-----GVD----ARVIDPET-LEELPPGEV 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2260 GELLVEGPILARGYLNDVDKTQAAFIDdpawlLEGypghegrqGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVEL 2339
Cdd:PRK08314   385 GEIVVHGPQVFKGYWNRPEATAEAFIE-----IDG--------KRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWP 451
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 2340 GEVEHHMRKcLPEANQLAVEVVPPS--GERdhamLAAFIRLDDETRNSPL---IIKYAEDN 2395
Cdd:PRK08314   452 AEVENLLYK-HPAIQEACVIATPDPrrGET----VKAVVVLRPEARGKTTeeeIIAWAREH 507
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
7609-8135 5.33e-17

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 89.47  E-value: 5.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7609 VHDLFAEQARARPGAPAIcAWDGE------LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGG 7682
Cdd:cd05968     63 VEQLLDKWLADTRTRPAL-RWEGEdgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7683 AFVPL----DPDHPASRHE----------EIFEQTGAQV-VVASAQYSARWTSSSCHVVTVSKALSSQLPAVVD------ 7741
Cdd:cd05968    142 IVVPIfsgfGKEAAATRLQdaeakalitaDGFTRRGREVnLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRdlsyde 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7742 ------STNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAV---ATSCLGHGraFGITNLSRVLQFASYTFDACIAEIITT 7812
Cdd:cd05968    222 eketagDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFplkAAQDMYFQ--FDLKPGDLLTWFTDLGWMMGPWLIFGG 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7813 LLCGGCIC----VPsDSDRRNSLAKAISTMDVNWAFLTPSVARLLDP-GLIP-------SLKILAIGGEQSSSADWN--- 7877
Cdd:cd05968    300 LILGATMVlydgAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALKPrGDAPvnahdlsSLRVLGSTGEPWNPEPWNwlf 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7878 --RWPGSVQKIHVYGPTECC--IFCtGYTTKQgFEPSTIGTSVASVSWVVDPENHNRLAPlgSMGELLMEGPI--LARGY 7951
Cdd:cd05968    379 etVGKGRNPIINYSGGTEISggILG-NVLIKP-IKPSSFNGPVPGMKADVLDESGKPARP--EVGELVLLAPWpgMTRGF 454
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7952 LNDVDKTEAAFID--DPAWLlegypgHpgrqgrlyktGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE------HH 8023
Cdd:cd05968    455 WRDEDRYLETYWSrfDNVWV------H----------GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIEsvlnahPA 518
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8024 VREClpearqLAVEVilPSGQKNHAMLAvFVQLGKGthiahleekaggedsmaqVVFLTGTEEELAKRLPKHM----VPT 8099
Cdd:cd05968    519 VLES------AAIGV--PHPVKGEAIVC-FVVLKPG------------------VTPTEALAEELMERVADELgkplSPE 571
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1820002560 8100 VFFALLHFPMTTSGKADRKRLReigASFTAQQLAET 8135
Cdd:cd05968    572 RILFVKDLPKTRNAKVMRRVIR---AAYLGKELGDL 604
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
7633-8026 5.34e-17

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 88.88  E-value: 5.34e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD--PDHPASRHEE-----IFEQTGA 7705
Cdd:cd05906     40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvpPTYDEPNARLrklrhIWQLLGS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7706 QVVVASAQ---------YSARWTSSSCHVVTVSKALSSQLPAVVdstntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVA 7776
Cdd:cd05906    120 PVVLTDAElvaefagleTLSGLPGIRVLSIEELLDTAADHDLPQ------SRPDDLALLMLTSGSTGFPKAVPLTHRNIL 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7777 TSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGC--ICVPSDSDRRNSLA--KAIST--MDVNWA--FLTPS 7848
Cdd:cd05906    194 ARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCqqVHVPTEEILADPLRwlDLIDRyrVTITWApnFAFAL 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7849 VARLLD-----PGLIPSLKILAIGGEQSSSADWNRWPGSVQK-------IH-VYGPTECC---IFCTG---YTTKQGFEP 7909
Cdd:cd05906    274 LNDLLEeiedgTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPyglppdaIRpAFGMTETCsgvIYSRSfptYDHSQALEF 353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7910 STIGTSVASVSW-VVDPEnhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpAWllegypghpgrqgrlYKTGD 7988
Cdd:cd05906    354 VSLGRPIPGVSMrIVDDE--GQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED-GW---------------FRTGD 415
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1820002560 7989 LvQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVRE 8026
Cdd:cd05906    416 L-GFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEE 452
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3-284 7.34e-17

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 87.87  E-value: 7.34e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    3 VNWALLTPSVARLL-----EPSHIP-SLRILVMGGEQV--NSADWDRWPSSVQTINGYGPTECCIVCTGYTSEQDFTTGT 74
Cdd:cd05971    182 VTTAFLPPTALKMMrqqgeQLKHAQvKLRAIATGGESLgeELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPGS 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   75 IGTSI-ASVSWVVDpkDHGRLAPLGSVGELLVE--GPILARGYLSDPEKTAAVFINNpaWLLeghggyagrqgrlykTGD 151
Cdd:cd05971    262 MGKPIpGHRVAIVD--DNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD--WLL---------------TGD 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  152 LVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECL---PEAKQLAVeVVLP---LGQknhaTLAAFIQLDKGthn 225
Cdd:cd05971    323 LGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIE----ECLlkhPAVLMAAV-VGIPdpiRGE----IVKAFVVLNPG--- 390
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560  226 allkekVGGDDSIARvvflaGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLR 284
Cdd:cd05971    391 ------ETPSDALAR-----EIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
4551-5056 7.51e-17

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 88.46  E-value: 7.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTpAICAWDGE-----LTYGELDTLSSKLASHLVQLGVKPEDMVPLCfeksMWT----VVAMLAVLKAGGAFVPL 4621
Cdd:cd12119      6 ARLHGDR-EIVSRTHEgevhrYTYAEVAERARRLANALRRLGVKPGDRVATL----AWNthrhLELYYAVPGMGAVLHTI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4622 DPDHPASRHEHIFRQTGAQVVLASAQYATL-WTSLGR-----SVVIVSEASTSQLP----------VVTKTADPSVNP-- 4683
Cdd:cd12119     81 NPRLFPEQIAYIINHAEDRVVFVDRDFLPLlEAIAPRlptveHVVVMTDDAAMPEPagvgvlayeeLLAAESPEYDWPdf 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4684 -GNAAYAI-FTSGSTGIPKGVVLEHKAVVTSCLG--HGQAFGITDHTRVLqfasytfdaCIAEI---------ITTLLCC 4750
Cdd:cd12119    161 dENTAAAIcYTSGTTGNPKGVVYSHRSLVLHAMAalLTDGLGLSESDVVL---------PVVPMfhvnawglpYAAAMVG 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4751 GCICVPSDSDRRNNLAKAINAMDVNWALLTPSVARML------DPCVVQSLKILVLGGEQVNSADWDRW-PKSIQTINAY 4823
Cdd:cd12119    232 AKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLldhleaNGRDLSSLRRVVIGGSAVPRSLIEAFeERGVRVIHAW 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4824 GPTECSICCT--TYSGKQGFKSG--------TIGTSIVSVSW-VVDPENhNRLAPLG-SIGELLVEGPILARGYLNDMEK 4891
Cdd:cd12119    312 GMTETSPLGTvaRPPSEHSNLSEdeqlalraKQGRPVPGVELrIVDDDG-RELPWDGkAVGELQVRGPWVTKSYYKNDEE 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4892 TEAAFIDDpaWLlegygghsgrqgrlyKTGDLVRYDADGNLVYLGR-KDSqVKLRGQ---RVELgE---VEH-HVREClt 4963
Cdd:cd12119    391 SEALTEDG--WL---------------RTGDVATIDEDGYLTITDRsKDV-IKSGGEwisSVEL-EnaiMAHpAVAEA-- 449
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4964 eakqlAVeVIVPEGEGGYAMLAafvqlgddtyntLVKEKAGGDsltvqvVFLDRVEEELAKRVPEHMMLTTFFTLEAMPT 5043
Cdd:cd12119    450 -----AV-IGVPHPKWGERPLA------------VVVLKEGAT------VTAEELLEFLADKVAKWWLPDDVVFVDEIPK 505
                          570
                   ....*....|...
gi 1820002560 5044 TTSGKIDRKRLRE 5056
Cdd:cd12119    506 TSTGKIDKKALRE 518
PRK06164 PRK06164
acyl-CoA synthetase; Validated
856-1378 8.32e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 88.26  E-value: 8.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  856 DLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVV----PLCFEksmWtVVAMLAVLKAGGAFVP 931
Cdd:PRK06164    14 SLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVavwlPNCIE---W-VVLFLACARLGATVIA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  932 LDPGHpasRHEEI-----------------FKQIGAQVVLTSSQHAMLFASserHQVTVSKVSTSQLP------TVVNF- 987
Cdd:PRK06164    90 VNTRY---RSHEVahilgrgrarwlvvwpgFKGIDFAAILAAVPPDALPPL---RAIAVVDDAADATPapapgaRVQLFa 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  988 ---------AKSPVDPGNTAYIIFT-SGTTGIPKGVVLQHRAVttscLGHG----EAFGYTDHARVLQFASYTFDACIAE 1053
Cdd:PRK06164   164 lpdpappaaAGERAADPDAGALLFTtSGTTSGPKLVLHRQATL----LRHAraiaRAYGYDPGAVLLAALPFCGVFGFST 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1054 IITTLLYGG-CICVPSESDRRNnlAKAISTMDVNCALLTPSVARLL-----EPSAVPSLKRLVLQGEQVSFAD---WNRW 1124
Cdd:PRK06164   240 LLGALAGGApLVCEPVFDAART--ARALRRHRVTHTFGNDEMLRRIldtagERADFPSARLFGFASFAPALGElaaLARA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1125 PGSVQTiNGYGPTECsvccntysgkQGFKSGIIGTSVASLSW--------------VVDAGNhNRLAPLGSIGELLVEGP 1190
Cdd:PRK06164   318 RGVPLT-GLYGSSEV----------QALVALQPATDPVSVRIegggrpaspearvrARDPQD-GALLPDGESGEIEIRAP 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1191 ILARGYLNDIDKTEAAFIDDpawlleGYeghagrrgrlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVR 1270
Cdd:PRK06164   386 SLMRGYLDNPDATARALTDD------GY----------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALE 449
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1271 EClPEARQLAVEVILPSGQKEhalLAAFIQLDKGnhnalfeEKASGEDSMAQvvfltgveeeLAKRLPEHMVPTILFTVK 1350
Cdd:PRK06164   450 AL-PGVAAAQVVGATRDGKTV---PVAFVIPTDG-------ASPDEAGLMAA----------CREALAGFKVPARVQVVE 508
                          570       580       590
                   ....*....|....*....|....*....|.
gi 1820002560 1351 AMPITTSG---KIDRKRLQDIGASFTVQQLA 1378
Cdd:PRK06164   509 AFPVTESAngaKIQKHRLREMAQARLAAERA 539
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
1939-2464 9.51e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 88.30  E-value: 9.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 2018
Cdd:PRK07786    27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2019 EDIFRQTGAQVVVTSA-----QHSARWIGTNHQVVTVSAGSLEQ----FSTLVN-------PVDLPAkpENAAYVMFTSG 2082
Cdd:PRK07786   107 AFLVSDCGAHVVVTEAalapvATAVRDIVPLLSTVVVAGGSSDDsvlgYEDLLAeagpahaPVDIPN--DSPALIMYTSG 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2083 STGTPKGVVLEHRAVVTSCLGHGQAFGVtNLLRALQFTAYTF--DVCIAEIITTLVHGGCICV-PSDSERRDNLAKAITD 2159
Cdd:PRK07786   185 TTGRPKGAVLTHANLTGQAMTCLRTNGA-DINSDVGFVGVPLfhIAGIGSMLPGLLLGAPTVIyPLGAFDPGQLLDVLEA 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2160 MQVNWGYL--TSSVARLLDPCLVP-SLKVLVLGgeqvnstdWGKWPSS-------------VQTINGYGPTE----CCVF 2219
Cdd:PRK07786   264 EKVTGIFLvpAQWQAVCAEQQARPrDLALRVLS--------WGAAPASdtllrqmaatfpeAQILAAFGQTEmspvTCML 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2220 cTGYTGIQgfQSGNIGTSIASVSWVVDPENHGRLAPlGSIGELLVEGPILARGYLNDVDKTQAAFiddpawllegypghe 2299
Cdd:PRK07786   336 -LGEDAIR--KLGSVGKVIPTVAARVVDENMNDVPV-GEVGEIVYRAPTLMSGYWNNPEATAEAF--------------- 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2300 grQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEhhmrkclpeaNQLAvevvppsGERDHAMLAAFIRLD 2379
Cdd:PRK07786   397 --AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVE----------NVLA-------SHPDIVEVAVIGRAD 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2380 DETRNSPLIIkYAEDNSTAQIVfLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREigaSFTAQQLAEMRT 2459
Cdd:PRK07786   458 EKWGEVPVAV-AAVRNDDAALT-LEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE---RYGACVNVERRS 532

                   ....*
gi 1820002560 2460 SSEGP 2464
Cdd:PRK07786   533 ASAGF 537
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
7588-8130 9.63e-17

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 88.28  E-value: 9.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7588 PEDRQQLWAWNADVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKS 7667
Cdd:PRK06155     2 EPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7668 MWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSAR--------------WTSSSCHVVTVSKALS 7733
Cdd:PRK06155    82 IEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAAleaadpgdlplpavWLLDAPASVSVPAGWS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7734 -SQLPAVVDS-TNTSVRPENAAYIIFTSGSTGVPKGVVLEHR------AVATSCLGHGRA---------FGITNLSRVLQ 7796
Cdd:PRK06155   162 tAPLPPLDAPaPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAqfywwgRNSAEDLEIGADdvlyttlplFHTNALNAFFQ 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7797 -------------F-ASYTFDACIAEIIT-TLLCGGCICV-----PSDSDRRNSLAKAistmdvnwafltpsvarlldpg 7856
Cdd:PRK06155   242 allagatyvleprFsASGFWPAVRRHGATvTYLLGAMVSIllsqpARESDRAHRVRVA---------------------- 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7857 lipslkiLAIGGEQSSSADWNRWPGsVQKIHVYGPTECCIFCtgYTTKQGFEPSTIGTSVASV-SWVVDpeNHNRLAPLG 7935
Cdd:PRK06155   300 -------LGPGVPAALHAAFRERFG-VDLLDGYGSTETNFVI--AVTHGSQRPGSMGRLAPGFeARVVD--EHDQELPDG 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7936 SMGELLM---EGPILARGYLNDVDKTEAAFIDdpAWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGR-KDSqVKVR 8011
Cdd:PRK06155   368 EPGELLLradEPFAFATGYFGMPEKTVEAWRN--LW---------------FHTGDRVVRDADGWFRFVDRiKDA-IRRR 429
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8012 GQRVELGEVEHHVREclpearQLAVEVIlpsgqknhamlAVFVqlgkgthiahLEEKAGGEDSMAQVVFLTGTE---EEL 8088
Cdd:PRK06155   430 GENISSFEVEQVLLS------HPAVAAA-----------AVFP----------VPSELGEDEVMAAVVLRDGTAlepVAL 482
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 8089 AK----RLPKHMVPTVFFALLHFPMTTSGKADRKRLREIGasFTAQ 8130
Cdd:PRK06155   483 VRhcepRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQG--VTAD 526
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
854-1367 9.96e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 88.28  E-value: 9.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQL-GVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL 932
Cdd:PRK05677    26 IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNT 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  933 DPGHPASRHEEIFKQIGAQVVL---------------TSSQHA--------------MLFASSERHqvtVSK-VSTSQLP 982
Cdd:PRK05677   106 NPLYTAREMEHQFNDSGAKALVclanmahlaekvlpkTGVKHVivtevadmlpplkrLLINAVVKH---VKKmVPAYHLP 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  983 TVVNFAK----------SPVDPGN--TAYIIFTSGTTGIPKGVVLQHR----------AVTTSCLGHGEAFGYTDhARVL 1040
Cdd:PRK05677   183 QAVKFNDalakgagqpvTEANPQAddVAVLQYTGGTTGVAKGAMLTHRnlvanmlqcrALMGSNLNEGCEILIAP-LPLY 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1041 QFASYTFDaCIAeiitTLLYGG-CICVPSESDRR---NNLAK-------AISTMDVncALLTPSVARLLEPSAvpsLKRL 1109
Cdd:PRK05677   262 HIYAFTFH-CMA----MMLIGNhNILISNPRDLPamvKELGKwkfsgfvGLNTLFV--ALCNNEAFRKLDFSA---LKLT 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1110 VLQGEQVSFADWNRWPG--SVQTINGYGPTECS--VCCNTYSGKQgfkSGIIGTSVASLSWVV--DAGNHnrlAPLGSIG 1183
Cdd:PRK05677   332 LSGGMALQLATAERWKEvtGCAICEGYGMTETSpvVSVNPSQAIQ---VGTIGIPVPSTLCKVidDDGNE---LPLGEVG 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1184 ELLVEGPILARGYLNDIDKTEAAFiDDPAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELG 1263
Cdd:PRK05677   406 ELCVKGPQVMKGYWQRPEATDEIL-DSDGWL---------------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPN 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1264 EIEhHVRECLPEARQLAveVILPSGQKEHALLAAFIQLDKGnhNALFEEKasgedsmaqvvfltgVEEELAKRLPEHMVP 1343
Cdd:PRK05677   470 ELE-DVLAALPGVLQCA--AIGVPDEKSGEAIKVFVVVKPG--ETLTKEQ---------------VMEHMRANLTGYKVP 529
                          570       580
                   ....*....|....*....|....
gi 1820002560 1344 TILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:PRK05677   530 KAVEFRDELPTTNVGKILRRELRD 553
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
7616-8123 1.07e-16

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 87.61  E-value: 1.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7616 QARARPGAPAICAWDGELTYGELDVLSSNLAGHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 7694
Cdd:PRK06839    11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7695 RHEEIFEQTGAQVVVASAQYSA-----RWTSSSCHVVTVS--KALSSQLPAVVDSTNtsvrpENAAYII-FTSGSTGVPK 7766
Cdd:PRK06839    91 ELIFQLKDSGTTVLFVEKTFQNmalsmQKVSYVQRVISITslKEIEDRKIDNFVEKN-----ESASFIIcYTSGTTGKPK 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7767 GVVLE---------HRAVATSCLGHGRAFGITNLSRVLQFASYTFdaciaeiiTTLLCGGCICVPSDSDRRNSLaKAIST 7837
Cdd:PRK06839   166 GAVLTqenmfwnalNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAF--------PTLFAGGVIIVPRKFEPTKAL-SMIEK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7838 MDVNWAFLTPSVARlldpGLIPSLKILaiggeqSSSADWNRW------PGSVQKIHVYGPteccifcTGYTTKQGF---- 7907
Cdd:PRK06839   237 HKVTVVMGVPTIHQ----ALINCSKFE------TTNLQSVRWfynggaPCPEELMREFID-------RGFLFGQGFgmte 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7908 ---------------EPSTIGTSVASVSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFiddpawlleg 7972
Cdd:PRK06839   300 tsptvfmlseedarrKVGSIGKPVLFCDYELIDENKNKVEV-GEVGELLIRGPNVMKEYWNRPDATEETI---------- 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7973 ypghpgRQGRLYkTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVevilpsgqknhamlaV 8052
Cdd:PRK06839   369 ------QDGWLC-TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINK-LSDVYEVAV---------------V 425
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 8053 FVQLGKGTHIAHleekaggedsmAQVVFLTG---TEEELAK----RLPKHMVPTVFFALLHFPMTTSGKADRKRLREI 8123
Cdd:PRK06839   426 GRQHVKWGEIPI-----------AFIVKKSSsvlIEKDVIEhcrlFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
7603-8125 1.21e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 87.91  E-value: 1.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7603 PAIERCVHDLFAEQARARPGAPAICAWDGEL--TYGELDVLSSNLAGHLVQLGVNPEDVV----PLCFEksmWTVVAMlA 7676
Cdd:PRK12583    14 PLLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVgiwaPNCAE---WLLTQF-A 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7677 VLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQY-----------------SARWTSSSC-------HVVTVSKAL 7732
Cdd:PRK12583    90 TARIGAILVNINPAYRASELEYALGQSGVRWVICADAFktsdyhamlqellpglaEGQPGALACerlpelrGVVSLAPAP 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7733 SSQL--------------PAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLqfA 7798
Cdd:PRK12583   170 PPGFlawhelqargetvsREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLC--V 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7799 SYTFDACIAEIITTLLC---GGCICVPSDSDRRNSLAKAISTMDVNWAFLTPS--VARLLDPGL----IPSLKILAIGGE 7869
Cdd:PRK12583   248 PVPLYHCFGMVLANLGCmtvGACLVYPNEAFDPLATLQAVEEERCTALYGVPTmfIAELDHPQRgnfdLSSLRTGIMAGA 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7870 QSSSADWNRWPGSVQKIHV---YGPTECC--IFCTGYTTKQGFEPSTIGTSVASV-SWVVDPENHNrlAPLGSMGELLME 7943
Cdd:PRK12583   328 PCPIEVMRRVMDEMHMAEVqiaYGMTETSpvSLQTTAADDLERRVETVGRTQPHLeVKVVDPDGAT--VPRGEIGELCTR 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7944 GPILARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHH 8023
Cdd:PRK12583   406 GYSVMKGYWNNPEATAES-IDEDGWM---------------HTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEF 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8024 VrecLPEARQLAVEVILPSGQKNHAMLAVFVQLGKGtHIAhleekaggedsmaqvvfltgTEEELAK----RLPKHMVPT 8099
Cdd:PRK12583   470 L---FTHPAVADVQVFGVPDEKYGEEIVAWVRLHPG-HAA--------------------SEEELREfckaRIAHFKVPR 525
                          570       580
                   ....*....|....*....|....*.
gi 1820002560 8100 VFFALLHFPMTTSGKADRKRLREIGA 8125
Cdd:PRK12583   526 YFRFVDEFPMTVTGKVQKFRMREISI 551
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
4541-5057 1.21e-16

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 87.80  E-value: 1.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4541 RCVHDQFAEQARARPDTPAICAWDGE------LTYGELDTLSSKLASHLVQLGVKPEDMVPlCFEKSMWTVVAM-LAVLK 4613
Cdd:PRK13295    24 RTINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVS-CQLPNWWEFTVLyLACSR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4614 AGGAFVPLDPdhpasrhehIFRQTGAQVVLASAQYATL---------------------WTSLGRSVVIVSEASTS---- 4668
Cdd:PRK13295   103 IGAVLNPLMP---------IFRERELSFMLKHAESKVLvvpktfrgfdhaamarrlrpeLPALRHVVVVGGDGADSfeal 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4669 -------QLPVVTKT-ADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQ---FASYTFD 4737
Cdd:PRK13295   174 litpaweQEPDAPAIlARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMaspMAHQTGF 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4738 ACIAEIITTLlccGCICVPSDSDRRNNLAKAINAMDVNWALL-TPSVARM-----LDPCVVQSLKILVLGGEQVNSADWD 4811
Cdd:PRK13295   254 MYGLMMPVML---GATAVLQDIWDPARAAELIRTEGVTFTMAsTPFLTDLtravkESGRPVSSLRTFLCAGAPIPGALVE 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4812 RWPKSIQT--INAYGPTECSICCTTYSGKQGFKSGTigTSIVSVSW----VVDPENHNrlAPLGSIGELLVEGPILARGY 4885
Cdd:PRK13295   331 RARAALGAkiVSAWGMTENGAVTLTKLDDPDERAST--TDGCPLPGvevrVVDADGAP--LPAGQIGRLQVRGCSNFGGY 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4886 LN--DMEKTEAafiddpawllEGYgghsgrqgrlYKTGDLVRYDADGNLVYLGR-KDsqVKLRG-QRVELGEVEHHVREC 4961
Cdd:PRK13295   407 LKrpQLNGTDA----------DGW----------FDTGDLARIDADGYIRISGRsKD--VIIRGgENIPVVEIEALLYRH 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4962 LtEAKQLAVeVIVPE---GEGGYAMlaafvqlgddtyntlVKEKAG-GDSLTVQVVFLDrvEEELAKR-VPEHMMLttff 5036
Cdd:PRK13295   465 P-AIAQVAI-VAYPDerlGERACAF---------------VVPRPGqSLDFEEMVEFLK--AQKVAKQyIPERLVV---- 521
                          570       580
                   ....*....|....*....|.
gi 1820002560 5037 tLEAMPTTTSGKIDRKRLREI 5057
Cdd:PRK13295   522 -RDALPRTPSGKIQKFRLREM 541
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
5625-6129 1.24e-16

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 88.02  E-value: 1.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5625 HDLFTEQAKARPHAPAICaWDGE-------LTYGELDALSSKLAGHLTQLGVKPED----MVPLCFEksmwTVVAMLAVL 5693
Cdd:cd17634     56 ANALDRHLRENGDRTAII-YEGDdtsqsrtISYRELHREVCRFAGTLLDLGVKKGDrvaiYMPMIPE----AAVAMLACA 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5694 KAGGAFVPL----DPDHPASRHEDTfrhtGAQVVVTSAQHSARWIGTNHQVVTVSAGSLGQLS---TLV-----NPVG-- 5759
Cdd:cd17634    131 RIGAVHSVIfggfAPEAVAGRIIDS----SSRLLITADGGVRAGRSVPLKKNVDDALNPNVTSvehVIVlkrtgSDIDwq 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5760 --------------------LPAIPENAVYIMFTSGSTGIPKGVVLEHRA-VVTSCWGRGRAFGITNLSRVLQFA----- 5813
Cdd:cd17634    207 egrdlwwrdliakaspehqpEAMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTAdvgwv 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5814 ---SYTFDACMDEIITTLMYGGCICVPsDSDRrndLVKAISTMDVSCALLTPSVARLLEPS--------SVPTLQMLVLQ 5882
Cdd:cd17634    287 tghSYLLYGPLACGATTLLYEGVPNWP-TPAR---MWQVVDKHGVNILYTAPTAIRALMAAgddaiegtDRSSLRILGSV 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5883 GEQVSFADWnRWPASV------QTINGYGPTECS-ICCNTYSGKQGFKSG-----IIGTSVAsvswVVDPENHDrlAPLG 5950
Cdd:cd17634    363 GEPINPEAY-EWYWKKigkekcPVVDTWWQTETGgFMITPLPGAIELKAGsatrpVFGVQPA----VVDNEGHP--QPGG 435
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5951 SIGELLVEGPILArgylndiqKTAAVFIDDPAWLLEGYPGHPGrqgrLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRV 6030
Cdd:cd17634    436 TEGNLVITDPWPG--------QTRTLFGDHERFEQTYFSTFKG----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRL 503
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6031 ELGEVEhHVRECLPEARQLAVeVILPSGQKDHAmLAAFVQLEEGTqnalldkeasgEDSmaqvvflASVEEELAKRLPEH 6110
Cdd:cd17634    504 GTAEIE-SVLVAHPKVAEAAV-VGIPHAIKGQA-PYAYVVLNHGV-----------EPS-------PELYAELRNWVRKE 562
                          570       580
                   ....*....|....*....|...
gi 1820002560 6111 MVPTVFFSLLHF----PTTTSGK 6129
Cdd:cd17634    563 IGPLATPDVVHWvdslPKTRSGK 585
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
3024-3336 1.27e-16

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 86.66  E-value: 1.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3024 PCTPMQEGILTSQGKDPD--AYWVCFIYEVIPnqetSISLARLQQAWKGVVHQHSLLRTLLVDNVPGsTGTTNVVLKDPQ 3101
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGgpAYNIPGAWRLTG----PLDVEALREALRDVVARHEALRTLLVRDDGG-VPRQEILPPGPA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3102 P----SISVFSSEGTATIELFRSRYNPAAQRSIGQLQHHLSICQLNNGKVYLCLDINHAIIDAHSRGILMHDLQEAYD-- 3175
Cdd:cd19539     78 PlevrDLSDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAar 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3176 -----ANLNPQSTSFRDFASYIKQQSQEEAGR----YWAEYLDGVEPCFFPslGDSGGANTIPRT-----VEVPSIDSSA 3241
Cdd:cd19539    158 rkgpaAPLPELRQQYKEYAAWQREALAAPRAAelldFWRRRLRGAEPTALP--TDRPRPAGFPYPgadlrFELDAELVAA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3242 VHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPihNVNSIFGPLISILPCRIHLHKQLTVLEALKTVQ 3321
Cdd:cd19539    236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLIARVR 313
                          330
                   ....*....|....*
gi 1820002560 3322 ENYASSLSFQTFPLA 3336
Cdd:cd19539    314 KALVDAQRHQELPFQ 328
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
6852-7041 1.36e-16

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 87.57  E-value: 1.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6852 LGSIGELLVEGPILARGYLNDADKTAAAFVNDpaWLVE-GH-------GKHP------GRRGRLYKTGDLVYYNKDGNLV 6917
Cdd:cd17647    312 IGEVGEIYVRAGGLAEGYRGLPELNKEKFVNN--WFVEpDHwnyldkdNNEPwrqfwlGPRDRLYRTGDLGRYLPNGDCE 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6918 YIGRKDGQVKVRGQRVELGEIENRL-RECMPRATQMAVEvispaGAAEQAKTMVVAFLQLNDEARDALLGGNVPNDDNLS 6996
Cdd:cd17647    390 CCGRADDQVKIRGFRIELGEIDTHIsQHPLVRENITLVR-----RDKDEEPTLVSYIVPRFDKPDDESFAQEDVPKEVST 464
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 6997 AQVV--------FPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd17647    465 DPIVkgligyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
5197-5490 1.46e-16

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 86.65  E-value: 1.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5197 YPCSPLQEGlMSLTAKRAGD---YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHsELGLLQVVVEEK----- 5268
Cdd:cd19533      2 LPLTSAQRG-VWFAEQLDPEgsiYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWIDPYTpvpir 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5269 -IQWTESKRLEE----YLREDKAVSMGLGDR-LARYALIKepYDGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGAVP 5342
Cdd:cd19533     80 hIDLSGDPDPEGaaqqWMQEDLRKPLPLDNDpLFRHALFT--LGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5343 ERQPSFNAFIQYLGQQDLEAA----------TLYWQTALADckaalfptLPPTVT------QPVADTTVEYQCPPPSQ-- 5404
Cdd:cd19533    158 GRPAPPAPFGSFLDLVEEEQAyrqserferdRAFWTEQFED--------LPEPVSlarrapGRSLAFLRRTAELPPELtr 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5405 ------SATDITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRnapiAGVEA--MVGPTIATVPLRVCLQKDQTVSTLLE 5476
Cdd:cd19533    230 tlleaaEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR----LGAAArqTPGMVANTLPLRLTVDPQQTFAELVA 305
                          330
                   ....*....|....
gi 1820002560 5477 CLQQQSTDMIAHEQ 5490
Cdd:cd19533    306 QVSRELRSLLRHQR 319
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
877-1368 1.48e-16

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 87.52  E-value: 1.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpgHPASRHEEIfkqigaQVVLTS 956
Cdd:cd05932      6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTLNPDTI------RYVLEH 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  957 SQHAMLFA------SSERHQVTVSKVS-TSQLPTVVNF---------------AKSPVDPGNTAYIIFTSGTTGIPKGVV 1014
Cdd:cd05932     77 SESKALFVgklddwKAMAPGVPEGLISiSLPPPSAANCqyqwddliaqhppleERPTRFPEQLATLIYTSGTTGQPKGVM 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1015 LQHRAVTTSCLGHGEAFGYTDHARVLqfaSYTFDACIAE---IITTLLYGGCICVPSESDRR--NNLAKAIST------- 1082
Cdd:cd05932    157 LTFGSFAWAAQAGIEHIGTEENDRML---SYLPLAHVTErvfVEGGSLYGGVLVAFAESLDTfvEDVQRARPTlffsvpr 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1083 ------MDVNCALLTPSVARLLEPSAVPSL-KRLVLQG---EQVSFA------------DWNRWPGsVQTINGYGPTE-C 1139
Cdd:cd05932    234 lwtkfqQGVQDKIPQQKLNLLLKIPVVNSLvKRKVLKGlglDQCRLAgcgsapvppallEWYRSLG-LNILEAYGMTEnF 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1140 SVCCNTYSGKQgfKSGIIGTSVAslswvvdaGNHNRLAPlgsIGELLVEGPILARGYLNDIDKTEAAFIDDpAWLlegye 1219
Cdd:cd05932    313 AYSHLNYPGRD--KIGTVGNAGP--------GVEVRISE---DGEILVRSPALMMGYYKDPEATAEAFTAD-GFL----- 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1220 ghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKV-RGQRVELGEIEHHVreclpeARQLAVEVILPSGQKEHALLAAF 1298
Cdd:cd05932    374 ----------RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKL------AEHDRVEMVCVIGSGLPAPLALV 437
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 1299 IQLDKGNHNALFEEKASGEDSMAQVvfLTGVEEELAKRlpEHMVPTIL----FTVKAMPITTSGKIDRKRLQDI 1368
Cdd:cd05932    438 VLSEEARLRADAFARAELEASLRAH--LARVNSTLDSH--EQLAGIVVvkdpWSIDNGILTPTLKIKRNVLEKA 507
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
7183-7475 1.50e-16

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 86.65  E-value: 1.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7183 YPCSPLQEGlISLTAKRAGD---YIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHsELGLLQVVVEEK----- 7254
Cdd:cd19533      2 LPLTSAQRG-VWFAEQLDPEgsiYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWIDPYTpvpir 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7255 -IQWTES----EALEEYLKEDKAVSMGL-GDPLAHYALVKeaWGGKRWFVW-TIHHALYDGGSLPLILHAVKQVYSGAVL 7327
Cdd:cd19533     80 hIDLSGDpdpeGAAQQWMQEDLRKPLPLdNDPLFRHALFT--LGDNRHFWYqRVHHIVMDGFSFALFGQRVAEIYTALLK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7328 ERQ------PSFNAFI----QYLGQQDLEATAAYWQTALSDC-EAVLF-PPLPSTVTQPVADTTVeyqCPPLSKATLDTT 7395
Cdd:cd19533    158 GRPappapfGSFLDLVeeeqAYRQSERFERDRAFWTEQFEDLpEPVSLaRRAPGRSLAFLRRTAE---LPPELTRTLLEA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7396 TS-------TLIRAAWAIVTSCYTSSDDVVYGTTVTGRnapiAGVEA--MVGPTIATVPVRLRVQRDQTVFAFLQGLQQQ 7466
Cdd:cd19533    235 AEahgaswpSFFIALVAAYLHRLTGANDVVLGVPVMGR----LGAAArqTPGMVANTLPLRLTVDPQQTFAELVAQVSRE 310

                   ....*....
gi 1820002560 7467 STDMIAHEQ 7475
Cdd:cd19533    311 LRSLLRHQR 319
PRK07514 PRK07514
malonyl-CoA synthase; Validated
5632-6020 1.52e-16

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 87.24  E-value: 1.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGE-LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 5710
Cdd:PRK07514    12 AFADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5711 HEDTFRHTGAQVVVTsAQHSARWI-------GTNHqVVTVSA---GSLGQLSTLVnPVGLPAIPENA---VYIMFTSGST 5777
Cdd:PRK07514    92 LDYFIGDAEPALVVC-DPANFAWLskiaaaaGAPH-VETLDAdgtGSLLEAAAAA-PDDFETVPRGAddlAAILYTSGTT 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5778 GIPKGVVLEHR------AVVTSCWGRGR------------------AFGITNLSRVLQFASYTFDAcmDEII-----TTL 5828
Cdd:PRK07514   169 GRSKGAMLSHGnllsnaLTLVDYWRFTPddvlihalpifhthglfvATNVALLAGASMIFLPKFDP--DAVLalmprATV 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5829 MYGgcicVPS------DSDRrndlvkaistmdvscalLTPSVA---RLLEPSSVPTLqmlvlqGEqvSFADWnrwpasvQ 5899
Cdd:PRK07514   247 MMG----VPTfytrllQEPR-----------------LTREAAahmRLFISGSAPLL------AE--THREF-------Q 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5900 TING------YGPTE-CSICCNTYSGKQgfKSGIIGTSVASVSW-VVDPENHDRLAPlGSIGELLVEGPILARGYLNDIQ 5971
Cdd:PRK07514   291 ERTGhailerYGMTEtNMNTSNPYDGER--RAGTVGFPLPGVSLrVTDPETGAELPP-GEIGMIEVKGPNVFKGYWRMPE 367
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5972 KTAAVFIDDpawlleGYpghpgrqgrlYKTGDLVRYDANGNLVCLGR-KD 6020
Cdd:PRK07514   368 KTAEEFRAD------GF----------FITGDLGKIDERGYVHIVGRgKD 401
PRK05857 PRK05857
fatty acid--CoA ligase;
7599-8035 1.54e-16

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 87.37  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7599 ADVPPAI-ERCVhdlfaEQARARPGAPAICAWDG--ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAML 7675
Cdd:PRK05857    10 PQLPSTVlDRVF-----EQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7676 AVLKAGGAFVPLDPDHPA---SRHEEIFEQTGAQV-----VVASAQYSARWTSSSCHVVTVSKALSSQLPAVVD--STNT 7745
Cdd:PRK05857    85 ACAKLGAIAVMADGNLPIaaiERFCQITDPAAALVapgskMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAAslAGNA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7746 SVRPENAAYIIFTSGSTGVPKGVVLEHR---AVATSClghgRAFGITNLSRVLQFASY-----TFDACIAEIITTLLCGG 7817
Cdd:PRK05857   165 DQGSEDPLAMIFTSGTTGEPKAVLLANRtffAVPDIL----QKEGLNWVTWVVGETTYsplpaTHIGGLWWILTCLMHGG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7818 -CIcvpSDSDRRNSLAKAISTMDVNWAFLTPSVARLLDPGL------IPSLKILAIGGEQSSSADWnRW--PGSVQKIHV 7888
Cdd:PRK05857   241 lCV---TGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELksanatVPSLRLVGYGGSRAIAADV-RFieATGVRTAQV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7889 YGPTE--CCIFC--TGYTTKQGFEPSTIGTSVASVSWVVDPENHN-----RLAPLGSMGELLMEGPILARGYLNDVDKTE 7959
Cdd:PRK05857   317 YGLSEtgCTALClpTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIgptapGAGPSASFGTLWIKSPANMLGYWNNPERTA 396
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 7960 AAFIDdpAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLA 8035
Cdd:PRK05857   397 EVLID--GWV---------------NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGVSGVREAA 454
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
851-1368 1.55e-16

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 87.42  E-value: 1.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  851 DRCIHDLFAEQARARPDASAVCAWDGE------LTYGELDELSSKLAAHLVQLGVKREDVVPlCFEKSMWTVVAM-LAVL 923
Cdd:PRK13295    23 DRTINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVS-CQLPNWWEFTVLyLACS 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  924 KAGGAFVPLDP-----------GHPASR------------HEEIFKQIGA------QVVLTSSQHAMLFassERHQVTVS 974
Cdd:PRK13295   102 RIGAVLNPLMPifrerelsfmlKHAESKvlvvpktfrgfdHAAMARRLRPelpalrHVVVVGGDGADSF---EALLITPA 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  975 KVSTSQLPTVvnFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYT-DHarVLQFASytfdaCIAE 1053
Cdd:PRK13295   179 WEQEPDAPAI--LARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGaDD--VILMAS-----PMAH 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1054 iITTLLYG-------GCICVPSESDRRNNLAKAISTMDVNCALL-TPSVARLLE-----PSAVPSLKRLVLQGEQVsfad 1120
Cdd:PRK13295   250 -QTGFMYGlmmpvmlGATAVLQDIWDPARAAELIRTEGVTFTMAsTPFLTDLTRavkesGRPVSSLRTFLCAGAPI---- 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1121 wnrwPGSV----------QTINGYGPTECSVCCNTYSGKQGFKSgiIGTSVASLSW----VVDAGNHNrlAPLGSIGELL 1186
Cdd:PRK13295   325 ----PGALveraraalgaKIVSAWGMTENGAVTLTKLDDPDERA--STTDGCPLPGvevrVVDADGAP--LPAGQIGRLQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1187 VEGPILARGYLNdidkteaafidDPAWLLEGYEGhagrrgrLYKTGDLVRCDADGNLVCLGR-KDsqVKVRG-QRVELGE 1264
Cdd:PRK13295   397 VRGCSNFGGYLK-----------RPQLNGTDADG-------WFDTGDLARIDADGYIRISGRsKD--VIIRGgENIPVVE 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1265 IE----HHvreclPEARQLAVeVILPSGQ-KEHAllAAFIQLDKGnhnalfeekaSGEDSMAQVVFLTgvEEELAKR-LP 1338
Cdd:PRK13295   457 IEallyRH-----PAIAQVAI-VAYPDERlGERA--CAFVVPRPG----------QSLDFEEMVEFLK--AQKVAKQyIP 516
                          570       580       590
                   ....*....|....*....|....*....|
gi 1820002560 1339 EHMVptilfTVKAMPITTSGKIDRKRLQDI 1368
Cdd:PRK13295   517 ERLV-----VRDALPRTPSGKIQKFRLREM 541
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
5618-6140 1.56e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 87.52  E-value: 1.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5618 PAIERCVHDLFTEQAKARPHAPAICAWDGEL--TYGELDALSSKLAGHLTQLGVKPEDMV----PLCFEksmWTVVAMlA 5691
Cdd:PRK12583    14 PLLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVgiwaPNCAE---WLLTQF-A 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5692 VLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTS-AQHSARWIGT---------NHQVVTVSAGSLGQLSTLV-----N 5756
Cdd:PRK12583    90 TARIGAILVNINPAYRASELEYALGQSGVRWVICAdAFKTSDYHAMlqellpglaEGQPGALACERLPELRGVVslapaP 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5757 PVGLPAIPE-----------------------NAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLqfA 5813
Cdd:PRK12583   170 PPGFLAWHElqargetvsrealaerqasldrdDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLC--V 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5814 SYTFDACMDEIITTLM---YGGCICVPSDSDRRNDLVKAIStmDVSCALL----TPSVARLLEPS----SVPTLQMLVLQ 5882
Cdd:PRK12583   248 PVPLYHCFGMVLANLGcmtVGACLVYPNEAFDPLATLQAVE--EERCTALygvpTMFIAELDHPQrgnfDLSSLRTGIMA 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5883 GEQVSFADWNRWPASVQ----TInGYGPTECSICCNtysgkQGFKSGIIGTSVASV--------SWVVDPENHdrLAPLG 5950
Cdd:PRK12583   326 GAPCPIEVMRRVMDEMHmaevQI-AYGMTETSPVSL-----QTTAADDLERRVETVgrtqphleVKVVDPDGA--TVPRG 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5951 SIGELLVEGPILARGYLNDIQKTAAVfIDDPAWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRV 6030
Cdd:PRK12583   398 EIGELCTRGYSVMKGYWNNPEATAES-IDEDGWM---------------HTGDLATMDEQGYVRIVGRSKDMIIRGGENI 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6031 ELGEVEHHVrecLPEARQLAVEVILPSGQKDHAMLAAFVQLEEGTQNAlldkeasgedsmaqvvflasvEEELAK----R 6106
Cdd:PRK12583   462 YPREIEEFL---FTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAAS---------------------EEELREfckaR 517
                          570       580       590
                   ....*....|....*....|....*....|....
gi 1820002560 6107 LPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGA 6140
Cdd:PRK12583   518 IAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISI 551
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
1166-1461 1.63e-16

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 84.42  E-value: 1.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1166 WVVDAGNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPAwllegyeGHAGRRGRLYKTGDLVRCDADGNLVC 1245
Cdd:COG3433     23 AIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPF-------IPVPYPAQPGRQADDLRLLLRRGLGP 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1246 LGRKDSQVKVRGQRVELGEIEHHVREC--LPEARQLAVEVILPSGQKEHALLAAfiqldkgnhnalfeekASGEDSMAqv 1323
Cdd:COG3433     96 GGGLERLVQQVVIRAERGEEEELLLVLraAAVVRVAVLAALRGAGVGLLLIVGA----------------VAALDGLA-- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1324 vfltgVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDIgasfTVQQLAEMRTSSQGPKRQPSTEVEQTMQQLW 1403
Cdd:COG3433    158 -----AAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAP----ALAAAEALLAAASPAPALETALTEEELRADV 228
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 1404 AQVLSIEPNSIGLDDSFFRLGGDSIVAMKLVGEARRTGLQLSVADIFRHPRLVDLARV 1461
Cdd:COG3433    229 AELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWAL 286
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5-284 1.72e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 86.73  E-value: 1.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    5 WALLTpsvaRL-LEPSHIPSLRILVMGGEQVNSADWDRWPSSV---QTINGYGPTECCIVCTGYTSEQDFTT-GTIGTSI 79
Cdd:cd05922    217 YAMLT----RLgFDPAKLPSLRYLTQAGGRLPQETIARLRELLpgaQVYVMYGQTEATRRMTYLPPERILEKpGSIGLAI 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   80 ASVSWVVDPKDHGRLAPlGSVGELLVEGPILARGYLSDPEKTAAvfinnpawllEGHGGyagrqGRLYkTGDLVRYDADG 159
Cdd:cd05922    293 PGGEFEILDDDGTPTPP-GEPGEIVHRGPNVMKGYWNDPPYRRK----------EGRGG-----GVLH-TGDLARRDEDG 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  160 NLVCLGRKDSQVKLRGQRVELGEVEHHVRECLPEAKQLAVEVVLPLGQKnhatLAAFIQLDKGThnallkekvggDDSIA 239
Cdd:cd05922    356 FLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEK----LALFVTAPDKI-----------DPKDV 420
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560  240 RVVflagveeeLAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLR 284
Cdd:cd05922    421 LRS--------LAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
7633-8121 1.83e-16

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 86.24  E-value: 1.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP----LDPDHPASRheeiFEQTGAQVV 7708
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPlttlLGPKDIEYR----LEAAGAKAI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7709 VASAqysarwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVLEHRAVatscLGHGR-AFG 7787
Cdd:cd05972     77 VTDA-------------------------------------EDPALIYFTSGTTGLPKGVLHTHSYP----LGHIPtAAY 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7788 ITNLSRV-----------LQFASYTFDACIAEIITTLLCGGCICVPsdsdrRNSLaKAISTMDVNWAFLTPSVARLL--- 7853
Cdd:cd05972    116 WLGLRPDdihwniadpgwAKGAWSSFFGPWLLGATVFVYEGPRFDA-----ERIL-ELLERYGVTSFCGPPTAYRMLikq 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7854 --DPGLIPSLKILAIGGEQSSSADWNRWPGSVQ-KIH-VYGPTECCIFCTGYTTkQGFEPSTIGTSVASVSWVVDPENHN 7929
Cdd:cd05972    190 dlSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGlPIRdGYGQTETGLTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGR 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7930 RLAPlGSMGEL-LMEGPI-LARGYLNDVDKTEAAFIDDpaWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQ 8007
Cdd:cd05972    269 ELPP-GEEGDIaIKLPPPgLFLGYVGDPEKTEASIRGD--Y---------------YLTGDRAYRDEDGYFWFVGRADDI 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8008 VKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKNHAMLAvFVQLGKGthiahleekAGGEDSMAqvvfltgteEE 8087
Cdd:cd05972    331 IKSSGYRIGPFEVESALLE-HPAVAEAAV-VGSPDPVRGEVVKA-FVVLTSG---------YEPSEELA---------EE 389
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 8088 LA----KRLPKHMVPTVFFALLHFPMTTSGKADRKRLR 8121
Cdd:cd05972    390 LQghvkKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
PRK05857 PRK05857
fatty acid--CoA ligase;
4534-5054 1.95e-16

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 87.37  E-value: 1.95e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4534 DVPPAI-ERCVhdqfaEQARARPDTPAICAWDG--ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLA 4610
Cdd:PRK05857    11 QLPSTVlDRVF-----EQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4611 VLKAGGAFVPLDPDHPA---SRHEHIFRQTGAQV-----VLASAQYATLWTSLGRSVVIVSEASTSQLPVvtKTADPSVN 4682
Cdd:PRK05857    86 CAKLGAIAVMADGNLPIaaiERFCQITDPAAALVapgskMASSAVPEALHSIPVIAVDIAAVTRESEHSL--DAASLAGN 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4683 PGNAA----YAIFTSGSTGIPKGVVLEHKAVvtsclghgqaFGITDHTRV--LQFASY-----TFDACIAEIITTL---L 4748
Cdd:PRK05857   164 ADQGSedplAMIFTSGTTGEPKAVLLANRTF----------FAVPDILQKegLNWVTWvvgetTYSPLPATHIGGLwwiL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4749 CC---GCICVpSDSDRRNNLAKAINAMDVNWALLTPSVARML------DPCVVQSLKILVLGGEQVNSADWdRWPKS--I 4817
Cdd:PRK05857   234 TClmhGGLCV-TGGENTTSLLEILTTNAVATTCLVPTLLSKLvselksANATVPSLRLVGYGGSRAIAADV-RFIEAtgV 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4818 QTINAYGPTE--CS-ICCTTYSGK-QGFKSGTIGTSIVSVSWVVDPENHN-----RLAPLGSIGELLVEGPILARGYLND 4888
Cdd:PRK05857   312 RTAQVYGLSEtgCTaLCLPTDDGSiVKIEAGAVGRPYPGVDVYLAATDGIgptapGAGPSASFGTLWIKSPANMLGYWNN 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4889 MEKTEAAFIDdpAWLlegygghsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhHVRECLTEAKQL 4968
Cdd:PRK05857   392 PERTAEVLID--GWV---------------NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGVSGVREA 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4969 AVEVIvPEGEGGYAMLAAFVQLGDdtyntlvKEKAGGDSLTVQVVFLDRVEEELAKRvPehmmlTTFFTLEAMPTTTSGK 5048
Cdd:PRK05857   454 ACYEI-PDEEFGALVGLAVVASAE-------LDESAARALKHTIAARFRRESEPMAR-P-----STIVIVTDIPRTQSGK 519

                   ....*.
gi 1820002560 5049 IDRKRL 5054
Cdd:PRK05857   520 VMRASL 525
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
4558-5055 2.37e-16

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 85.99  E-value: 2.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4558 PAICAWDGELTYGELDTLSSKLASHLV-QLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQ 4636
Cdd:cd05958      2 TCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4637 TGaqvvlasaqyatlwtslgRSVVIVSEASTsqlpvvtkTADpsvnpgNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGH 4716
Cdd:cd05958     82 AR------------------ITVALCAHALT--------ASD------DICILAFTSGTTGAPKATMHFHRDPLASADRY 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4717 G-QAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLAKAINAMDVNWALLTPSVAR-MLDPC---- 4790
Cdd:cd05958    130 AvNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRaMLAHPdaag 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4791 -VVQSLKILVLGGEQVNSADWDRWPKS--IQTINAYGPTEC-SICCTTYSGKqgFKSGTIGTSIVSVSW-VVDPENhnRL 4865
Cdd:cd05958    210 pDLSSLRKCVSAGEALPAALHRAWKEAtgIPIIDGIGSTEMfHIFISARPGD--ARPGATGKPVPGYEAkVVDDEG--NP 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4866 APLGSIGELLVEGPIlarGYLNDMEKTEAAFIDDpAWLLegygghsgrqgrlykTGDLVRYDADGNLVYLGRKDSQVKLR 4945
Cdd:cd05958    286 VPDGTIGRLAVRGPT---GCRYLADKRQRTYVQG-GWNI---------------TGDTYSRDPDGYFRHQGRSDDMIVSG 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4946 GQRVELGEVE----HH--VREClteakqlAVeVIVPEGEGGyAMLAAFVqlgddtynTLVKEKAGGDSLTVQVVflDRVE 5019
Cdd:cd05958    347 GYNIAPPEVEdvllQHpaVAEC-------AV-VGHPDESRG-VVVKAFV--------VLRPGVIPGPVLARELQ--DHAK 407
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1820002560 5020 EELAK-RVPEHMMLTTfftleAMPTTTSGKIDRKRLR 5055
Cdd:cd05958    408 AHIAPyKYPRAIEFVT-----ELPRTATGKLQRFALR 439
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
5660-6136 2.55e-16

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 86.78  E-value: 2.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5660 LAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVT--SAQH-------- 5729
Cdd:PLN02860    45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTdeTCSSwyeelqnd 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5730 ---SARW---IGTNHQVVTVSAGSLGQLSTLVNPVGLPAI------PENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGR 5797
Cdd:PLN02860   125 rlpSLMWqvfLESPSSSVFIFLNSFLTTEMLKQRALGTTEldyawaPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAK 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5798 GRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGC-ICVPS-DSdrrNDLVKAISTMDVSCALLTPSV-ARLLEPS--- 5871
Cdd:PLN02860   205 IAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAChVLLPKfDA---KAALQAIKQHNVTSMITVPAMmADLISLTrks 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5872 ----SVPTLQMLVLQGEQVS---FADWNRWPASVQTINGYGPTE-CS--------------------ICCNTYSGKQGFK 5923
Cdd:PLN02860   282 mtwkVFPSVRKILNGGGSLSsrlLPDAKKLFPNAKLFSAYGMTEaCSsltfmtlhdptlespkqtlqTVNQTKSSSVHQP 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5924 SGI-IGTSVASVSWVVDPENHDRlaplgsIGELLVEGPILARGYLNDIQKTAAVFIDDpAWLlegypghpgrqgrlyKTG 6002
Cdd:PLN02860   362 QGVcVGKPAPHVELKIGLDESSR------VGRILTRGPHVMLGYWGQNSETASVLSND-GWL---------------DTG 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6003 DLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVE----HH------VRECLPEARQLavevilpsgqkdhAMLAAFVQLE 6072
Cdd:PLN02860   420 DIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEavlsQHpgvasvVVVGVPDSRLT-------------EMVVACVRLR 486
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6073 EGTQNALLDKEASGEDsmaqvvFLASvEEEL-----AKRLPEHMVPTVFFSLLH-FPTTTSGKTDRKRLR 6136
Cdd:PLN02860   487 DGWIWSDNEKENAKKN------LTLS-SETLrhhcrEKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVR 549
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
5217-5520 2.68e-16

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 85.87  E-value: 2.68e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5217 YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSElGLLQVVVEE---KIQWTESKRLEEYLREDKAvsmglgD 5293
Cdd:cd19531     24 YNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDG-EPVQVILPPlplPLPVVDLSGLPEAEREAEA------Q 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5294 RLARyALIKEPYD--------------GGKRW-FVWTIHHALYDGWSLPRILQAVKQIYSGAVPERQPSFNAF-IQY--- 5354
Cdd:cd19531     97 RLAR-EEARRPFDlargpllratllrlGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPPLpIQYady 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5355 -------LGQQDLEAATLYWQTALADCKAAL-FPT------------------LPPTVTQPVADTtveyqcpppSQsATD 5408
Cdd:cd19531    176 avwqrewLQGEVLERQLAYWREQLAGAPPVLeLPTdrprpavqsfrgarvrftLPAELTAALRAL---------AR-REG 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5409 ITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAH 5488
Cdd:cd19531    246 ATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRA--ELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAYAH 323
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 5489 ---------EQTGLQRIAKMSPgarhacGFQTLLVVQPTDD 5520
Cdd:cd19531    324 qdlpfeklvEALQPERDLSRSP------LFQVMFVLQNAPA 358
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
6851-7044 2.79e-16

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 86.70  E-value: 2.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPI--LARGYLNDADKTAAAFvndpawlvegHGKHPGrrgrLYKTGDLVYYNKDGNLVYIGRKDGQVKV 6928
Cdd:COG0365    381 PPGEEGELVIKGPWpgMFRGYWNDPERYRETY----------FGRFPG----WYRTGDGARRDEDGYFWILGRSDDVINV 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6929 RGQRVELGEIENRL------RECmpratqmAVevispAGAAEQAK-TMVVAFLQLNDEARDallggnvpnDDNLSAQVVf 7001
Cdd:COG0365    447 SGHRIGTAEIESALvshpavAEA-------AV-----VGVPDEIRgQVVKAFVVLKPGVEP---------SDELAKELQ- 504
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 7002 pAKVDEKLSnllpSYMMPEVYFAVPQLPMMISGKTDRKRLREI 7044
Cdd:COG0365    505 -AHVREELG----PYAYPREIEFVDELPKTRSGKIMRRLLRKI 542
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
6842-7135 2.89e-16

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 83.65  E-value: 2.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPAwlveGHGKHPGRRGRLYKTGDLVYYNKDGNLvyiGR 6921
Cdd:COG3433     26 QARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPF----IPVPYPAQPGRQADDLRLLLRRGLGPG---GG 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 KDGQVKVRGQRVELGEIENRLRECMPRATQMAVEVISPAGaaeqaktmvvaflqlnDEARDALLGGNVPNDDNLSAQVVf 7001
Cdd:COG3433     99 LERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRG----------------AGVGLLLIVGAVAALDGLAAAAA- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7002 pakvdekLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREIGASFTAQQLAEmrTSSQGPKRQPSTEAErtMQQLWAR 7081
Cdd:COG3433    162 -------LAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAA--ASPAPALETALTEEE--LRADVAE 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 7082 MLKVKADSIGLDDSFFRLGGDSIVAMKLVGEARRTGLQLSVADVFRHPRLVDLA 7135
Cdd:COG3433    231 LLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWW 284
PLN02574 PLN02574
4-coumarate--CoA ligase-like
864-1368 2.92e-16

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 86.82  E-value: 2.92e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  864 ARPDASAVC-AWDGE-LTYGELDELSSKLAAHLVQ-LGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASr 940
Cdd:PLN02574    51 NHNGDTALIdSSTGFsISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLG- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  941 heeifkQIGAQVVLTSSqhAMLFASSErhqvTVSKVSTSQLPTV-----VNF---------------------AKSPVDP 994
Cdd:PLN02574   130 ------EIKKRVVDCSV--GLAFTSPE----NVEKLSPLGVPVIgvpenYDFdskriefpkfyelikedfdfvPKPVIKQ 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  995 GNTAYIIFTSGTTGIPKGVVLQHRAVTTSClghgEAFgytdharvLQF--ASYTFDAC---------------IAEIITT 1057
Cdd:PLN02574   198 DDVAAIMYSSGTTGASKGVVLTHRNLIAMV----ELF--------VRFeaSQYEYPGSdnvylaalpmfhiygLSLFVVG 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1058 LL-YGGCICVPSESDrRNNLAKAISTMDVNCALLTPSVARLLEPSAVP----SLKRLVLQG------EQVSFADWNRWPG 1126
Cdd:PLN02574   266 LLsLGSTIVVMRRFD-ASDMVKVIDRFKVTHFPVVPPILMALTKKAKGvcgeVLKSLKQVScgaaplSGKFIQDFVQTLP 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1127 SVQTINGYGPTEcsvccNTYSGKQGFKSGIIG--TSVASL-----SWVVDAGNHNRLAPlGSIGELLVEGPILARGYLND 1199
Cdd:PLN02574   345 HVDFIQGYGMTE-----STAVGTRGFNTEKLSkySSVGLLapnmqAKVVDWSTGCLLPP-GNCGELWIQGPGVMKGYLNN 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1200 iDKTEAAFIDDPAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQL 1279
Cdd:PLN02574   419 -PKATQSTIDKDGWL---------------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLIS-HPEIIDA 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1280 AVeviLPSGQKEhallaafiqldKGNHNALFEEKASGEdSMAQVVFLTGVEEELAkrlPEHMVPTILFTvKAMPITTSGK 1359
Cdd:PLN02574   482 AV---TAVPDKE-----------CGEIPVAFVVRRQGS-TLSQEAVINYVAKQVA---PYKKVRKVVFV-QSIPKSPAGK 542

                   ....*....
gi 1820002560 1360 IDRKRLQDI 1368
Cdd:PLN02574   543 ILRRELKRS 551
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
877-1367 2.99e-16

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 85.48  E-value: 2.99e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpghpasRHeeifkqigaqvvLTS 956
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN------TR------------LTP 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  957 sqHAMLFasserhQVTVSKVSTSQlptvvnfakspvdpgnTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDH 1036
Cdd:cd05912     63 --NELAF------QLKDSDVKLDD----------------IATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1037 ARVLQFASYTFDACIAEIITTLLYGGCICVP---SESDRRNNL-AKAISTMDVNCALLTpsvaRLLE--PSAVPSLKRLV 1110
Cdd:cd05912    119 DNWLCALPLFHISGLSILMRSVIYGMTVYLVdkfDAEQVLHLInSGKVTIISVVPTMLQ----RLLEilGEGYPNNLRCI 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1111 LQG---------EQVSFADwnrwpgsVQTINGYGPTE-CSVCCnTYSGKQGF-KSGIIGTSVASlswvVDAGNHNRLAPL 1179
Cdd:cd05912    195 LLGggpapkpllEQCKEKG-------IPVYQSYGMTEtCSQIV-TLSPEDALnKIGSAGKPLFP----VELKIEDDGQPP 262
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1180 GSIGELLVEGPILARGYLNDIDKTEAAFIDDpaWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQR 1259
Cdd:cd05912    263 YEVGEILLKGPNVTKGYLNRPDATEESFENG--WF---------------KTGDIGYLDEEGFLYVLDRRSDLIISGGEN 325
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1260 VELGEIEHHVREcLPEARQLAVeVILPS---GQKEHallaAFIqldkgnhnalfeeKASGEDSMAQvvfltgVEEELAKR 1336
Cdd:cd05912    326 IYPAEIEEVLLS-HPAIKEAGV-VGIPDdkwGQVPV----AFV-------------VSERPISEEE------LIAYCSEK 380
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1820002560 1337 LPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:cd05912    381 LAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
PRK07798 PRK07798
acyl-CoA synthetase; Validated
7611-8021 3.13e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 86.48  E-value: 3.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 7690
Cdd:PRK07798     7 DLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7691 HPASRHEEIFEQTGAQVVVASAQYSARW------TSSSCHVVTVSKALSSQLP--------AVVDSTNTSVRPENAA--- 7753
Cdd:PRK07798    87 YVEDELRYLLDDSDAVALVYEREFAPRVaevlprLPKLRTLVVVEDGSGNDLLpgavdyedALAAGSPERDFGERSPddl 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7754 YIIFTSGSTGVPKGVVLEHRAVATSCLGhGRAFG----ITNLSRVLQFA-----SYTFDAC-------IAEIITTLLCGG 7817
Cdd:PRK07798   167 YLLYTGGTTGMPKGVMWRQEDIFRVLLG-GRDFAtgepIEDEEELAKRAaagpgMRRFPAPplmhgagQWAAFAALFSGQ 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7818 CICVPSDS--DRRNSLA-----KAISTMDVNWAFLTPSVARLLDPG--LIPSLKILAIGGEQSSSADWNRWPGSVQKIHV 7888
Cdd:PRK07798   246 TVVLLPDVrfDADEVWRtiereKVNVITIVGDAMARPLLDALEARGpyDLSSLFAIASGGALFSPSVKEALLELLPNVVL 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7889 ---YGPTEccifcTGY----TTKQGFEPSTIGTSVASVSWVVDPENHNRLAPlGS--MGELLMEGPIlARGYLNDVDKTE 7959
Cdd:PRK07798   326 tdsIGSSE-----TGFggsgTVAKGAVHTGGPRFTIGPRTVVLDEDGNPVEP-GSgeIGWIARRGHI-PLGYYKDPEKTA 398
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 7960 AAFiddpawllegypghPGRQGRLYK-TGDLVQYNADGNLVYLGRkDSQ-VKVRGQRVELGEVE 8021
Cdd:PRK07798   399 ETF--------------PTIDGVRYAiPGDRARVEADGTITLLGR-GSVcINTGGEKVFPEEVE 447
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
3457-3979 3.34e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 86.37  E-value: 3.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3457 PAIERCVHDLFTEQAKARPHAPAICAWDGEL--TYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmWTVVAMlA 3530
Cdd:PRK12583    14 PLLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVgiwaPNCAE---WLLTQF-A 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3531 VLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQY-----------------SARWTSSSC-------HVVTVSKAL 3586
Cdd:PRK12583    90 TARIGAILVNINPAYRASELEYALGQSGVRWVICADAFktsdyhamlqellpglaEGQPGALACerlpelrGVVSLAPAP 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3587 SSQL--------------PAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLqfA 3652
Cdd:PRK12583   170 PPGFlawhelqargetvsREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLC--V 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3653 SYTFDACIAEIITTLLC---GGCICVPSDSDRRNSLAKAISTMDVNWAFLTPS--VARLLDPGL----IPSLKILAIGGE 3723
Cdd:PRK12583   248 PVPLYHCFGMVLANLGCmtvGACLVYPNEAFDPLATLQAVEEERCTALYGVPTmfIAELDHPQRgnfdLSSLRTGIMAGA 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3724 QSSSADWNRWPGSVQKIHV---YGPTECC--IFCTGYTTKQGFEPSTIGTSVASV-SWVVDPENHNrlAPLGSMGELLME 3797
Cdd:PRK12583   328 PCPIEVMRRVMDEMHMAEVqiaYGMTETSpvSLQTTAADDLERRVETVGRTQPHLeVKVVDPDGAT--VPRGEIGELCTR 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3798 GPILARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHH 3877
Cdd:PRK12583   406 GYSVMKGYWNNPEATAES-IDEDGWM---------------HTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEF 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3878 VrecLPEARQLAVEVILPSGQKDHAMLAAFVQLEEGTQNAlldkeaggedsmaqvvflasvEEELAK----RLPEHMVPT 3953
Cdd:PRK12583   470 L---FTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAAS---------------------EEELREfckaRIAHFKVPR 525
                          570       580
                   ....*....|....*....|....*.
gi 1820002560 3954 VFFSLLHFPTTTSGKTDRKRLREIGA 3979
Cdd:PRK12583   526 YFRFVDEFPMTVTGKVQKFRMREISI 551
PRK07788 PRK07788
acyl-CoA synthetase; Validated
5632-6138 3.36e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 86.52  E-value: 3.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 5711
Cdd:PRK07788    59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5712 EDTFRHTGAQVVVTSAQHSAR-------------WIG--TNHQVVTVSAGSLGQLSTLVNPVGLPAIPENAVYIMFTSGS 5776
Cdd:PRK07788   139 AEVAAREGVKALVYDDEFTDLlsalppdlgrlraWGGnpDDDEPSGSTDETLDDLIAGSSTAPLPKPPKPGGIVILTSGT 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5777 TGIPKGVVLEH-------RAVVT----------------------SCWGRGRAFGITN-LSRVlqfasytFDA--CMDEI 5824
Cdd:PRK07788   219 TGTPKGAPRPEpsplaplAGLLSrvpfragettllpapmfhatgwAHLTLAMALGSTVvLRRR-------FDPeaTLEDI 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5825 ----ITTLmyggcICVPSDSDRRNDLV-KAISTMDVScalltpsvarllepssvpTLQMLVLQGEQVSFADWNRWPASVQ 5899
Cdd:PRK07788   292 akhkATAL-----VVVPVMLSRILDLGpEVLAKYDTS------------------SLKIIFVSGSALSPELATRALEAFG 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5900 TI--NGYGPTECSICcnTYSGKQGFK--SGIIGTSVASVSWVVDPENHDRLaPLGSIGELLVEGPILARGYLNdiqktaa 5975
Cdd:PRK07788   349 PVlyNLYGSTEVAFA--TIATPEDLAeaPGTVGRPPKGVTVKILDENGNEV-PRGVVGRIFVGNGFPFEGYTD------- 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5976 vfiddpawllegyPGHPGRQGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhHVRECLPEARQLAVevil 6055
Cdd:PRK07788   419 -------------GRDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVE-DLLAGHPDVVEAAV---- 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6056 pSGQKDHAM---LAAFVQLEEGTQnalLDKEAsgedsmaqvvflasVEEELAKRLPEHMVP--TVFFSLLhfPTTTSGKT 6130
Cdd:PRK07788   481 -IGVDDEEFgqrLRAFVVKAPGAA---LDEDA--------------IKDYVRDNLARYKVPrdVVFLDEL--PRNPTGKV 540

                   ....*...
gi 1820002560 6131 DRKRLREI 6138
Cdd:PRK07788   541 LKRELREM 548
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
7614-8036 3.39e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 86.37  E-value: 3.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7614 AEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPA 7693
Cdd:PRK07786    24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7694 SRHEEIFEQTGAQVVVASAQYS-----ARWTSSSCHVVTVSKALS--------------SQLPAVVDSTNTSvrpenAAY 7754
Cdd:PRK07786   104 PEIAFLVSDCGAHVVVTEAALApvataVRDIVPLLSTVVVAGGSSddsvlgyedllaeaGPAHAPVDIPNDS-----PAL 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7755 IIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFD-ACIAEIITTLLCGGCICV-PSDSDRRNSLA 7832
Cdd:PRK07786   179 IMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHiAGIGSMLPGLLLGAPTVIyPLGAFDPGQLL 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7833 KAISTMDVNWAFLTPS--VARLLDPGLIP---SLKILAIGGEQSSSADWNR----WPGSvQKIHVYGPTE-----CCIFC 7898
Cdd:PRK07786   259 DVLEAEKVTGIFLVPAqwQAVCAEQQARPrdlALRVLSWGAAPASDTLLRQmaatFPEA-QILAAFGQTEmspvtCMLLG 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7899 TGYTTKQGfepsTIGTSVASVSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFiddpawllegypghpg 7978
Cdd:PRK07786   338 EDAIRKLG----SVGKVIPTVAARVVDENMNDVPV-GEVGEIVYRAPTLMSGYWNNPEATAEAF---------------- 396
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 7979 rQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAV 8036
Cdd:PRK07786   397 -AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVE-NVLASHPDIVEVAV 452
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
1910-2452 3.74e-16

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 86.35  E-value: 3.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1910 PEDRQQLWAWNQEVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKS 1989
Cdd:PRK06155     2 EPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1990 MWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSAQHSAR--------------WI----GTNHQVVTVS 2051
Cdd:PRK06155    82 IEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAAleaadpgdlplpavWLldapASVSVPAGWS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2052 AGSLEQFSTLVNPVDlpAKPENAAYVMFTSGSTGTPKGVvlehravvtsCLGHGQAF--GVtNLLRALQFTA----YT-- 2123
Cdd:PRK06155   162 TAPLPPLDAPAPAAA--VQPGDTAAILYTSGTTGPSKGV----------CCPHAQFYwwGR-NSAEDLEIGAddvlYTtl 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2124 --FDV-CIAEIITTLVHGGCICVP---SDSERRDNLAKAitdmQVNWGYLTSSVARLLDPclVP--------SLKVLVLG 2189
Cdd:PRK06155   229 plFHTnALNAFFQALLAGATYVLEprfSASGFWPAVRRH----GATVTYLLGAMVSILLS--QParesdrahRVRVALGP 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2190 GEQVNSTDWGKWPSSVQTINGYGPTECCVFCtgYTGIQGFQSGNIGtSIAS--VSWVVDpeNHGRLAPLGSIGELLV--- 2264
Cdd:PRK06155   303 GVPAALHAAFRERFGVDLLDGYGSTETNFVI--AVTHGSQRPGSMG-RLAPgfEARVVD--EHDQELPDGEPGELLLrad 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2265 EGPILARGYLNDVDKTQAAFIDdpAWllegypghegrqgrlYKTGDLVRYSSDGNLVCLGR-KDSqVKVRGQRVELGEVE 2343
Cdd:PRK06155   378 EPFAFATGYFGMPEKTVEAWRN--LW---------------FHTGDRVVRDADGWFRFVDRiKDA-IRRRGENISSFEVE 439
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2344 HHMRKcLPEANQLAVEVVPPSGERDHAMLAafIRLDDETRNSPL-IIKYAEdnstaqivfltgieeelsERLPQHMVPTV 2422
Cdd:PRK06155   440 QVLLS-HPAVAAAAVFPVPSELGEDEVMAA--VVLRDGTALEPVaLVRHCE------------------PRLAYFAVPRY 498
                          570       580       590
                   ....*....|....*....|....*....|
gi 1820002560 2423 FFALVHFPTTTSGKTDRKRLREIGasFTAQ 2452
Cdd:PRK06155   499 VEFVAALPKTENGKVQKFVLREQG--VTAD 526
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
3471-3996 4.21e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 85.98  E-value: 4.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 3550
Cdd:PRK07786    27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3551 EEIFEQTGAQVVVASAQYS-----ARWTSSSCHVVTVSKALS--------------SQLPAVVDSTNTSvrpenAAYIIF 3611
Cdd:PRK07786   107 AFLVSDCGAHVVVTEAALApvataVRDIVPLLSTVVVAGGSSddsvlgyedllaeaGPAHAPVDIPNDS-----PALIMY 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3612 TSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFD-ACIAEIITTLLCGGCICV-PSDSDRRNSLAKAI 3689
Cdd:PRK07786   182 TSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHiAGIGSMLPGLLLGAPTVIyPLGAFDPGQLLDVL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3690 STMDVNWAFLTPS--VARLLDPGLIP---SLKILAIGGEQSSSADWNR----WPGSvQKIHVYGPTE-----CCIFCTGY 3755
Cdd:PRK07786   262 EAEKVTGIFLVPAqwQAVCAEQQARPrdlALRVLSWGAAPASDTLLRQmaatFPEA-QILAAFGQTEmspvtCMLLGEDA 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3756 TTKQGfepsTIGTSVASVSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFiddpawllegypghpgrQG 3835
Cdd:PRK07786   341 IRKLG----SVGKVIPTVAARVVDENMNDVPV-GEVGEIVYRAPTLMSGYWNNPEATAEAF-----------------AG 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3836 RLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAveVILPSGQKDHAMLAAFVQLeegtq 3915
Cdd:PRK07786   399 GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVE-NVLASHPDIVEVA--VIGRADEKWGEVPVAVAAV----- 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3916 nalldkeAGGEDSMAqvvfLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREigaSFTAQQLAEMRTSSQG 3995
Cdd:PRK07786   471 -------RNDDAALT----LEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE---RYGACVNVERRSASAG 536

                   .
gi 1820002560 3996 P 3996
Cdd:PRK07786   537 F 537
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
73-285 4.40e-16

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 85.42  E-value: 4.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   73 GTIGTSIASVSWVVDPKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinnpawlleghggyagRQGRLYKTGDL 152
Cdd:cd05941    264 GTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF----------------TDDGWFKTGDL 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  153 VRYDADGNLVCLGR-KDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVeVVLP---LGQKnhatLAAFIQLDKGTHNall 228
Cdd:cd05941    328 GVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLA-HPGVSECAV-IGVPdpdWGER----VVAVVVLRAGAAA--- 398
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  229 kekvggddsiarvVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:cd05941    399 -------------LSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
3477-3975 5.15e-16

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 85.22  E-value: 5.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3477 APAICAWDGELTYGELDALSSKLASHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFE 3555
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3556 QTGAQVVVASAQYSARwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVLEHRAVATSCLG 3635
Cdd:cd05958     81 KARITVALCAHALTAS--------------------------------DDICILAFTSGTTGAPKATMHFHRDPLASADR 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3636 HGR-AFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFLTPSVAR----LLDPG 3710
Cdd:cd05958    129 YAVnVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRamlaHPDAA 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3711 --LIPSLKILAIGGEQSSSADWNRWPGS--VQKIHVYGPTECC-IFCTgyTTKQGFEPSTIGTSVASVSW-VVDPENhnR 3784
Cdd:cd05958    209 gpDLSSLRKCVSAGEALPAALHRAWKEAtgIPIIDGIGSTEMFhIFIS--ARPGDARPGATGKPVPGYEAkVVDDEG--N 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3785 LAPLGSMGELLMEGPIlarGYLNDVDKTEAAFIDDpAWLLegypghpgrqgrlykTGDLVQYNADGNLVYLGRKDSQVKV 3864
Cdd:cd05958    285 PVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQG-GWNI---------------TGDTYSRDPDGYFRHQGRSDDMIVS 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3865 RGQRVELGEVEhhvrECL---PEARQLAVevilpSGQKDHAMLA---AFVQLEEGtqnalldkEAGGEDSMAQVvflasv 3938
Cdd:cd05958    346 GGYNIAPPEVE----DVLlqhPAVAECAV-----VGHPDESRGVvvkAFVVLRPG--------VIPGPVLAREL------ 402
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 3939 eEELAKR-LPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd05958    403 -QDHAKAhIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
7633-8122 5.29e-16

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 85.12  E-value: 5.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHPASRHEE---IFEQTGAQVVV 7709
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFREHElafILRRAKAKVFV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7710 AsaqysarwtssschvvtvskalssqlPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGIT 7789
Cdd:cd05903     79 V--------------------------PERFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7790 NLSRVLQFASYtfdACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFL----TPSVARLLD-----PGLIPS 7860
Cdd:cd05903    133 PGDVFLVASPM---AHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFmmgaTPFLTDLLNaveeaGEPLSR 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7861 LKILAIGG--------EQSSSAdwnrwpGSVQKIHVYGPTECCIFCTGYT-TKQGFEPSTIGTSVASVSWVVDPENHNRL 7931
Cdd:cd05903    210 LRTFVCGGatvprslaRRAAEL------LGAKVCSAYGSTECPGAVTSITpAPEDRRLYTDGRPLPGVEIKVVDDTGATL 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7932 APlGSMGELLMEGPILARGYLNDVDKTEAAFIDdpAWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVR 8011
Cdd:cd05903    284 AP-GVEGELLSRGPSVFLGYLDRPDLTADAAPE--GW---------------FRTGDLARLDEDGYLRITGRSKDIIIRG 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8012 GQRVELGEVEhhvrECL---PEARQLAVeVILPSGQKNHAMLAVFVQlgkgthiahleeKAGGEDSMAQVV-FLTGteee 8087
Cdd:cd05903    346 GENIPVLEVE----DLLlghPGVIEAAV-VALPDERLGERACAVVVT------------KSGALLTFDELVaYLDR---- 404
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1820002560 8088 laKRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:cd05903    405 --QGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
2-285 5.50e-16

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 85.58  E-value: 5.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARL------LEPSHIPSLRILVMGGEQVNSADWDR----WPSSVQTIngYGPTECCIVCTGYTSEQDFT 71
Cdd:COG1021    274 RVTVTALVPPLALLwldaaeRSRYDLSSLRVLQVGGAKLSPELARRvrpaLGCTLQQV--FGMAEGLVNYTRLDDPEEVI 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   72 TGTIGTSIAS---VsWVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNpawlleghgGYagrqgrlYK 148
Cdd:COG1021    352 LTTQGRPISPddeV-RIVD--EDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPD---------GF-------YR 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  149 TGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVeVVLP---LGQKNHatlaAFIQLDKGTHN 225
Cdd:COG1021    413 TGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLA-HPAVHDAAV-VAMPdeyLGERSC----AFVVPRGEPLT 486
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  226 AL-LKEkvggddsiarvvFLAgveeelAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:COG1021    487 LAeLRR------------FLR------ERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
4543-5056 5.69e-16

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 85.60  E-value: 5.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4543 VHDQFA--EQARARPDTPAICAWDG---EL--TYGELDTLSSKLASHLVQL-GVKPEDMVPLCFEK-SMWTVVAmLAVLK 4613
Cdd:cd05928     11 VLDQWAdkEKAGKRPPNPALWWVNGkgdEVkwSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRvPEWWLVN-VACIR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4614 AGGAFVPLDPDHPASRHEHIFRQTGAQVVLASAQYATLWTSLG------RSVVIVSE---------------ASTSQLPV 4672
Cdd:cd05928     90 TGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVAsecpslKTKLLVSEksrdgwlnfkellneASTEHHCV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4673 VTKTADPSVnpgnaayAIFTSGSTGIPKgvVLEHKavvTSCLGHGQAFG---ITDHTRVLQFASYTFDACIAEIITTLL- 4748
Cdd:cd05928    170 ETGSQEPMA-------IYFTSGTTGSPK--MAEHS---HSSLGLGLKVNgryWLDLTASDIMWNTSDTGWIKSAWSSLFe 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4749 --CCGCiCVPSDSDRR---NNLAKAINAMDVNWALLTPSVARMLdpcvVQ---------SLKILVLGGEQVNSADWDRWP 4814
Cdd:cd05928    238 pwIQGA-CVFVHHLPRfdpLVILKTLSSYPITTFCGAPTVYRML----VQqdlssykfpSLQHCVTGGEPLNPEVLEKWK 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4815 K--SIQTINAYGPTECSICCTTYSGKQgFKSGTIGTSIVSVSWVVDPENHNRLAPlGSIGELLVE-GPI----LARGYLN 4887
Cdd:cd05928    313 AqtGLDIYEGYGQTETGLICANFKGMK-IKPGSMGKASPPYDVQIIDDNGNVLPP-GTEGDIGIRvKPIrpfgLFSGYVD 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4888 DMEKTEAAFiddpawllegygghsgrQGRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVRECLTEAKQ 4967
Cdd:cd05928    391 NPEKTAATI-----------------RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVES 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4968 LAVEVIVP-EGEggyaMLAAFVQLGDDtyntlvkekaggdsltvqvvFLDRVEEELAKRVPEHMMLTTF---------FT 5037
Cdd:cd05928    454 AVVSSPDPiRGE----VVKAFVVLAPQ--------------------FLSHDPEQLTKELQQHVKSVTApykyprkveFV 509
                          570
                   ....*....|....*....
gi 1820002560 5038 LEaMPTTTSGKIDRKRLRE 5056
Cdd:cd05928    510 QE-LPKTVTGKIQRNELRD 527
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
7632-8123 6.32e-16

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 85.66  E-value: 6.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7632 ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVAS 7711
Cdd:cd17642     44 NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7712 AQYSARWTSSSCHVVTVSKAL------------------SSQLPAVVDS----TNTSVRPENAAYIIFTSGSTGVPKGVV 7769
Cdd:cd17642    124 KKGLQKVLNVQKKLKIIKTIIildskedykgyqclytfiTQNLPPGFNEydfkPPSFDRDEQVALIMNSSGSTGLPKGVQ 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7770 LEHRAVATScLGHGR--AFG--ITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLaKAISTMDVNWAFL 7845
Cdd:cd17642    204 LTHKNIVAR-FSHARdpIFGnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFL-RSLQDYKVQSALL 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7846 TPSV------ARLLDPGLIPSLKILAIGGEQSSS------ADWNRWPGSVQKihvYGPTECCIfcTGYTTKQGF-EPSTI 7912
Cdd:cd17642    282 VPTLfaffakSTLVDKYDLSNLHEIASGGAPLSKevgeavAKRFKLPGIRQG---YGLTETTS--AILITPEGDdKPGAV 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7913 GTSVASVSW-VVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTGDLVQ 7991
Cdd:cd17642    357 GKVVPFFYAkVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEATKAL-IDKDGWL---------------HSGDIAY 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7992 YNADGNLVYLGRKDSQVKVRGQRVELGEVehhvreclpEARQLAVEVILPSGqknhamlavfvqlgkgthIAHLEEKAGG 8071
Cdd:cd17642    420 YDEDGHFFIVDRLKSLIKYKGYQVPPAEL---------ESILLQHPKIFDAG------------------VAGIPDEDAG 472
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 8072 EDSMAQVVFLTG---TEEEL----------AKRLPKhmvpTVFFaLLHFPMTTSGKADRKRLREI 8123
Cdd:cd17642    473 ELPAAVVVLEAGktmTEKEVmdyvasqvstAKRLRG----GVKF-VDEVPKGLTGKIDRRKIREI 532
PRK05857 PRK05857
fatty acid--CoA ligase;
5615-6050 6.48e-16

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 85.45  E-value: 6.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5615 NVPPAI-ERCVhdlftEQAKARPHAPAICAWDG--ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLA 5691
Cdd:PRK05857    11 QLPSTVlDRVF-----EQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5692 VLKAGGAFVPLDPDHPA---SRHEDTFRHT------GAQVVVTSAQHSARWIGTNHQVVTVSAGSLGQLSTLVNPVGLPA 5762
Cdd:PRK05857    86 CAKLGAIAVMADGNLPIaaiERFCQITDPAaalvapGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNAD 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5763 I-PENAVYIMFTSGSTGIPKGVVLEHR---AVVTSCwgrgRAFGITNLSRVLQFASY-----TFDACMDEIITTLMYGG- 5832
Cdd:PRK05857   166 QgSEDPLAMIFTSGTTGEPKAVLLANRtffAVPDIL----QKEGLNWVTWVVGETTYsplpaTHIGGLWWILTCLMHGGl 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5833 CIcvpSDSDRRNDLVKAISTMDVSCALLTPS-VARL-----LEPSSVPTLQMLVLQGEQVSFADWNRWPAS-VQTINGYG 5905
Cdd:PRK05857   242 CV---TGGENTTSLLEILTTNAVATTCLVPTlLSKLvselkSANATVPSLRLVGYGGSRAIAADVRFIEATgVRTAQVYG 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5906 PTE--CS-ICCNTYSGK-QGFKSGIIGTSVASVSWVVDPENH-----DRLAPLGSIGELLVEGPILARGYLNDIQKTAAV 5976
Cdd:PRK05857   319 LSEtgCTaLCLPTDDGSiVKIEAGAVGRPYPGVDVYLAATDGigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAEV 398
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 5977 FIDdpAWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhHVRECLPEARQLA 6050
Cdd:PRK05857   399 LID--GWV---------------NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGVSGVREAA 454
PRK06188 PRK06188
acyl-CoA synthetase; Validated
5626-6137 6.58e-16

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 85.42  E-value: 6.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpd 5705
Cdd:PRK06188    16 HLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL--- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5706 HP-ASRHEDTFRHTGAQV---VVTSAQHSARWIGTNHQVVTVS----------AGSLGQLSTLVNPVGL--PAIPENAVY 5769
Cdd:PRK06188    93 HPlGSLDDHAYVLEDAGIstlIVDPAPFVERALALLARVPSLKhvltlgpvpdGVDLLAAAAKFGPAPLvaAALPPDIAG 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 IMFTSGSTGIPKGVVLEHRAVVT------SCWG---RGRAFGITNLSRvlqfASYTFdacmdeIITTLMYGGCICVPSDS 5840
Cdd:PRK06188   173 LAYTGGTTGKPKGVMGTHRSIATmaqiqlAEWEwpaDPRFLMCTPLSH----AGGAF------FLPTLLRGGTVIVLAKF 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5841 DrRNDLVKAISTMDVSCALLTPS-VARLLEPSSVPT-----LQMLVLQGEQVSfadwnrwPAS-VQTINGYGP------- 5906
Cdd:PRK06188   243 D-PAEVLRAIEEQRITATFLVPTmIYALLDHPDLRTrdlssLETVYYGASPMS-------PVRlAEAIERFGPifaqyyg 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5907 -TECSICCNTYSGKQ------------GFKsgIIGTSVAsvswVVDPEnhDRLAPLGSIGELLVEGPILARGYLNDIQKT 5973
Cdd:PRK06188   315 qTEAPMVITYLRKRDhdpddpkrltscGRP--TPGLRVA----LLDED--GREVAQGEVGEICVRGPLVMDGYWNRPEET 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5974 AAVFIDDpaWLlegypgHpgrqgrlykTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAV-- 6051
Cdd:PRK06188   387 AEAFRDG--WL------H---------TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAE-HPAVAQVAVig 448
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6052 -------E-----VILPSGQK-DHAMLAAFVQLEEGTQNAlldkeasgedsMAQVVFLASVeeelakrlpehmvptvffs 6118
Cdd:PRK06188   449 vpdekwgEavtavVVLRPGAAvDAAELQAHVKERKGSVHA-----------PKQVDFVDSL------------------- 498
                          570
                   ....*....|....*....
gi 1820002560 6119 llhfPTTTSGKTDRKRLRE 6137
Cdd:PRK06188   499 ----PLTALGKPDKKALRA 513
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
49-285 6.95e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 85.44  E-value: 6.95e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   49 INGYGPTECCIVCTGYTSEQDFTTGTIG-----TSIAsvswVVDPKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAA 123
Cdd:PRK05605   365 VEGYGLTETSPIIVGNPMSDDRRPGYVGvpfpdTEVR----IVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAK 440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  124 VFinnpawllegHGGYagrqgrlYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVeVVL 203
Cdd:PRK05605   441 SF----------LDGW-------FRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLRE-HPGVEDAAV-VGL 501
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  204 PLGQKNHATLAAfIQLDKGthnALLKEkvggddsiarvvflAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:PRK05605   502 PREDGSEEVVAA-VVLEPG---AALDP--------------EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREV 563

                   ..
gi 1820002560  284 RE 285
Cdd:PRK05605   564 RE 565
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
877-1368 7.20e-16

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 85.27  E-value: 7.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpghpasrheEIFKQIGAQVVLTS 956
Cdd:cd17642     44 NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTN---------DIYNERELDHSLNI 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  957 SQHAMLFASserhQVTVSKVST--SQLPTV------------------VNFAKSPVDPG---------------NTAYII 1001
Cdd:cd17642    115 SKPTIVFCS----KKGLQKVLNvqKKLKIIktiiildskedykgyqclYTFITQNLPPGfneydfkppsfdrdeQVALIM 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1002 FTSGTTGIPKGVVLQHRAVTTSclghgeafgyTDHARVLQFASYTF-DACIAEII---------TTLLYGGC---ICVPS 1068
Cdd:cd17642    191 NSSGSTGLPKGVQLTHKNIVAR----------FSHARDPIFGNQIIpDTAILTVIpfhhgfgmfTTLGYLICgfrVVLMY 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1069 ESDRRNNLaKAISTMDVNCALLTPSVARLLEPSAV------PSLKRLVLQGEQVS------FADWNRWPGSVQtinGYGP 1136
Cdd:cd17642    261 KFEEELFL-RSLQDYKVQSALLVPTLFAFFAKSTLvdkydlSNLHEIASGGAPLSkevgeaVAKRFKLPGIRQ---GYGL 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1137 TECSVCcnTYSGKQGF-KSGIIGTSVASLSW-VVDAGNHNRLAPlGSIGELLVEGPILARGYLNDIDKTEAAfIDDPAWL 1214
Cdd:cd17642    337 TETTSA--ILITPEGDdKPGAVGKVVPFFYAkVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEATKAL-IDKDGWL 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1215 legyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhhvreclpearqlavEVILpsgQKEHAL 1294
Cdd:cd17642    413 ---------------HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELE---------------SILL---QHPKIF 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1295 LAAFIQLdkgnhnalfEEKASGEDSMAQVVFLTGV---EEEL----------AKRLPEHMVptilfTVKAMPITTSGKID 1361
Cdd:cd17642    460 DAGVAGI---------PDEDAGELPAAVVVLEAGKtmtEKEVmdyvasqvstAKRLRGGVK-----FVDEVPKGLTGKID 525

                   ....*..
gi 1820002560 1362 RKRLQDI 1368
Cdd:cd17642    526 RRKIREI 532
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
5647-6137 7.54e-16

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 84.32  E-value: 7.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5647 ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDhpASRHEDTFRHTGAQVVVts 5726
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR--LTPNELAFQLKDSDVKL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5727 aqhsarwigtnhqvvtvsagslgqlstlvnpvglpaipENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNL 5806
Cdd:cd05912     77 --------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5807 SRVLQFASYTFDACMDEIITTLMYGGCICVPS--DSDRRNDLVKA--ISTMDVSCALLTPSVARLLEPSSvPTLQMLVLQ 5882
Cdd:cd05912    119 DNWLCALPLFHISGLSILMRSVIYGMTVYLVDkfDAEQVLHLINSgkVTIISVVPTMLQRLLEILGEGYP-NNLRCILLG 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5883 GEqvsfadwnrwPASVQTI-----------NGYGPTE-CSICCnTYSGKQGF-KSGIIGTSVASVSW-VVDPENhdrlaP 5948
Cdd:cd05912    198 GG----------PAPKPLLeqckekgipvyQSYGMTEtCSQIV-TLSPEDALnKIGSAGKPLFPVELkIEDDGQ-----P 261
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5949 LGSIGELLVEGPILARGYLNDIQKTAAVFIDDpaWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQ 6028
Cdd:cd05912    262 PYEVGEILLKGPNVTKGYLNRPDATEESFENG--WF---------------KTGDIGYLDEEGFLYVLDRRSDLIISGGE 324
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6029 RVELGEVEHHVREcLPEARQLAVeVILPSGQKDHAMLAAFVQLEEGTQNALLDkeasgedsmaqvvFLasvEEELAKrlp 6108
Cdd:cd05912    325 NIYPAEIEEVLLS-HPAIKEAGV-VGIPDDKWGQVPVAFVVSERPISEEELIA-------------YC---SEKLAK--- 383
                          490       500
                   ....*....|....*....|....*....
gi 1820002560 6109 eHMVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:cd05912    384 -YKVPKKIYFVDELPRTASGKLLRHELKQ 411
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
2561-2842 8.19e-16

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 84.38  E-value: 8.19e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2561 LTPIQHLYLTLD--PSGRSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFqRQTGGRWQQYISEHDSSSLIVN- 2637
Cdd:cd19066      4 LSPMQRGMWFLKklATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF-CEEAGRYEQVVLDKTVRFRIEIi 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2638 --HIHTRDTTEIVEALRQ-SRGSLDIERGPVLAAVLCDAGERQSLFV-AIHHLVVDLVSWRILLEELE----DLLLGQTL 2709
Cdd:cd19066     83 dlRNLADPEARLLELIDQiQQTIYDLERGPLVRVALFRLADERDVLVvAIHHIIVDGGSFQILFEDISsvydAAERQKPT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2710 PPALSTPFQAWHAAQAKYIEehvppSAVAQVELD-----------PDQLSYWGVSPDdvLSSYAISE-EFVLDRKTTSTL 2777
Cdd:cd19066    163 LPPPVGSYADYAAWLEKQLE-----SEAAQADLAywtsylhglppPLPLPKAKRPSQ--VASYEVLTlEFFLRSEETKRL 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 2778 LGSCNdAFSTRPLELMVAALSySFATIFSDRKPAAIFNEIHGREawdsSIDLTRTVGWFTSMCPV 2842
Cdd:cd19066    236 REVAR-ESGTTPTQLLLAAFA-LALKRLTASIDVVIGLTFLNRP----DEAVEDTIGLFLNLLPL 294
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
1955-2362 9.77e-16

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 84.57  E-value: 9.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPL--------------CFEKSMwTVVAMLAVLkaGGafvpldpdhPASRHEd 2020
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIfaetraewlitalgCWSQNI-PIVTVYATL--GE---------DALIHS- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2021 iFRQTGAQVVVTSAqhsarwigtnhqvvtvsagsleqfstlvnpvdlpaKPENAAYVMFTSGSTGTPKGVVLEHRAVVTS 2100
Cdd:cd17639     73 -LNETECSAIFTDG-----------------------------------KPDDLACIMYTSGSTGNPKGVMLTHGNLVAG 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2101 ClgHGQAFGVTNLL----RALQF--TAYTFDVCiAEIItTLVHGGCICVPS------DSERR------------------ 2150
Cdd:cd17639    117 I--AGLGDRVPELLgpddRYLAYlpLAHIFELA-AENV-CLYRGGTIGYGSprtltdKSKRGckgdltefkptlmvgvpa 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2151 --DNLAKAITDM---------QVNWGYLTSSVARLLDPCLVPSLKVLV-------LGGeQVNSTDWGKWPSSVQT----- 2207
Cdd:cd17639    193 iwDTIRKGVLAKlnpmgglkrTLFWTAYQSKLKALKEGPGTPLLDELVfkkvraaLGG-RLRYMLSGGAPLSADTqefln 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2208 ------INGYGPTE-CCvfCTGYTGIQGFQSGNIGTSIAS-----VSWvvdPE-NHGRLAPLGSiGELLVEGPILARGYL 2274
Cdd:cd17639    272 ivlcpvIQGYGLTEtCA--GGTVQDPGDLETGRVGPPLPCceiklVDW---EEgGYSTDKPPPR-GEILIRGPNVFKGYY 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2275 NDVDKTQAAFIDDpawllegypghegrqgRLYKTGDLVRYSSDGNLVCLGRKDSQVKVR-GQRVELGEVEHHMRKClPEA 2353
Cdd:cd17639    346 KNPEKTKEAFDGD----------------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSN-PLV 408

                   ....*....
gi 1820002560 2354 NQLAVEVVP 2362
Cdd:cd17639    409 NNICVYADP 417
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
4566-5051 1.01e-15

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 84.42  E-value: 1.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4566 ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLAS 4645
Cdd:cd05914      7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4646 aqyatlwtslgrsvvivseastsqlpvvtktadpsvNPGNAAYAIFTSGSTGIPKGVVLEHKAV---VTSCLGHGQAfGI 4722
Cdd:cd05914     87 ------------------------------------DEDDVALINYTSGTTGNSKGVMLTYRNIvsnVDGVKEVVLL-GK 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4723 TDHTRVLQFASYTFDACI----------------------------AEIITTLLccgcICVP------SDSDRRNNLAKA 4768
Cdd:cd05914    130 GDKILSILPLHHIYPLTFtlllpllngahvvfldkipsakiialafAQVTPTLG----VPVPlviekiFKMDIIPKLTLK 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4769 INAMDVNWALLTPSVARMLDPCVVQS----LKILVLGGEQVNsADWDRWPKSIQ--TINAYGPTECS--ICcttYSGKQG 4840
Cdd:cd05914    206 KFKFKLAKKINNRKIRKLAFKKVHEAfggnIKEFVIGGAKIN-PDVEEFLRTIGfpYTIGYGMTETApiIS---YSPPNR 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4841 FKSGTIGTSIVSVSWVVDPENhnrlaPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpAWLlegygghsgrqgrlyKT 4920
Cdd:cd05914    282 IRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKD-GWF---------------HT 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4921 GDLVRYDADGNLVYLGRKDSQVKL-RGQRVELGEVEhhvRECLTEAKQLAVEVIVPEGEGgyaMLAAFVqlgddtYNTLV 4999
Cdd:cd05914    341 GDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIE---AKINNMPFVLESLVVVQEKKL---VALAYI------DPDFL 408
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 5000 KEKAGGDSLTVQVVfLDRVEEELAKRVPEHMMLTTF-FTLEAMPTTTSGKIDR 5051
Cdd:cd05914    409 DVKALKQRNIIDAI-KWEVRDKVNQKVPNYKKISKVkIVKEEFEKTPKGKIKR 460
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
877-1365 1.02e-15

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 84.07  E-value: 1.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKRE-DVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLT 955
Cdd:cd05958     10 EWTYRDLLALANRIANVLVGELGIVPgNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  956 SsqhamlfasserHQVTVSKvstsqlptvvnfakspvdpgNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHG-EAFGYT 1034
Cdd:cd05958     90 A------------HALTASD--------------------DICILAFTSGTTGAPKATMHFHRDPLASADRYAvNVLRLR 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1035 DHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNNLAKAISTMDVNCALLTPSVARLLEPSA------VPSLKR 1108
Cdd:cd05958    138 EDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPdaagpdLSSLRK 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1109 LVLQGEQVSFADWNRWPGS--VQTINGYGPTECsvcCNTY-SGKQG-FKSGIIGTSVA--SLSWVVDAGNHnrlAPLGSI 1182
Cdd:cd05958    218 CVSAGEALPAALHRAWKEAtgIPIIDGIGSTEM---FHIFiSARPGdARPGATGKPVPgyEAKVVDDEGNP---VPDGTI 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1183 GELLVEGPIlarGYLNDIDKTEAAFIDDpAWLLegyeghagrrgrlykTGDLVRCDADGNLVCLGRKDSQVKVRGQRVEL 1262
Cdd:cd05958    292 GRLAVRGPT---GCRYLADKRQRTYVQG-GWNI---------------TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAP 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1263 GEIEhhvrECL---PEARQLAVeVILPSgQKEHALLAAFIQLDKGnhnalfeeKASGEDSMAQVvfltgveEELAKR-LP 1338
Cdd:cd05958    353 PEVE----DVLlqhPAVAECAV-VGHPD-ESRGVVVKAFVVLRPG--------VIPGPVLAREL-------QDHAKAhIA 411
                          490       500
                   ....*....|....*....|....*..
gi 1820002560 1339 EHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd05958    412 PYKYPRAIEFVTELPRTATGKLQRFAL 438
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
1955-2343 1.06e-15

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 84.33  E-value: 1.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVtsa 2034
Cdd:cd17640      6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2035 qhsarwigtnhqvvtvsagsleqfstlvnpvdLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVtsclghgqaFGVTNLL 2114
Cdd:cd17640     83 --------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANLL---------HQIRSLS 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2115 RALQFTA-------------------YTFDVC-IAEIITTLVHggcicVPSDSER----------------RDNLAKAIT 2158
Cdd:cd17640    122 DIVPPQPgdrflsilpiwhsyersaeYFIFACgCSQAYTSIRT-----LKDDLKRvkphyivsvprlweslYSGIQKQVS 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2159 DMqvnwgyltSSVARLLdpclvpsLKVLVLGGE-QVNSTDWGKWPSSVQT---------INGYGPTECC-VFCTGYTGIQ 2227
Cdd:cd17640    197 KS--------SPIKQFL-------FLFFLSGGIfKFGISGGGALPPHVDTffeaigievLNGYGLTETSpVVSARRLKCN 261
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2228 gfQSGNIGTSIASVSW-VVDPENHGRLAPlGSIGELLVEGPILARGYLNDVDKTQAAfIDDPAWLlegypghegrqgrly 2306
Cdd:cd17640    262 --VRGSVGRPLPGTEIkIVDPEGNVVLPP-GEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDGWF--------------- 322
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1820002560 2307 KTGDLVRYSSDGNLVCLGR-KDSQVKVRGQRVELGEVE 2343
Cdd:cd17640    323 NTGDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIE 360
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
1912-2444 1.08e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 85.08  E-value: 1.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1912 DRQQLWAWNQEVPPAIERCVHDL--FTEQAKAR-PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEK 1988
Cdd:PRK06710     4 EKPWLKSYPEEIPSTISYDIQPLhkYVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1989 SMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVV---------VTSAQHSARwigTNHQVVTVSAGSLEQFS 2059
Cdd:PRK06710    84 CPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlcldlvfprVTNVQSATK---IEHVIVTRIADFLPFPK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2060 TLVNP--------------------------------VDLPAKPEN-AAYVMFTSGSTGTPKGVVLEHRAVVTSCL---- 2102
Cdd:PRK06710   161 NLLYPfvqkkqsnlvvkvsesetihlwnsvekevntgVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNLVSNTLmgvq 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2103 -------GHGQAFGVTNLLRALQFTAYtfdvciaeIITTLVHG-GCICVPSDSERRdnLAKAITDMQVNW--GYLTSSVA 2172
Cdd:PRK06710   241 wlynckeGEEVVLGVLPFFHVYGMTAV--------MNLSIMQGyKMVLIPKFDMKM--VFEAIKKHKVTLfpGAPTIYIA 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2173 RLLDPCL----VPSLKVLVLGG--------EQVNSTDWGKwpssvqTINGYGPTECCVFCTGYTGIQGFQSGNIGTSIAS 2240
Cdd:PRK06710   311 LLNSPLLkeydISSIRACISGSaplpvevqEKFETVTGGK------LVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPD 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2241 VSWVVDPENHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDdpAWLlegypghegrqgrlyKTGDLVRYSSDGNL 2320
Cdd:PRK06710   385 TEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQD--GWL---------------HTGDVGYMDEDGFF 447
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2321 VCLGRKDSQVKVRGQRVELGEVEHHMRKclPEANQLAVEVVPPSGERDHAmLAAFIRLDDETRNSpliikyaednstaqi 2400
Cdd:PRK06710   448 YVKDRKKDMIVASGFNVYPREVEEVLYE--HEKVQEVVTIGVPDPYRGET-VKAFVVLKEGTECS--------------- 509
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 2401 vfltgiEEELSE----RLPQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:PRK06710   510 ------EEELNQfarkYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
6279-6670 1.08e-15

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 83.97  E-value: 1.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6279 PCSPLQEGLMSLTAKRAGD--YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQV----------VV 6346
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGpaYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEilppgpapleVR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6347 EEKIQWTESKR-LEEYLREDKAVSMGL-GDPLARYAIIKeaWGGKRWF-VWTIHHALYDGWSLPRV------LQAVKQAY 6417
Cdd:cd19539     83 DLSDPDSDRERrLEELLRERESRGFDLdEEPPIRAVLGR--FDPDDHVlVLVAHHTAFDAWSLDVFardlaaLYAARRKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6418 NGAVL-ETQPSFNAFIQYLSQQDLEATAA----YWQTALADCEAT-LFPPLPSSVkQLVADTTVeHQCPLPSRSTSDTTT 6491
Cdd:cd19539    161 PAAPLpELRQQYKEYAAWQREALAAPRAAelldFWRRRLRGAEPTaLPTDRPRPA-GFPYPGAD-LRFELDAELVAALRE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6492 S---------TLIRAAWAIVASRYTSSDDVVFGTTITGRNAPVTsiDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQA 6562
Cdd:cd19539    239 LakrarsslfMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRF--ESTVGFFVNLLPLRVDVSDCATFRDLIARVRKAL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6563 TEMIAYEQTGLQQIAKMGPdPQHACG----FQTLLVVQPAGDVLGSDDTLGKWRGYSGLQDFMTYALGVRCTLSAEGVKI 6638
Cdd:cd19539    317 VDAQRHQELPFQQLVAELP-VDRDAGrhplVQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRG 395
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1820002560 6639 TASFDARVIEHWVVEKMLGQFSFAMQQLAEAS 6670
Cdd:cd19539    396 SLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
1925-2447 1.10e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 84.82  E-value: 1.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1925 PAIERCVHDLFTEQAKARPHAPAICAWDGEL--TYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmWTVVAMlA 1998
Cdd:PRK12583    14 PLLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVgiwaPNCAE---WLLTQF-A 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1999 VLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVT-----SAQHSARWIGTNHQVVTVSAGSL--EQFSTL---------- 2061
Cdd:PRK12583    90 TARIGAILVNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEGQPGALacERLPELrgvvslapap 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2062 ----------------VNPVDLPAK-----PENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLRALqfT 2120
Cdd:PRK12583   170 ppgflawhelqargetVSREALAERqasldRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLC--V 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2121 AYTFDVCIAEIITTLV---HGGCICVPSDSERRDNLAKAITDMQVN--WGYLTSSVARLLDPCL----VPSLKVLVLGG- 2190
Cdd:PRK12583   248 PVPLYHCFGMVLANLGcmtVGACLVYPNEAFDPLATLQAVEEERCTalYGVPTMFIAELDHPQRgnfdLSSLRTGIMAGa 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2191 -----------EQVNSTDwgkwpssVQTinGYGPTEccvfcTGYTGIQGFQSGNIGTSIASV--------SWVVDPEnhG 2251
Cdd:PRK12583   328 pcpievmrrvmDEMHMAE-------VQI--AYGMTE-----TSPVSLQTTAADDLERRVETVgrtqphleVKVVDPD--G 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2252 RLAPLGSIGELLVEGPILARGYLNDVDKTQAAfIDDPAWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVK 2331
Cdd:PRK12583   392 ATVPRGEIGELCTRGYSVMKGYWNNPEATAES-IDEDGWM---------------HTGDLATMDEQGYVRIVGRSKDMII 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2332 VRGQRVELGEVEHHMRKcLPEANQLAVEVVPPS--GERdhamLAAFIRLDDETRNSpliikyaednstaqivfltgiEEE 2409
Cdd:PRK12583   456 RGGENIYPREIEEFLFT-HPAVADVQVFGVPDEkyGEE----IVAWVRLHPGHAAS---------------------EEE 509
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 2410 LSE----RLPQHMVPTVFFALVHFPTTTSGKTDRKRLREIGA 2447
Cdd:PRK12583   510 LREfckaRIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISI 551
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
8264-8441 1.32e-15

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 80.47  E-value: 1.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8264 ASYIQQ-FYIAtgvRAPREAFNYPF-IDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIPRHQDLPFSIFEV 8341
Cdd:COG4908      1 LSPAQKrFLFL---EPGSNAYNIPAvLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8342 NG--------ALAEESQAIHIRDLDQTSPLGLptSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQ----E 8409
Cdd:COG4908     78 SAlpepereaELEELVAEEASRPFDLARGPLL--RAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAAllegE 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1820002560 8410 PLLSTTGFHSYLAYVHNQRS--------ASINYWSRLLKG 8441
Cdd:COG4908    156 PPPLPELPIQYADYAAWQRAwlqsealeKQLEYWRQQLAG 195
PRK07529 PRK07529
AMP-binding domain protein; Validated
825-1366 1.42e-15

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 84.62  E-value: 1.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  825 VADIETTTLEDRqqlwvwnaDMPpavdRCIHDLFAEQARARPDASAVC------AWDG--ELTYGELDELSSKLAAHLVQ 896
Cdd:PRK07529    10 IEAIEAVPLAAR--------DLP----ASTYELLSRAAARHPDAPALSflldadPLDRpeTWTYAELLADVTRTANLLHS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  897 LGVKREDVV----PLCFEksmwTVVAMLAVLKAGGAFvP----LDPGHPAsrheEIFKQIGAQVVLT------------- 955
Cdd:PRK07529    78 LGVGPGDVVafllPNLPE----THFALWGGEAAGIAN-PinplLEPEQIA----ELLRAAGAKVLVTlgpfpgtdiwqkv 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  956 --------SSQHAMLFASSERHQVTVSKVSTSQLPT----VVNF----AKSPVD---------PGNTAYIIFTSGTTGIP 1010
Cdd:PRK07529   149 aevlaalpELRTVVEVDLARYLPGPKRLAVPLIRRKaharILDFdaelARQPGDrlfsgrpigPDDVAAYFHTGGTTGMP 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1011 KGVVLQHRAVTTSCLGHGEAFGYtDHARVLQFASYTF--DACIAEIITTLLYGGCICVPSESDRRN-----NLAKAISTM 1083
Cdd:PRK07529   229 KLAQHTHGNEVANAWLGALLLGL-GPGDTVFCGLPLFhvNALLVTGLAPLARGAHVVLATPQGYRGpgviaNFWKIVERY 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1084 DVNCALLTPSV-ARLLE-PSA---VPSLkRLVLQG-----EQVsFADWNRWPGsVQTINGYGPTE--CSVCCNTYSGKQg 1151
Cdd:PRK07529   308 RINFLSGVPTVyAALLQvPVDghdISSL-RYALCGaaplpVEV-FRRFEAATG-VRIVEGYGLTEatCVSSVNPPDGER- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1152 fKSGIIG-------TSVASLSwvvDAGNHNRLAPLGSIGELLVEGPILARGYLNDiDKTEAAFIDDpAWLlegyeghagr 1224
Cdd:PRK07529   384 -RIGSVGlrlpyqrVRVVILD---DAGRYLRDCAVDEVGVLCIAGPNVFSGYLEA-AHNKGLWLED-GWL---------- 447
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1225 rgrlyKTGDLVRCDADGNLVCLGR-KDsqVKVR-GQRVELGEIE----HHvreclpEARQLAVEVILPSGqkeHA--LLA 1296
Cdd:PRK07529   448 -----NTGDLGRIDADGYFWLTGRaKD--LIIRgGHNIDPAAIEeallRH------PAVALAAAVGRPDA---HAgeLPV 511
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 1297 AFIQLDKGnhnalfeekasgedsmAQVvfltgVEEELAKRLPEHM-----VPTILFTVKAMPITTSGKIDRKRLQ 1366
Cdd:PRK07529   512 AYVQLKPG----------------ASA-----TEAELLAFARDHIaeraaVPKHVRILDALPKTAVGKIFKPALR 565
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
16-297 1.50e-15

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 85.36  E-value: 1.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   16 LEPSHIPSLRILVMGGEQVNS--ADWDRWPSSVQTINGYGPTECCIV---------CTGYTSEQDFTTGTIGTSIASVSW 84
Cdd:PRK08633   892 LHPLMFASLRLVVAGAEKLKPevADAFEEKFGIRILEGYGATETSPVasvnlpdvlAADFKRQTGSKEGSVGMPLPGVAV 971
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   85 -VVDPkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVF--INNPAWlleghggyagrqgrlYKTGDLVRYDADGNL 161
Cdd:PRK08633   972 rIVDP-ETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdIDGIGW---------------YVTGDKGHLDEDGFL 1035
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  162 VCLGRKDSQVKLRGQRVELGEVEHHVRECLPEAKQLAVEVVLPLGQknhatlaafiqldKGTHNALLKEKVGGDdsiarv 241
Cdd:PRK08633  1036 TITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAVPDEK-------------KGEKLVVLHTCGAED------ 1096
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  242 vfLAGVEEELAK-RLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIgasftAQQLAE 297
Cdd:PRK08633  1097 --VEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL-----ALALLG 1146
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
5641-6137 1.52e-15

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 84.22  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5641 ICAWDGE-----LTYGELDALSSKLAGHLTQLGVKPEDMVPLCfeksMWT----VVAMLAVLKAGGAFVPLDPDHPASRH 5711
Cdd:cd12119     14 IVSRTHEgevhrYTYAEVAERARRLANALRRLGVKPGDRVATL----AWNthrhLELYYAVPGMGAVLHTINPRLFPEQI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5712 EDTFRHTGAQVVVTSAQ-------------HSARWIGTNHQVVTVSAGSLGQLS--TLVNPV----GLPAIPENAVYIM- 5771
Cdd:cd12119     90 AYIINHAEDRVVFVDRDflplleaiaprlpTVEHVVVMTDDAAMPEPAGVGVLAyeELLAAEspeyDWPDFDENTAAAIc 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5772 FTSGSTGIPKGVVLEHRAVVTSCWGrGRAFGITNLSrvlqfasyTFDACMDEI-----------ITTLMYGGCICVPSDS 5840
Cdd:cd12119    170 YTSGTTGNPKGVVYSHRSLVLHAMA-ALLTDGLGLS--------ESDVVLPVVpmfhvnawglpYAAAMVGAKLVLPGPY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5841 DRRNDLVKAISTMDVSCALLTPSVARLL------EPSSVPTLQMLVLQGEQVSFADWNRWPAS-VQTINGYGPTECS--I 5911
Cdd:cd12119    241 LDPASLAELIEREGVTFAAGVPTVWQGLldhleaNGRDLSSLRRVVIGGSAVPRSLIEAFEERgVRVIHAWGMTETSplG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5912 CCNTYSGKQGFKSGI--------IGTSVASVSW-VVDPEnhDRLAPL--GSIGELLVEGPILARGYLNDIQKTAAVFIDD 5980
Cdd:cd12119    321 TVARPPSEHSNLSEDeqlalrakQGRPVPGVELrIVDDD--GRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDG 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5981 paWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGR-KDSqVKLRGQ---RVELgE---VEHhvreclPEARQLAVeV 6053
Cdd:cd12119    399 --WL---------------RTGDVATIDEDGYLTITDRsKDV-IKSGGEwisSVEL-EnaiMAH------PAVAEAAV-I 452
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6054 ILPSGQKDHAMLaAFVQLEEGTQnalLDKEAsgedsmaqvvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRK 6133
Cdd:cd12119    453 GVPHPKWGERPL-AVVVLKEGAT---VTAEE--------------LLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKK 514

                   ....
gi 1820002560 6134 RLRE 6137
Cdd:cd12119    515 ALRE 518
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
5638-6136 1.57e-15

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 83.68  E-value: 1.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5638 APAICAWDGELTYGELDALSSKLAGHLT-QLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFR 5716
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5717 HTGAQVVVTSAQHSARwigtnhqvvtvsagslgqlstlvnpvglpaipENAVYIMFTSGSTGIPKGVVLEHRAVVTSC-- 5794
Cdd:cd05958     81 KARITVALCAHALTAS--------------------------------DDICILAFTSGTTGAPKATMHFHRDPLASAdr 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5795 WGRgRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRNDLVKAIS-----------TMDVSCALLTPS 5863
Cdd:cd05958    129 YAV-NVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIArykptvlftapTAYRAMLAHPDA 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5864 VARLLEPssvptLQMLVLQGEQVSFADWNRWPAS--VQTINGYGPTEcsiCCNTY-SGKQG-FKSGIIGTSVASV-SWVV 5938
Cdd:cd05958    208 AGPDLSS-----LRKCVSAGEALPAALHRAWKEAtgIPIIDGIGSTE---MFHIFiSARPGdARPGATGKPVPGYeAKVV 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5939 DPENHDrlAPLGSIGELLVEGPIlarGYLNDIQKTAAVFIDDpAWLLegypghpgrqgrlykTGDLVRYDANGNLVCLGR 6018
Cdd:cd05958    280 DDEGNP--VPDGTIGRLAVRGPT---GCRYLADKRQRTYVQG-GWNI---------------TGDTYSRDPDGYFRHQGR 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6019 KDSQVKLRGQRVELGEVEhhvrECL---PEARQLAVevilpSGQKDHAMLA---AFVQLEEGtqnalldkEASGEDSMAQ 6092
Cdd:cd05958    339 SDDMIVSGGYNIAPPEVE----DVLlqhPAVAECAV-----VGHPDESRGVvvkAFVVLRPG--------VIPGPVLARE 401
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 6093 VvflasveEELAKR-LPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:cd05958    402 L-------QDHAKAhIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
PRK07514 PRK07514
malonyl-CoA synthase; Validated
4551-5056 1.62e-15

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 84.16  E-value: 1.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAICAWDGE-LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 4629
Cdd:PRK07514    12 AFADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4630 HEHIFRQTG-AQVVLASAQYATL----WTSLGRSVVIVSEASTSQLPVVTKTADPS-----VNPGNAAYAIFTSGSTGIP 4699
Cdd:PRK07514    92 LDYFIGDAEpALVVCDPANFAWLskiaAAAGAPHVETLDADGTGSLLEAAAAAPDDfetvpRGADDLAAILYTSGTTGRS 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4700 KGVVLEHKAVVTSCLGHGQAFGITD-----------HTRVLQFASYtfdaciaeiiTTLLcCGC--ICVPS-DSDR-RNN 4764
Cdd:PRK07514   172 KGAMLSHGNLLSNALTLVDYWRFTPddvlihalpifHTHGLFVATN----------VALL-AGAsmIFLPKfDPDAvLAL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4765 LAKAINAMDVnwalltPSV-ARML-----DPCVVQSLKILVLGgeqvnSAdwdrwPKSIQTINA------------YGPT 4826
Cdd:PRK07514   241 MPRATVMMGV------PTFyTRLLqeprlTREAAAHMRLFISG-----SA-----PLLAETHREfqertghailerYGMT 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4827 E-CSICCTTYSGKQgfKSGTIGTSI--VSVSwVVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAFIDDpawl 4903
Cdd:PRK07514   305 EtNMNTSNPYDGER--RAGTVGFPLpgVSLR-VTDPETGAELPP-GEIGMIEVKGPNVFKGYWRMPEKTAEEFRAD---- 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4904 leGYgghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhhvreclTEAKQLA--VE--VI-VPE-- 4976
Cdd:PRK07514   377 --GF----------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVE-------GEIDELPgvVEsaVIgVPHpd 437
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4977 -GEGGYAMLAAfvqlgddtyntlvKEKAGGDSLTVqvvfLDRVEEELAK-RVPEHmmlttFFTLEAMPTTTSGKIDRKRL 5054
Cdd:PRK07514   438 fGEGVTAVVVP-------------KPGAALDEAAI----LAALKGRLARfKQPKR-----VFFVDELPRNTMGKVQKNLL 495

                   ..
gi 1820002560 5055 RE 5056
Cdd:PRK07514   496 RE 497
PRK07514 PRK07514
malonyl-CoA synthase; Validated
855-1250 1.82e-15

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 83.77  E-value: 1.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  855 HDLFA--EQARARPDASAVCAWDGE-LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVP 931
Cdd:PRK07514     3 NNLFDalRAAFADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  932 LDPGHPASrheEIFKQIG----AQVVLTSSQHAMLFASSERHQVTvsKVST-------------SQLPTvvNFAKSPVDP 994
Cdd:PRK07514    83 LNTAYTLA---ELDYFIGdaepALVVCDPANFAWLSKIAAAAGAP--HVETldadgtgslleaaAAAPD--DFETVPRGA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  995 GNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTD-----------HARVLQFASYtfdaciaeiiTTLLYGG- 1062
Cdd:PRK07514   156 DDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPddvlihalpifHTHGLFVATN----------VALLAGAs 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1063 CICVPS-ESDR-RNNLAKAISTMDVncalltPSV-ARLLE-----PSAVPSLkRLVLQG------EqvSFADWNRWPGsv 1128
Cdd:PRK07514   226 MIFLPKfDPDAvLALMPRATVMMGV------PTFyTRLLQeprltREAAAHM-RLFISGsapllaE--THREFQERTG-- 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1129 QTI-NGYGPTE-CSVCCNTYSGKQ-----GFKsgIIGTSVAslswVVDAGNHNRLAPlGSIGELLVEGPILARGYLNDID 1201
Cdd:PRK07514   295 HAIlERYGMTEtNMNTSNPYDGERragtvGFP--LPGVSLR----VTDPETGAELPP-GEIGMIEVKGPNVFKGYWRMPE 367
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1202 KTEAAFIDDpawlleGYeghagrrgrlYKTGDLVRCDADGNLVCLGR-KD 1250
Cdd:PRK07514   368 KTAEEFRAD------GF----------FITGDLGKIDERGYVHIVGRgKD 401
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3603-3975 1.83e-15

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 82.33  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3603 PENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRV-LQFASYTFDACIAEIITTLLCGGCICVPSDS-D 3680
Cdd:cd05917      1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcIPVPLFHCFGSVLGVLACLTHGATMVFPSPSfD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3681 RRNSLAkAISTMDVNWAFLTPS--VARLLDPGL----IPSLKILAIGGEQSSSADWNRwpgSVQKIH------VYGPTEC 3748
Cdd:cd05917     81 PLAVLE-AIEKEKCTALHGVPTmfIAELEHPDFdkfdLSSLRTGIMAGAPCPPELMKR---VIEVMNmkdvtiAYGMTET 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3749 CIFCTgyttkQGFEPSTIGTSVASV--------SWVVDPENhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAfIDDP 3820
Cdd:cd05917    157 SPVST-----QTRTDDSIEKRVNTVgrimphteAKIVDPEG-GIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA-IDGD 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3821 AWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGR-KDsqVKVRGqrvelGE--VEHHVRECL---PEARQlaVEVIl 3894
Cdd:cd05917    230 GW---------------LHTGDLAVMDEDGYCRIVGRiKD--MIIRG-----GEniYPREIEEFLhthPKVSD--VQVV- 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3895 psGQKDHAM---LAAFVQLEEGtqnalldKEAGGEDsmaqvvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDR 3971
Cdd:cd05917    285 --GVPDERYgeeVCAWIRLKEG-------AELTEED----------IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345

                   ....
gi 1820002560 3972 KRLR 3975
Cdd:cd05917    346 FKLR 349
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
3450-3976 1.86e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 84.04  E-value: 1.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3450 GWNADVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQL-GVNPEDVVPLCFEKSMWTVVAM 3528
Cdd:PRK05677    13 GIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAV 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3529 LAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARWT-----SSSCHVV-----------------TVSKAL 3586
Cdd:PRK05677    93 FGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEkvlpkTGVKHVIvtevadmlpplkrllinAVVKHV 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3587 SSQLPAV-----------------VDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHR----------AVATSCLGHGRA 3639
Cdd:PRK05677   173 KKMVPAYhlpqavkfndalakgagQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRnlvanmlqcrALMGSNLNEGCE 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3640 FGITNLSrVLQFASYTFDaCIAeiitTLLCGG---CICVPSDSDrrnSLAKAIStmdvNWAFL------TPSVA------ 3704
Cdd:PRK05677   253 ILIAPLP-LYHIYAFTFH-CMA----MMLIGNhniLISNPRDLP---AMVKELG----KWKFSgfvglnTLFVAlcnnea 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3705 -RLLDpglIPSLKILAIGGEQSSSADWNRWPGsvqkihVYGptecCIFCTGY-----------TTKQGFEPSTIGTSVAS 3772
Cdd:PRK05677   320 fRKLD---FSALKLTLSGGMALQLATAERWKE------VTG----CAICEGYgmtetspvvsvNPSQAIQVGTIGIPVPS 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3773 VSW-VVDPENHNrlAPLGSMGELLMEGPILARGYLNDVDKTEAAFiDDPAWLlegypghpgrqgrlyKTGDLVQYNADGN 3851
Cdd:PRK05677   387 TLCkVIDDDGNE--LPLGEVGELCVKGPQVMKGYWQRPEATDEIL-DSDGWL---------------KTGDIALIQEDGY 448
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3852 LVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAveVILPSGQKDHAMLAAFVQLEEGtqnALLDKEAggedsmaq 3931
Cdd:PRK05677   449 MRIVDRKKDMILVSGFNVYPNELE-DVLAALPGVLQCA--AIGVPDEKSGEAIKVFVVVKPG---ETLTKEQ-------- 514
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 3932 vvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:PRK05677   515 ------VMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
3499-3975 1.94e-15

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 84.08  E-value: 1.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3499 LASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQ----------- 3567
Cdd:PLN02860    45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETcsswyeelqnd 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3568 --YSARW-----TSSSCHVVTVSKALSS----QLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGH 3636
Cdd:PLN02860   125 rlPSLMWqvfleSPSSSVFIFLNSFLTTemlkQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAK 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3637 GRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGC------------------------ICVPSdsdrrnSLAKAIST- 3691
Cdd:PLN02860   205 IAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAChvllpkfdakaalqaikqhnvtsmITVPA------MMADLISLt 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3692 -MDVNWAfLTPSVARLLDPGLIPSLKILAIGGEQSSSAdwnrwpgsvQKIHVYGPTECC---IFCTGYTTKQGFEPSTIG 3767
Cdd:PLN02860   279 rKSMTWK-VFPSVRKILNGGGSLSSRLLPDAKKLFPNA---------KLFSAYGMTEACsslTFMTLHDPTLESPKQTLQ 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3768 TSVASVSWVVD-----------PENHNRLAPLGS--MGELLMEGPILARGYLnDVDKTEAAFIDDPAWLlegypghpgrq 3834
Cdd:PLN02860   349 TVNQTKSSSVHqpqgvcvgkpaPHVELKIGLDESsrVGRILTRGPHVMLGYW-GQNSETASVLSNDGWL----------- 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3835 grlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE----HH------VRECLPEARQLavevilpsgqkdhAML 3904
Cdd:PLN02860   417 ----DTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEavlsQHpgvasvVVVGVPDSRLT-------------EMV 479
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 3905 AAFVQLEEGTQNALLDKE-AGGEDSMAQVVFLASVEEelaKRLPEHMVPTVFFSLLH-FPTTTSGKTDRKRLR 3975
Cdd:PLN02860   480 VACVRLRDGWIWSDNEKEnAKKNLTLSSETLRHHCRE---KNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVR 549
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
3022-3387 2.04e-15

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 83.13  E-value: 2.04e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3022 VFPCTPMQEGILTsQG---KDPDAYWVCFIYEVIPNQETSIslarLQQAWKGVVHQHSLLRTLLVdnVPGSTGTTNVVLK 3098
Cdd:cd19547      1 VYPLAPMQEGMLF-RGlfwPDSDAYFNQNVLELVGGTDEDV----LREAWRRVADRYEILRTGFT--WRDRAEPLQYVRD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3099 DPQPSISVFSSEGTAT---IELFRSRY--NPAAQRSIGQLQ-HHLSICQLNNGKVYLCLDINHAIIDAHSRGILMHDLQE 3172
Cdd:cd19547     74 DLAPPWALLDWSGEDPdrrAELLERLLadDRAAGLSLADCPlYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3173 AYD-------ANLNPqSTSFRDFASYIKQQSQ--EEAGRYWAEYLDGVEPCFF---PSlGDSGGANTIPRtvEVPSIDSS 3240
Cdd:cd19547    154 VYEelahgrePQLSP-CRPYRDYVRWIRARTAqsEESERFWREYLRDLTPSPFstaPA-DREGEFDTVVH--EFPEQLTR 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3241 AVHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPIHNVNSIFGPLISILPCRIHLHKQLTVLEALKTV 3320
Cdd:cd19547    230 LVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETI 309
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 3321 QENYASSLSFQTFPLASMHSFLG---LGTSALFNTALSLQRI-DDIGPCSASEITLKMKEGLDPTEYNITL 3387
Cdd:cd19547    310 HRDLATTAAHGHVPLAQIKSWASgerLSGGRVFDNLVAFENYpEDNLPGDDLSIQIIDLHAQEKTEYPIGL 380
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
862-1367 2.33e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 83.86  E-value: 2.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  862 ARARPDASAVCAWDGELTYGELDELSSKLAAHLVQ-LGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASR 940
Cdd:PRK08314    20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  941 HEEIFKQIGAQVVLTSS---------------QHAML-----------------FASSERHQVTVSKVSTSQLPTVVNFA 988
Cdd:PRK08314   100 LAHYVTDSGARVAIVGSelapkvapavgnlrlRHVIVaqysdylpaepeiavpaWLRAEPPLQALAPGGVVAWKEALAAG 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  989 KSP----VDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQFASYtFD--ACIAEIITTLLYGG 1062
Cdd:PRK08314   180 LAPpphtAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHvtGMVHSMNAPIYAGA 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1063 CICVPSESDRRnnLAK------------AISTMDVNcALLTPSvarlLEPSAVPSLKRLVLQGEQVSFADWNRWPG--SV 1128
Cdd:PRK08314   259 TVVLMPRWDRE--AAArlieryrvthwtNIPTMVVD-FLASPG----LAERDLSSLRYIGGGGAAMPEAVAERLKEltGL 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1129 QTINGYGPTEcsvccnTYSG-----KQGFKSGIIGTSVASL-SWVVDAGNHNRLAPlGSIGELLVEGPILARGYLNDIDK 1202
Cdd:PRK08314   332 DYVEGYGLTE------TMAQthsnpPDRPKLQCLGIPTFGVdARVIDPETLEELPP-GEVGEIVVHGPQVFKGYWNRPEA 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1203 TEAAFIDdpawlLEGyeghagrrGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIE----HH--VREC---- 1272
Cdd:PRK08314   405 TAEAFIE-----IDG--------KRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVEnllyKHpaIQEAcvia 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1273 LPEARqlavevilpSGQKehalLAAFIQLDKGnhnalFEEKASGEDSMAqvvfltgveeeLAKrlpEHM----VPTILFT 1348
Cdd:PRK08314   472 TPDPR---------RGET----VKAVVVLRPE-----ARGKTTEEEIIA-----------WAR---EHMaaykYPRIVEF 519
                          570
                   ....*....|....*....
gi 1820002560 1349 VKAMPITTSGKIDRKRLQD 1367
Cdd:PRK08314   520 VDSLPKSGSGKILWRQLQE 538
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
16-284 2.37e-15

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 82.89  E-value: 2.37e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   16 LEPSHIPSLRILVMGGEQVNSADWDRWPSS--VQTINGYGPTEccivcTGYTseqdFTTG-----TIGTSIASVSW---- 84
Cdd:cd05919    202 GSPDALRSLRLCVSAGEALPRGLGERWMEHfgGPILDGIGATE-----VGHI----FLSNrpgawRLGSTGRPVPGyeir 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   85 VVDPKdhGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinnpawlleghggyagrQGRLYKTGDLVRYDADGNLVCL 164
Cdd:cd05919    273 LVDEE--GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-----------------NGGWYRTGDKFCRDADGWYTHA 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  165 GRKDSQVKLRGQRVELGEVEhhvrECLPEAKQLAVEVVLPLGQKNHAT-LAAFIQLDKGTHNallkekvggDDSIARvvf 243
Cdd:cd05919    334 GRADDMLKVGGQWVSPVEVE----SLIIQHPAVAEAAVVAVPESTGLSrLTAFVVLKSPAAP---------QESLAR--- 397
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1820002560  244 laGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLR 284
Cdd:cd05919    398 --DIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
PRK08316 PRK08316
acyl-CoA synthetase; Validated
7598-8122 2.56e-15

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 83.44  E-value: 2.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7598 NADVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAV 7677
Cdd:PRK08316     2 MERSTRARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLAC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7678 LKAGGAFVP----LDPDHPASrheeIFEQTGAQVVVASAQYS--ARWTSSSCHVVTVSKALSSQLPAVVDST-------- 7743
Cdd:PRK08316    82 ARAGAVHVPvnfmLTGEELAY----ILDHSGARAFLVDPALAptAEAALALLPVDTLILSLVLGGREAPGGWldfadwae 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7744 -------NTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVA---TSCLGHGR---------------------------AF 7786
Cdd:PRK08316   158 agsvaepDVELADDDLAQILYTSGTESLPKGAMLTHRALIaeyVSCIVAGDmsaddiplhalplyhcaqldvflgpylYV 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7787 GITNLsrVLQFAS--YTFDACIAEIITTLLCGGCICVP----SDSDRRN--SLAKA---ISTMDVnwafltPSVARLLDP 7855
Cdd:PRK08316   238 GATNV--ILDAPDpeLILRTIEAERITSFFAPPTVWISllrhPDFDTRDlsSLRKGyygASIMPV------EVLKELRER 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7856 glIPSLKIlaiggeqsssadWNrwpgsvqkihVYGPTEccifCTGYTTKQGFE-----PSTIGTSVASV-SWVVDpENHN 7929
Cdd:PRK08316   310 --LPGLRF------------YN----------CYGQTE----IAPLATVLGPEehlrrPGSAGRPVLNVeTRVVD-DDGN 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7930 RLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVK 8009
Cdd:PRK08316   361 DVAP-GEVGEIVHRSPQLMLGYWDDPEKTAEAFRGG--W---------------FHSGDLGVMDEEGYITVVDRKKDMIK 422
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8010 VRGQRVELGEVEhhvrECLPEARQLA-VEVI-LPSGQKNHAMLAVFVQlgkgthiahleeKAGgedsmAQVvfltgTEEE 8087
Cdd:PRK08316   423 TGGENVASREVE----EALYTHPAVAeVAVIgLPDPKWIEAVTAVVVP------------KAG-----ATV-----TEDE 476
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 8088 L----AKRLPKHMVP-TVFF--ALlhfPMTTSGKADRKRLRE 8122
Cdd:PRK08316   477 LiahcRARLAGFKVPkRVIFvdEL---PRNPSGKILKRELRE 515
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
4567-5003 3.53e-15

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 83.03  E-value: 3.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLcFEKSMWT-VVAMLAVLKAGgafvpldpdhpasrhehifrqtgaqVVLAS 4645
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKVAI-FAETRAEwLITALGCWSQN-------------------------IPIVT 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4646 AqYATLwtslGRSVVIVSEASTSQLPVVTktadpSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSClgHGQAFGITDH 4725
Cdd:cd17639     60 V-YATL----GEDALIHSLNETECSAIFT-----DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGI--AGLGDRVPEL 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4726 T----RVLqfaSYTFDACIAEIITTLLCC--GC------------------------------ICVPS--DSDRRNNLAK 4767
Cdd:cd17639    128 LgpddRYL---AYLPLAHIFELAAENVCLyrGGtigygsprtltdkskrgckgdltefkptlmVGVPAiwDTIRKGVLAK 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4768 aINAMD-----------------VNWALLTPsvarMLDPCVVQSLKIL-------VLGGEQVNSADWDRWPKSI--QTIN 4821
Cdd:cd17639    205 -LNPMGglkrtlfwtayqsklkaLKEGPGTP----LLDELVFKKVRAAlggrlryMLSGGAPLSADTQEFLNIVlcPVIQ 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4822 AYGPTEcSICCTTYSGKQGFKSGTIGTSIVS-----VSWvvdPE-NHNRLAPLGSiGELLVEGPILARGYLNDMEKTEAA 4895
Cdd:cd17639    280 GYGLTE-TCAGGTVQDPGDLETGRVGPPLPCceiklVDW---EEgGYSTDKPPPR-GEILIRGPNVFKGYYKNPEKTKEA 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4896 FIDDpawllegygghsgrqgRLYKTGDLVRYDADGNLVYLGRKDSQVKLR-GQRVELGEVEHHVRECLT---------EA 4965
Cdd:cd17639    355 FDGD----------------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLvnnicvyadPD 418
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 4966 KQLAVEVIVPEgEGGYAMLAAFVQLGDDTYNTLVKEKA 5003
Cdd:cd17639    419 KSYPVAIVVPN-EKHLTKLAEKHGVINSEWEELCEDKK 455
PLN02246 PLN02246
4-coumarate--CoA ligase
3464-3976 3.70e-15

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 83.11  E-value: 3.70e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3464 HDLFTEQAKARPHAPaiCAWDGE----LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFV 3539
Cdd:PLN02246    26 HDYCFERLSEFSDRP--CLIDGAtgrvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3540 PLDPDHPASrheEIFEQ---TGAQVVVASAQYSARWTSSSCH----VVTV-------------SKALSSQLPAVvdstnt 3599
Cdd:PLN02246   104 TANPFYTPA---EIAKQakaSGAKLIITQSCYVDKLKGLAEDdgvtVVTIddppegclhfselTQADENELPEV------ 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3600 SVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL----GHGRAFGITNLSRVL----QFASYTFDaciaeiiTTLLCG- 3670
Cdd:PLN02246   175 EISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFHSDDVILcvlpMFHIYSLN-------SVLLCGl 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3671 --GCICVPSDSDRRNSLAKAISTMDVNWAFLTP----SVAR--LLDPGLIPSLKILAIG----GEQSSSADWNRWPGSV- 3737
Cdd:PLN02246   248 rvGAAILIMPKFEIGALLELIQRHKVTIAPFVPpivlAIAKspVVEKYDLSSIRMVLSGaaplGKELEDAFRAKLPNAVl 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3738 -QKihvYGPTE-------CCIFctgytTKQGFE--PSTIGTSV--ASVSwVVDPENHNRLaPLGSMGELLMEGPILARGY 3805
Cdd:PLN02246   328 gQG---YGMTEagpvlamCLAF-----AKEPFPvkSGSCGTVVrnAELK-IVDPETGASL-PRNQPGEICIRGPQIMKGY 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3806 LNDVDKTEAAfIDDPAWLlegypgHpgrqgrlykTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE-----Hhvre 3880
Cdd:PLN02246   398 LNDPEATANT-IDKDGWL------H---------TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEallisH---- 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3881 clPEARQLAVevilpSGQKDHA---MLAAFVQLEEGTQNAlldkeaggEDSM-----AQVVFLasveeelaKRLpeHMvp 3952
Cdd:PLN02246   458 --PSIADAAV-----VPMKDEVageVPVAFVVRSNGSEIT--------EDEIkqfvaKQVVFY--------KRI--HK-- 510
                          570       580
                   ....*....|....*....|....
gi 1820002560 3953 tVFFsLLHFPTTTSGKTDRKRLRE 3976
Cdd:PLN02246   511 -VFF-VDSIPKAPSGKILRKDLRA 532
PLN02574 PLN02574
4-coumarate--CoA ligase-like
4553-5057 3.81e-15

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 83.35  E-value: 3.81e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4553 ARPDTPA-ICAWDGE-LTYGELDTLSSKLASHLVQ-LGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 4629
Cdd:PLN02574    51 NHNGDTAlIDSSTGFsISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGE 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4630 HEHIFRQTGAQVVLASAQYATLWTSLGRSVVIVSEAST--SQLPVVTKTAD-----------PSVNPGNAAYAIFTSGST 4696
Cdd:PLN02574   131 IKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYDfdSKRIEFPKFYElikedfdfvpkPVIKQDDVAAIMYSSGTT 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4697 GIPKGVVLEHKAVVTSClghgqafgitdHTRVLQFAS-YTFDAC---------------IAEIITTLLCCGCICVPSDSD 4760
Cdd:PLN02574   211 GASKGVVLTHRNLIAMV-----------ELFVRFEASqYEYPGSdnvylaalpmfhiygLSLFVVGLLSLGSTIVVMRRF 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4761 RRNNLAKAINAMDVNWALLTPSVARML----DPCVVQSLKILVlggeQVNSADWDRWPKSIQT----------INAYGPT 4826
Cdd:PLN02574   280 DASDMVKVIDRFKVTHFPVVPPILMALtkkaKGVCGEVLKSLK----QVSCGAAPLSGKFIQDfvqtlphvdfIQGYGMT 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4827 ECSICCTT-YSGKQGFKSGTIGTSIVSV-SWVVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAFIDDpAWLl 4904
Cdd:PLN02574   356 ESTAVGTRgFNTEKLSKYSSVGLLAPNMqAKVVDWSTGCLLPP-GNCGELWIQGPGVMKGYLNNPKATQSTIDKD-GWL- 432
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4905 egygghsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVrecLTEAKQLAVEVI-VPEGEGGyAM 4983
Cdd:PLN02574   433 --------------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVL---ISHPEIIDAAVTaVPDKECG-EI 494
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 4984 LAAFVqlgddtyntlVKEKagGDSLTvQVVFLDRVEEELAkrvPEHMMLTTFFTlEAMPTTTSGKIDRKRLREI 5057
Cdd:PLN02574   495 PVAFV----------VRRQ--GSTLS-QEAVINYVAKQVA---PYKKVRKVVFV-QSIPKSPAGKILRRELKRS 551
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
4117-4506 4.31e-15

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 82.04  E-value: 4.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4117 PCSPLQEGLMSLTAKRAGD--YIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSE-------LGLLQVVVEER 4187
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGpaYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGgvprqeiLPPGPAPLEVR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4188 IqwtESESLEEYPREDKAV---SMGVGDRLARYALIKE---PYDGGKRWFVWTMHHALYDGWSLPRILHAVKQAYSGVVL 4261
Cdd:cd19539     83 D---LSDPDSDRERRLEELlreRESRGFDLDEEPPIRAvlgRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4262 ERQPSFNA-------FIQYLSQQDPEAAAA----YWQTALVDCKAALFPTLPPTVTQPVADTTVEYQCPPPSQSATditT 4330
Cdd:cd19539    160 GPAAPLPElrqqykeYAAWQREALAAPRAAelldFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAA---L 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4331 STLAR-----------AAWAIVTSRYTSSDDVVFGATVTGRNAPiaGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQ 4399
Cdd:cd19539    237 RELAKrarsslfmvllAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLIARVRK 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4400 QATDMIAHEQTGLQRIAK-----MSPGARHAcgFQTLLVVQPTDDVLGSDDMLGEWRSYSEMQDFTTYALMVQCVLVKDR 4474
Cdd:cd19539    315 ALVDAQRHQELPFQQLVAelpvdRDAGRHPL--VQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTG 392
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1820002560 4475 VGVTASFDARVIEQWVVEKMLRQFGFVMQQLA 4506
Cdd:cd19539    393 LRGSLGYATSLFDEETIQGFLADYLQVLRQLL 424
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
1955-2326 4.49e-15

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 83.03  E-value: 4.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVN--PEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP----LDPDhpASRHedIFRQTGAQ 2028
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPlydtLGPE--AIEY--ILNHAEIS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2029 VVVTSAqhsarwigtnhqvvTVSAGSLEQFSTL--VNPVDL-PAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHG 2105
Cdd:cd05927     82 IVFCDA--------------GVKVYSLEEFEKLgkKNKVPPpPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVF 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2106 QAFGVTNLLRAlQFT-------AYTFDVCIaeIITTLVHGGCI-----------------------CVP----------- 2144
Cdd:cd05927    148 KILEILNKINP-TDVyisylplAHIFERVV--EALFLYHGAKIgfysgdirlllddikalkptvfpGVPrvlnriydkif 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2145 ----SDSERRDNLAKAITDMQVNWgyLTSSVAR---LLDPCLVPSLKVLvLGGEqVNSTDWGKWPSSVQTI--------- 2208
Cdd:cd05927    225 nkvqAKGPLKRKLFNFALNYKLAE--LRSGVVRaspFWDKLVFNKIKQA-LGGN-VRLMLTGSAPLSPEVLeflrvalgc 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2209 ---NGYGPTECCVFCTgytgIQGFQSGNIGTSIASVSWV----VD-PE-------NHGRlaplgsiGELLVEGPILARGY 2273
Cdd:cd05927    301 pvlEGYGQTECTAGAT----LTLPGDTSVGHVGGPLPCAevklVDvPEmnydakdPNPR-------GEVCIRGPNVFSGY 369
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 2274 LNDVDKTQAAFIDDpAWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLGRK 2326
Cdd:cd05927    370 YKDPEKTAEALDED-GWL---------------HTGDIGEWLPNGTLKIIDRK 406
PRK05857 PRK05857
fatty acid--CoA ligase;
844-1365 4.81e-15

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 82.75  E-value: 4.81e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  844 ADMPPAV-DRCIhdlfaEQARARPDASAVCAWDG--ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAML 920
Cdd:PRK05857    10 PQLPSTVlDRVF-----EQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  921 AVLKAGGAFVPLDPGHPASRHEEiFKQIGAQVVLTSSQHAMLFASS---ERHQVTVSKVSTSQLPTvvNFAKSP------ 991
Cdd:PRK05857    85 ACAKLGAIAVMADGNLPIAAIER-FCQITDPAAALVAPGSKMASSAvpeALHSIPVIAVDIAAVTR--ESEHSLdaasla 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  992 VDPGNTA----YIIFTSGTTGIPKGVVLQHR---AVTTSCLGHGEAF-GYTDHARVLQFASYTFDACIAEIITTLLYGG- 1062
Cdd:PRK05857   162 GNADQGSedplAMIFTSGTTGEPKAVLLANRtffAVPDILQKEGLNWvTWVVGETTYSPLPATHIGGLWWILTCLMHGGl 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1063 CIcvpSESDRRNNLAKAISTMDVNCALLTPS-VARL-----LEPSAVPSLKRLVLQGEQVSFADWnRW--PGSVQTINGY 1134
Cdd:PRK05857   242 CV---TGGENTTSLLEILTTNAVATTCLVPTlLSKLvselkSANATVPSLRLVGYGGSRAIAADV-RFieATGVRTAQVY 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1135 GPTE--CS-VCCNTYSGK-QGFKSGIIGTSVASLS-WVVDAG----NHNRLAPLGSIGELLVEGPILARGYLNDIDKTEA 1205
Cdd:PRK05857   318 GLSEtgCTaLCLPTDDGSiVKIEAGAVGRPYPGVDvYLAATDgigpTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1206 AFIDdpAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhHVRECLPEARQLAVEVIl 1285
Cdd:PRK05857   398 VLID--GWV---------------NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGVSGVREAACYEI- 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1286 PSGQKEHALLAAFIqldkgnhnALFEEKASGEDSMAQVVfltgveEELAKRLPEHMV-PTILFTVKAMPITTSGKIDRKR 1364
Cdd:PRK05857   459 PDEEFGALVGLAVV--------ASAELDESAARALKHTI------AARFRRESEPMArPSTIVIVTDIPRTQSGKVMRAS 524

                   .
gi 1820002560 1365 L 1365
Cdd:PRK05857   525 L 525
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
7203-7575 5.24e-15

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 81.66  E-value: 5.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7203 YIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQV----------VVEEKIQWTESEA-LEEYLKEDK 7271
Cdd:cd19539     24 YNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEilppgpapleVRDLSDPDSDRERrLEELLRERE 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7272 AVSMGL-GDPLAHYALVKeaWGGKRWF-VWTIHHALYDGGSLPLI------LHAVKQVYSGAVL-ERQPSFNAFI----Q 7338
Cdd:cd19539    104 SRGFDLdEEPPIRAVLGR--FDPDDHVlVLVAHHTAFDAWSLDVFardlaaLYAARRKGPAAPLpELRQQYKEYAawqrE 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7339 YLGQQDLEATAAYWQTALSDCEAVLFP---PLPSTVTQPVADTTVEY------QCPPLSKATLDTTTSTLIrAAWAIVTS 7409
Cdd:cd19539    182 ALAAPRAAELLDFWRRRLRGAEPTALPtdrPRPAGFPYPGADLRFELdaelvaALRELAKRARSSLFMVLL-AAYCVLLR 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7410 CYTSSDDVVYGTTVTGRNAPiaGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQTGLQHIAKLgSGPR 7489
Cdd:cd19539    261 RYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQLVAE-LPVD 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7490 HACG----FQTLLVVQPVDDVLGSDDMLGEWRSYSKMQDFTTYALMVQFTLAAEGVQITASFDARVIEHWVLEKMLRQFS 7565
Cdd:cd19539    338 RDAGrhplVQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYL 417
                          410
                   ....*....|
gi 1820002560 7566 FIMQQLAEAS 7575
Cdd:cd19539    418 QVLRQLLANP 427
PRK07788 PRK07788
acyl-CoA synthetase; Validated
7617-8123 5.34e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 82.67  E-value: 5.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 7696
Cdd:PRK07788    59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7697 EEIFEQTGAQVVVASAQYSA----------RWTSSSCHVVTVSKALSS--QLPAVVDSTNTSVRP---ENAAYIIFTSGS 7761
Cdd:PRK07788   139 AEVAAREGVKALVYDDEFTDllsalppdlgRLRAWGGNPDDDEPSGSTdeTLDDLIAGSSTAPLPkppKPGGIVILTSGT 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7762 TGVPKGVVLEHravaTSCLGHGRAFgitnLSRV-------LQFASYTFDA---CIAEIITTLlcGGCICVPSDSDRRNSL 7831
Cdd:PRK07788   219 TGTPKGAPRPE----PSPLAPLAGL----LSRVpfragetTLLPAPMFHAtgwAHLTLAMAL--GSTVVLRRRFDPEATL 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7832 AkAISTMDVNWAFLTPS-VARLLDpgLIP---------SLKILAIGGEQSSsadwnrwPGSVQKIH---------VYGPT 7892
Cdd:PRK07788   289 E-DIAKHKATALVVVPVmLSRILD--LGPevlakydtsSLKIIFVSGSALS-------PELATRALeafgpvlynLYGST 358
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7893 ECCiFCTGYTTKQ-GFEPSTIGTSVASVSWVVDPENHNRLaPLGSMGEllmegpILARGYLndvdkteaafiddpawLLE 7971
Cdd:PRK07788   359 EVA-FATIATPEDlAEAPGTVGRPPKGVTVKILDENGNEV-PRGVVGR------IFVGNGF----------------PFE 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7972 GY--PGHPGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAV------EvilpSG 8043
Cdd:PRK07788   415 GYtdGRDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVE-DLLAGHPDVVEAAVigvddeE----FG 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8044 QKnhamLAVFVQLGKGTHIahleekagGEDSMAQVVfltgteeelAKRLPKHMVP-TVFFaLLHFPMTTSGKADRKRLRE 8122
Cdd:PRK07788   490 QR----LRAFVVKAPGAAL--------DEDAIKDYV---------RDNLARYKVPrDVVF-LDELPRNPTGKVLKRELRE 547

                   .
gi 1820002560 8123 I 8123
Cdd:PRK07788   548 M 548
PRK09274 PRK09274
peptide synthase; Provisional
7615-8015 5.50e-15

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 82.64  E-value: 5.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7615 EQARARPGAPAICAWDG----------ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAF 7684
Cdd:PRK09274    14 RAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7685 VPLDPDHPASRHEEIFEQTGAQVVV--ASAQYSARW----TSSSCHVVTVSKALS------SQLPAVVDSTNTSVR---P 7749
Cdd:PRK09274    94 VLVDPGMGIKNLKQCLAEAQPDAFIgiPKAHLARRLfgwgKPSVRRLVTVGGRLLwggttlATLLRDGAAAPFPMAdlaP 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7750 ENAAYIIFTSGSTGVPKGVVLEHR---AVATScLGHgrAFGITNLSRVLQ----FAsyTFDACiaeiittllCGGCICVP 7822
Cdd:PRK09274   174 DDMAAILFTSGSTGTPKGVVYTHGmfeAQIEA-LRE--DYGIEPGEIDLPtfplFA--LFGPA---------LGMTSVIP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7823 ---------SDSDRrnsLAKAISTMDVNWAFLTPSV-ARLLDPGL-----IPSLKILAIGGEQSSSADWNRW----PGSV 7883
Cdd:PRK09274   240 dmdptrpatVDPAK---LFAAIERYGVTNLFGSPALlERLGRYGEangikLPSLRRVISAGAPVPIAVIERFramlPPDA 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7884 QKIHVYGPTEC----------CIFCTGYTTKQGfEPSTIGTSVASVSWVV-----DPENH---NRLAPLGSMGELLMEGP 7945
Cdd:PRK09274   317 EILTPYGATEAlpissiesreILFATRAATDNG-AGICVGRPVDGVEVRIiaisdAPIPEwddALRLATGEIGEIVVAGP 395
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7946 ILARGYLNDVDKTEAAFIDDpawllegypghpGRQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRV 8015
Cdd:PRK09274   396 MVTRSYYNRPEATRLAKIPD------------GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
877-1366 6.02e-15

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 82.42  E-value: 6.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTS 956
Cdd:PRK08008    37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  957 SQHAMLFASSER------HQVTVSKVSTSQLPTVVNFAK------------SPVDPGNTAYIIFTSGTTGIPKGVVLQHr 1018
Cdd:PRK08008   117 AQFYPMYRQIQQedatplRHICLTRVALPADDGVSSFTQlkaqqpatlcyaPPLSTDDTAEILFTSGTTSRPKGVVITH- 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1019 avttsclghgeafgYTdharvLQFASYtfdaciaeiittllYGGCICVPSESDRRnnlakaISTM-----DVNCALLTP- 1092
Cdd:PRK08008   196 --------------YN-----LRFAGY--------------YSAWQCALRDDDVY------LTVMpafhiDCQCTAAMAa 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1093 -SVAR---LLEP-SA-----------------VPSLKR-LVLQ--------------------GEQVSFADWNRWpgSVQ 1129
Cdd:PRK08008   237 fSAGAtfvLLEKySArafwgqvckyratitecIPMMIRtLMVQppsandrqhclrevmfylnlSDQEKDAFEERF--GVR 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1130 TINGYGPTECSVccntysgkqgfksGIIGT---------SV--ASLSW---VVDAgnHNRLAPLGSIGELLVEG---PIL 1192
Cdd:PRK08008   315 LLTSYGMTETIV-------------GIIGDrpgdkrrwpSIgrPGFCYeaeIRDD--HNRPLPAGEIGEICIKGvpgKTI 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1193 ARGYLNDIDKTEAAFIDDpAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHhVREC 1272
Cdd:PRK08008   380 FKEYYLDPKATAKVLEAD-GWL---------------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELEN-IIAT 442
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1273 LPEARQLAVeVILPSGQKEHALlAAFIQLDKGnhnalfeEKASGEDsmaqvvFLTGVEEELAKrlpeHMVPTILFTVKAM 1352
Cdd:PRK08008   443 HPKIQDIVV-VGIKDSIRDEAI-KAFVVLNEG-------ETLSEEE------FFAFCEQNMAK----FKVPSYLEIRKDL 503
                          570
                   ....*....|....
gi 1820002560 1353 PITTSGKIDRKRLQ 1366
Cdd:PRK08008   504 PRNCSGKIIKKNLK 517
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3023-3322 6.62e-15

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 81.38  E-value: 6.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3023 FPCTPMQEgiltsqgkdpdAYWV------------CFIYevipnQE---TSISLARLQQAWKGVVHQHSLLRTLLVDNvp 3087
Cdd:cd19535      2 FPLTDVQY-----------AYWIgrqddqelggvgCHAY-----LEfdgEDLDPDRLERAWNKLIARHPMLRAVFLDD-- 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3088 gstGTTNVVLKDPQPSISVF----SSEGTATIELFRSRYNPAAQR---SIGQLqHHLSICQLNNGKVYLCLDINHAIIDA 3160
Cdd:cd19535     64 ---GTQQILPEVPWYGITVHdlrgLSEEEAEAALEELRERLSHRVldvERGPL-FDIRLSLLPEGRTRLHLSIDLLVADA 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3161 HSRGILMHDLQEAY---DANLNPQSTSFRDfasYIKQQSQEEAGR------YWAEYLDGvepcfFPslgdsgGANTIPRT 3231
Cdd:cd19535    140 LSLQILLRELAALYedpGEPLPPLELSFRD---YLLAEQALRETAyeraraYWQERLPT-----LP------PAPQLPLA 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3232 VEVPSIDSSAVHMFCKI-----WE----------VTPATIIQTAWALVLSRYTNSTN-----PCFgnlssgrD-LPIH-N 3289
Cdd:cd19535    206 KDPEEIKEPRFTRREHRlsaeqWQrlkerarqhgVTPSMVLLTAYAEVLARWSGQPRfllnlTLF-------NrLPLHpD 278
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1820002560 3290 VNSIFGPLISILPCRIHLHKQLTVLEALKTVQE 3322
Cdd:cd19535    279 VNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQ 311
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
3456-3984 7.41e-15

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 82.11  E-value: 7.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3456 PPAiERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAG 3535
Cdd:PRK06155    17 PPS-ERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLG 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3536 GAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSAR--------------WTSSSCHVVTVSKALS-SQLPAVVDS-TNT 3599
Cdd:PRK06155    96 AIAVPINTALRGPQLEHILRNSGARLLVVEAALLAAleaadpgdlplpavWLLDAPASVSVPAGWStAPLPPLDAPaPAA 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3600 SVRPENAAYIIFTSGSTGVPKGVVLEHR------AVATSCLGHGRA---------FGITNLSRVLQ-------------F 3651
Cdd:PRK06155   176 AVQPGDTAAILYTSGTTGPSKGVCCPHAqfywwgRNSAEDLEIGADdvlyttlplFHTNALNAFFQallagatyvleprF 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3652 -ASYTFDACIAEIIT-TLLCGGCICV-----PSDSDRRNSLAKAistmdvnwafltpsvarlldpglipslkiLAIGGEQ 3724
Cdd:PRK06155   256 sASGFWPAVRRHGATvTYLLGAMVSIllsqpARESDRAHRVRVA-----------------------------LGPGVPA 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3725 SSSADWNRWPGsVQKIHVYGPTECCIFCtgYTTKQGFEPSTIGTSVASV-SWVVDpeNHNRLAPLGSMGELLM---EGPI 3800
Cdd:PRK06155   307 ALHAAFRERFG-VDLLDGYGSTETNFVI--AVTHGSQRPGSMGRLAPGFeARVVD--EHDQELPDGEPGELLLradEPFA 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3801 LARGYLNDVDKTEAAFIDdpAWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGR-KDSqVKVRGQRVELGEVEHHVR 3879
Cdd:PRK06155   382 FATGYFGMPEKTVEAWRN--LW---------------FHTGDRVVRDADGWFRFVDRiKDA-IRRRGENISSFEVEQVLL 443
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3880 EcLPEARQLAVeVILPSGQKDHAMLAAFVqLEEGTQnalLDkeaggedsmaqvvFLASVEEELAkRLPEHMVPTVFFSLL 3959
Cdd:PRK06155   444 S-HPAVAAAAV-FPVPSELGEDEVMAAVV-LRDGTA---LE-------------PVALVRHCEP-RLAYFAVPRYVEFVA 503
                          570       580
                   ....*....|....*....|....*
gi 1820002560 3960 HFPTTTSGKTDRKRLREIGasFTAQ 3984
Cdd:PRK06155   504 ALPKTENGKVQKFVLREQG--VTAD 526
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
850-1373 7.86e-15

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 81.96  E-value: 7.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  850 VDRCIHDLFAEQARarPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKRED--VVPLCFEKSMWtvVAMLAVLKAGg 927
Cdd:PRK10946    23 QDLPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDtaLVQLGNVAEFY--ITFFALLKLG- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  928 aFVPLDPGHPASRHE--EIFKQIGAQVVLTSSQHAmLFA------------SSERHQVTVSKVSTSQLPTVV-----NFA 988
Cdd:PRK10946    98 -VAPVNALFSHQRSElnAYASQIEPALLIADRQHA-LFSdddflntlvaehSSLRVVLLLNDDGEHSLDDAInhpaeDFT 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  989 KSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQF--ASYTFDACIAEIITTLLYGGCI-- 1064
Cdd:PRK10946   176 ATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCAlpAAHNYPMSSPGALGVFLAGGTVvl 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1065 --------CVPSESDRRNNLAkaistmdvncALLTPSVARLLEPSAVP-------SLKRLVLQGEQVSFADWNRWPGSV- 1128
Cdd:PRK10946   256 apdpsatlCFPLIEKHQVNVT----------ALVPPAVSLWLQAIAEGgsraqlaSLKLLQVGGARLSETLARRIPAELg 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1129 -QTINGYGPTECSVCcntYSGKQGFKSGIIGTSVASLS-----WVVDAgNHNRLAPlGSIGELLVEGPILARGYLNDIDK 1202
Cdd:PRK10946   326 cQLQQVFGMAEGLVN---YTRLDDSDERIFTTQGRPMSpddevWVADA-DGNPLPQ-GEVGRLMTRGPYTFRGYYKSPQH 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1203 TEAAFiDDpawllEGYeghagrrgrlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVreclpearqLAVE 1282
Cdd:PRK10946   401 NASAF-DA-----NGF----------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLL---------LRHP 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1283 VILpsgqkeHALLAAfiqldkgnhnalFEEKASGEDSMAQVVFLTGVEE-ELAKRLPEHMV-----PTILFTVKAMPITT 1356
Cdd:PRK10946   456 AVI------HAALVS------------MEDELMGEKSCAFLVVKEPLKAvQLRRFLREQGIaefklPDRVECVDSLPLTA 517
                          570
                   ....*....|....*..
gi 1820002560 1357 SGKIDRKRLQDIGASFT 1373
Cdd:PRK10946   518 VGKVDKKQLRQWLASRA 534
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
2-283 8.35e-15

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 81.61  E-value: 8.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSVARLL------EPSHIPSLRILVMGGEQVNSADWDRWPS----SVQTIngYGPTECCIVCTGYTSEQDFT 71
Cdd:cd05920    229 GVTVTALVPALVSLWldaaasRRADLSSLRLLQVGGARLSPALARRVPPvlgcTLQQV--FGMAEGLLNYTRLDDPDEVI 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   72 TGTIGTSIASV--SWVVDPkdHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNpawlleghgGYagrqgrlYKT 149
Cdd:cd05920    307 IHTQGRPMSPDdeIRVVDE--EGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPD---------GF-------YRT 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  150 GDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVeVVLP---LGQKnhatLAAFIQLDKGTHNA 226
Cdd:cd05920    369 GDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR-HPAVHDAAV-VAMPdelLGER----SCAFVVLRDPPPSA 442
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  227 LlkekvggddSIARVVFLAGVEeelAKRLPKHMVPtvffaLLHFPTTTSGKTDRKRL 283
Cdd:cd05920    443 A---------QLRRFLRERGLA---AYKLPDRIEF-----VDSLPLTAVGKIDKKAL 482
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
4136-4439 8.47e-15

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 81.25  E-value: 8.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4136 YIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSElGLLQVVVEE---RIQWTESESLEEYPREDKAvsmgvgD 4212
Cdd:cd19531     24 YNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDG-EPVQVILPPlplPLPVVDLSGLPEAEREAEA------Q 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4213 RLARyALIKEPYD--------------GGKRW-FVWTMHHALYDGWSLPRILHAVKQAYSGVVLERQPSFNAF-IQY--- 4273
Cdd:cd19531     97 RLAR-EEARRPFDlargpllratllrlGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPPLpIQYady 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4274 -------LSQQDPEAAAAYWQTALVDCKAALfpTLP-----PTVTQPVADtTVEYQCPPpsqsatDITTS--TLAR---- 4335
Cdd:cd19531    176 avwqrewLQGEVLERQLAYWREQLAGAPPVL--ELPtdrprPAVQSFRGA-RVRFTLPA------ELTAAlrALARrega 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4336 -------AAWAIVTSRYTSSDDVVFGATVTGRNAPiaGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQATDMIAH- 4407
Cdd:cd19531    247 tlfmtllAAFQVLLHRYSGQDDIVVGTPVAGRNRA--ELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAYAHq 324
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1820002560 4408 --------EQTGLQRIAKMSPgarhacGFQTLLVVQPTDD 4439
Cdd:cd19531    325 dlpfeklvEALQPERDLSRSP------LFQVMFVLQNAPA 358
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
7639-8121 8.49e-15

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 82.15  E-value: 8.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7639 DVLSsnLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQ----- 7713
Cdd:PLN02860    41 GVLS--LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETcsswy 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7714 --------YSARW-----TSSSCHVVTVSKALSS----QLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVA 7776
Cdd:PLN02860   119 eelqndrlPSLMWqvfleSPSSSVFIFLNSFLTTemlkQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALI 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7777 TSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGC------------------------ICVPSdsdrrnSLA 7832
Cdd:PLN02860   199 VQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAChvllpkfdakaalqaikqhnvtsmITVPA------MMA 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7833 KAIST--MDVNWAfLTPSVARLLDPGLIPSLKILAIGGEQSSSAdwnrwpgsvQKIHVYGPTECC---IFCTGYTTKQGF 7907
Cdd:PLN02860   273 DLISLtrKSMTWK-VFPSVRKILNGGGSLSSRLLPDAKKLFPNA---------KLFSAYGMTEACsslTFMTLHDPTLES 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7908 EPSTIGTSVASVSWVVD-----------PENHNRLAPLGS--MGELLMEGPILARGYLnDVDKTEAAFIDDPAWLlegyp 7974
Cdd:PLN02860   343 PKQTLQTVNQTKSSSVHqpqgvcvgkpaPHVELKIGLDESsrVGRILTRGPHVMLGYW-GQNSETASVLSNDGWL----- 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7975 ghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE----HH------VRECLPEARQLavevilpsgq 8044
Cdd:PLN02860   417 ----------DTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEavlsQHpgvasvVVVGVPDSRLT---------- 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8045 knhAMLAVFVQLGKGTHIAHLE-EKAGGEdsmaqvvfLTGTEEEL-----AKRLPKHMVPTVFFALLH-FPMTTSGKADR 8117
Cdd:PLN02860   477 ---EMVVACVRLRDGWIWSDNEkENAKKN--------LTLSSETLrhhcrEKNLSRFKIPKLFVQWRKpFPLTTTGKIRR 545

                   ....
gi 1820002560 8118 KRLR 8121
Cdd:PLN02860   546 DEVR 549
PLN02574 PLN02574
4-coumarate--CoA ligase-like
7619-8021 8.97e-15

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 81.81  E-value: 8.97e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7619 ARPGAPA-ICAWDGE-LTYGELDVLSSNLAGHLVQ-LGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPdhpASR 7695
Cdd:PLN02574    51 NHNGDTAlIDSSTGFsISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP---SSS 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7696 HEEIFEQ---TGAQVVVASAQYSARWTSSSCHVVTVSKALSSQLPAVVDSTNTS-------------VRPENAAYIIFTS 7759
Cdd:PLN02574   128 LGEIKKRvvdCSVGLAFTSPENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFYElikedfdfvpkpvIKQDDVAAIMYSS 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7760 GSTGVPKGVVLEHRAVatsclghgrafgITNLSRVLQF--ASYTFDAC---------------IAEIITTLLCGGCICVP 7822
Cdd:PLN02574   208 GTTGASKGVVLTHRNL------------IAMVELFVRFeaSQYEYPGSdnvylaalpmfhiygLSLFVVGLLSLGSTIVV 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7823 SDSDRRNSLAKAISTMDVNWAFLTPSV-------ARLLDPGLIPSLKILAIGGEQSSSA---DWNRWPGSVQKIHVYGPT 7892
Cdd:PLN02574   276 MRRFDASDMVKVIDRFKVTHFPVVPPIlmaltkkAKGVCGEVLKSLKQVSCGAAPLSGKfiqDFVQTLPHVDFIQGYGMT 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7893 ECCIFCT-GYTTKQGFEPSTIGTSVASV-SWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpAWLl 7970
Cdd:PLN02574   356 ESTAVGTrGFNTEKLSKYSSVGLLAPNMqAKVVDWSTGCLLPP-GNCGELWIQGPGVMKGYLNNPKATQSTIDKD-GWL- 432
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 7971 egypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 8021
Cdd:PLN02574   433 --------------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLE 469
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
6851-7037 9.16e-15

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 80.02  E-value: 9.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFvndpawlveghgkhpgrRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:cd04433    190 PPGEIGELVVRGPSVMKGYWNNPEATAAVD-----------------EDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGG 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6931 QRVELGEIENRLRECmPRATQMAVeVISPAGAAEQAktmVVAFLQLNDEARDAllggnvpnddnlsaqvvfPAKVDEKLS 7010
Cdd:cd04433    253 ENVYPAEVEAVLLGH-PGVAEAAV-VGVPDPEWGER---VVAVVVLRPGADLD------------------AEELRAHVR 309
                          170       180
                   ....*....|....*....|....*..
gi 1820002560 7011 NLLPSYMMPEVYFAVPQLPMMISGKTD 7037
Cdd:cd04433    310 ERLAPYKVPRRVVFVDALPRTASGKID 336
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
445-820 9.51e-15

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 80.89  E-value: 9.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  445 YIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQV----------VVEEKMQWTESES-LEEYLNEDK 513
Cdd:cd19539     24 YNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEilppgpapleVRDLSDPDSDRERrLEELLRERE 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  514 AASMGL-GDRLARYALIKESCGGKrWFVWTIHHALYDGWSLPLVLDAVKQVYSGAALERQP-------SFNTFIQYVSQQ 585
Cdd:cd19539    104 SRGFDLdEEPPIRAVLGRFDPDDH-VLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAAplpelrqQYKEYAAWQREA 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  586 D----VKAAAAYWQTALADCEAV-LFPPLPSTVTQPvADTTVkYQCPPSPEVTS-----SNITTSTL---IRAAWAIIAS 652
Cdd:cd19539    183 LaaprAAELLDFWRRRLRGAEPTaLPTDRPRPAGFP-YPGAD-LRFELDAELVAalrelAKRARSSLfmvLLAAYCVLLR 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  653 RYTSSEDIVFGTTVTGRNAPitGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTGLQRIMKMGPgPQ 732
Cdd:cd19539    261 RYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQLVAELP-VD 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  733 HACG----FQTLLVVhpTDDVLSSDDTLGEWHSRSDSELQYFTTYALTIQCTLAVEGVQITASFDARVVEHWVVEKMLGQ 808
Cdd:cd19539    338 RDAGrhplVQIVFQV--TNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQGFLAD 415
                          410
                   ....*....|..
gi 1820002560  809 FSFVMQQLAEAG 820
Cdd:cd19539    416 YLQVLRQLLANP 427
PRK08316 PRK08316
acyl-CoA synthetase; Validated
3452-3976 1.12e-14

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 81.52  E-value: 1.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3452 NADVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAV 3531
Cdd:PRK08316     2 MERSTRARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLAC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3532 LKAGGAFVP----LDPDHPASrheeIFEQTGAQVVVASAQYS--ARWTSSSCHVVTVSKALSSQLPAVVDST-------- 3597
Cdd:PRK08316    82 ARAGAVHVPvnfmLTGEELAY----ILDHSGARAFLVDPALAptAEAALALLPVDTLILSLVLGGREAPGGWldfadwae 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3598 -------NTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVA---TSCLGHGR---------------------------AF 3640
Cdd:PRK08316   158 agsvaepDVELADDDLAQILYTSGTESLPKGAMLTHRALIaeyVSCIVAGDmsaddiplhalplyhcaqldvflgpylYV 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3641 GITNLsrVLQFAS--YTFDACIAEIITTLLCGGCICVP----SDSDRRN--SLAKA---ISTMDVnwafltPSVARLLDP 3709
Cdd:PRK08316   238 GATNV--ILDAPDpeLILRTIEAERITSFFAPPTVWISllrhPDFDTRDlsSLRKGyygASIMPV------EVLKELRER 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3710 glIPSLKIlaiggeqsssadWNrwpgsvqkihVYGPTEccifCTGYTTKQGFE-----PSTIGTSVASV-SWVVDpENHN 3783
Cdd:PRK08316   310 --LPGLRF------------YN----------CYGQTE----IAPLATVLGPEehlrrPGSAGRPVLNVeTRVVD-DDGN 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3784 RLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVK 3863
Cdd:PRK08316   361 DVAP-GEVGEIVHRSPQLMLGYWDDPEKTAEAFRGG--W---------------FHSGDLGVMDEEGYITVVDRKKDMIK 422
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3864 VRGQRVELGEVEhhvrECLPEARQLA-VEVI-LPSGQKDHAmLAAFVQLEEGtqnALLDKEAggedsmaqvvflasVEEE 3941
Cdd:PRK08316   423 TGGENVASREVE----EALYTHPAVAeVAVIgLPDPKWIEA-VTAVVVPKAG---ATVTEDE--------------LIAH 480
                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1820002560 3942 LAKRLPEHMVP-TVFF--SLlhfPTTTSGKTDRKRLRE 3976
Cdd:PRK08316   481 CRARLAGFKVPkRVIFvdEL---PRNPSGKILKRELRE 515
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
3486-3941 1.18e-14

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 81.36  E-value: 1.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3486 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVAS 3565
Cdd:cd05932      6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3566 A--QYSARWTSSSCHVVTVS-------------KALSSQLPAVVDSTNTSvrPENAAYIIFTSGSTGVPKGVVLEHRAVA 3630
Cdd:cd05932     86 KldDWKAMAPGVPEGLISISlpppsaancqyqwDDLIAQHPPLEERPTRF--PEQLATLIYTSGTTGQPKGVMLTFGSFA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3631 TSCLGHGRAFGITNLSRVLqfaSYTFDACIAEiiTTLLCGGCICvpsdSDRRNSLAKAISTM--DVNWAFLTP--SVAR- 3705
Cdd:cd05932    164 WAAQAGIEHIGTEENDRML---SYLPLAHVTE--RVFVEGGSLY----GGVLVAFAESLDTFveDVQRARPTLffSVPRl 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3706 -------------------LLDPGLIPSL---KIL-AIGGEQ-----SSSA-------DWNRWPGsVQKIHVYGPTECC- 3749
Cdd:cd05932    235 wtkfqqgvqdkipqqklnlLLKIPVVNSLvkrKVLkGLGLDQcrlagCGSApvppallEWYRSLG-LNILEAYGMTENFa 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3750 --IFCTGYTTKQGfepsTIGTSVASVSWVVDPEnhnrlaplgsmGELLMEGPILARGYLNDVDKTEAAFIDDpAWLlegy 3827
Cdd:cd05932    314 ysHLNYPGRDKIG----TVGNAGPGVEVRISED-----------GEILVRSPALMMGYYKDPEATAEAFTAD-GFL---- 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3828 pghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKV-RGQRVELGEVEH------HVREC------LPEARQLAVeviL 3894
Cdd:cd05932    374 -----------RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENklaehdRVEMVcvigsgLPAPLALVV---L 439
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 3895 PSGQKDHAMLAAFVQLEEGTQnALLDKEAGGEDSMAQVVFLASVEEE 3941
Cdd:cd05932    440 SEEARLRADAFARAELEASLR-AHLARVNSTLDSHEQLAGIVVVKDP 485
PRK07798 PRK07798
acyl-CoA synthetase; Validated
4545-4942 1.20e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 81.47  E-value: 1.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4545 DQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 4624
Cdd:PRK07798     7 DLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4625 HPASRHEHIFRQTGAQVVLASAQY----ATLWTSLG--RSVVIVSEASTSQLP---------VVTKTADPSVNPGNA--A 4687
Cdd:PRK07798    87 YVEDELRYLLDDSDAVALVYEREFaprvAEVLPRLPklRTLVVVEDGSGNDLLpgavdyedaLAAGSPERDFGERSPddL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4688 YAIFTSGSTGIPKGVVLEHKAVVTSCLGhGQAFG----ITDHTRVLQFA-----SYTFDAC-------IAEIITTLLCCG 4751
Cdd:PRK07798   167 YLLYTGGTTGMPKGVMWRQEDIFRVLLG-GRDFAtgepIEDEEELAKRAaagpgMRRFPAPplmhgagQWAAFAALFSGQ 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4752 CICVPS----DSDRrnnLAKAINAMDVNWALLT-PSVAR-MLD------PCVVQSLKILVLGGEQVNSADWDRWPKSIQT 4819
Cdd:PRK07798   246 TVVLLPdvrfDADE---VWRTIEREKVNVITIVgDAMARpLLDaleargPYDLSSLFAIASGGALFSPSVKEALLELLPN 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4820 I---NAYGPTECSICCTTYSGKQGFKSG----TIGTSIVsvswVVDpENHNRLAPlGS--IGELLVEGPIlARGYLNDME 4890
Cdd:PRK07798   323 VvltDSIGSSETGFGGSGTVAKGAVHTGgprfTIGPRTV----VLD-EDGNPVEP-GSgeIGWIARRGHI-PLGYYKDPE 395
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 4891 KTEAAF--IDDPAWLLegygghsgrqgrlykTGDLVRYDADGNLVYLGRkDSQV 4942
Cdd:PRK07798   396 KTAETFptIDGVRYAI---------------PGDRARVEADGTITLLGR-GSVC 433
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2071-2443 1.23e-14

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 79.63  E-value: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2071 PENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLR-ALQFTAYTFDVCIAEIITTLVHGGCICVPSDS-E 2148
Cdd:cd05917      1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRlCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSfD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2149 RRDNLAkAITDMQ--VNWGYLTSSVARLLDPCL----VPSLKVLVLGG------------EQVNSTDWgkwpssvqTInG 2210
Cdd:cd05917     81 PLAVLE-AIEKEKctALHGVPTMFIAELEHPDFdkfdLSSLRTGIMAGapcppelmkrviEVMNMKDV--------TI-A 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2211 YGPTECCVFCTgytgiQGFQSGNIGTSIASV--------SWVVDPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQA 2282
Cdd:cd05917    151 YGMTETSPVST-----QTRTDDSIEKRVNTVgrimphteAKIVDPEG-GIVPPVGVPGELCIRGYSVMKGYWNDPEKTAE 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2283 AfIDDPAWllegypghegrqgrlYKTGDLVRYSSDGNLVCLGR-KDsqVKVRG-QRVELGEVEHHMRKcLPEANQLAVEV 2360
Cdd:cd05917    225 A-IDGDGW---------------LHTGDLAVMDEDGYCRIVGRiKD--MIIRGgENIYPREIEEFLHT-HPKVSDVQVVG 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2361 VPpsgerDHAM---LAAFIRLDDETRNSpliikyAEDnstaqivfltgIEEELSERLPQHMVPTVFFALVHFPTTTSGKT 2437
Cdd:cd05917    286 VP-----DERYgeeVCAWIRLKEGAELT------EED-----------IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKI 343

                   ....*.
gi 1820002560 2438 DRKRLR 2443
Cdd:cd05917    344 QKFKLR 349
PRK07798 PRK07798
acyl-CoA synthetase; Validated
5626-6076 1.28e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 81.47  E-value: 1.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 5705
Cdd:PRK07798     7 DLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5706 HPASRHEDTFRHTGAQVVVTSAQHSARwigtnhqVVTVSAgSLGQLSTLV-------NPVGLPAIP-ENAV--------- 5768
Cdd:PRK07798    87 YVEDELRYLLDDSDAVALVYEREFAPR-------VAEVLP-RLPKLRTLVvvedgsgNDLLPGAVDyEDALaagsperdf 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5769 --------YIMFTSGSTGIPKGVVLEHRAVVTSCWGrGRAFG----ITNLSRVLQFA-----SYTFDAC-------MDEI 5824
Cdd:PRK07798   159 gerspddlYLLYTGGTTGMPKGVMWRQEDIFRVLLG-GRDFAtgepIEDEEELAKRAaagpgMRRFPAPplmhgagQWAA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5825 ITTLMYGGCICVPS----DSDR------RN---------D-----LVKAISTM---DVSC--------ALLTPSV-ARLL 5868
Cdd:PRK07798   238 FAALFSGQTVVLLPdvrfDADEvwrtieREkvnvitivgDamarpLLDALEARgpyDLSSlfaiasggALFSPSVkEALL 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5869 EpsSVPTLqMLvlqgeqvsfadwnrwpasvqtINGYGPTEcsiccntySGKQGF---KSGIIGTSVASV----SWVVDPE 5941
Cdd:PRK07798   318 E--LLPNV-VL---------------------TDSIGSSE--------TGFGGSgtvAKGAVHTGGPRFtigpRTVVLDE 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5942 NHDRLAPlGS--IGELLVEGPIlARGYLNDIQKTAAVFiddpawllegypghPGRQGRLYK-TGDLVRYDANGNLVCLGR 6018
Cdd:PRK07798   366 DGNPVEP-GSgeIGWIARRGHI-PLGYYKDPEKTAETF--------------PTIDGVRYAiPGDRARVEADGTITLLGR 429
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6019 kDSQ-VKLRGQRVELGEVEhhvrECLpeARQLAVE----VILPS---GQKdhamLAAFVQLEEGTQ 6076
Cdd:PRK07798   430 -GSVcINTGGEKVFPEEVE----EAL--KAHPDVAdalvVGVPDerwGQE----VVAVVQLREGAR 484
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
3471-3628 1.32e-14

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 80.69  E-value: 1.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 3550
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 3551 EEIFEqtgaqvvvasaQYSARWTSSSCHVVTVSKALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRA 3628
Cdd:PRK09029    93 EELLP-----------SLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQA 159
PRK08316 PRK08316
acyl-CoA synthetase; Validated
854-1367 1.39e-14

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 81.13  E-value: 1.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 933
Cdd:PRK08316    13 IGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVN 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 PGHPASRHEEIFKQIGAQVVLTSS------QHAMlfASSERHQVTVSKVSTSQLP-----TVVNFAKS--------PVDP 994
Cdd:PRK08316    93 FMLTGEELAYILDHSGARAFLVDPalaptaEAAL--ALLPVDTLILSLVLGGREApggwlDFADWAEAgsvaepdvELAD 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  995 GNTAYIIFTSGTTGIPKGVVLQHRAVT---TSCLGHGEaFGYTD---HARVLqFASYTFDAciaeIITTLLYGGCICVPS 1068
Cdd:PRK08316   171 DDLAQILYTSGTESLPKGAMLTHRALIaeyVSCIVAGD-MSADDiplHALPL-YHCAQLDV----FLGPYLYVGATNVIL 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1069 ESDRRNNLAKAISTMDVNCALLTPSV--ARLLEP-----------------SA--VPSLKRLVlqgeqvsfadwNRWPGs 1127
Cdd:PRK08316   245 DAPDPELILRTIEAERITSFFAPPTVwiSLLRHPdfdtrdlsslrkgyygaSImpVEVLKELR-----------ERLPG- 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1128 VQTINGYGPTECSVCCNTYSGK-QGFKSGIIGTSVASL-SWVVDAgNHNRLAPlGSIGELLVEGPILARGYLNDIDKTEA 1205
Cdd:PRK08316   313 LRFYNCYGQTEIAPLATVLGPEeHLRRPGSAGRPVLNVeTRVVDD-DGNDVAP-GEVGEIVHRSPQLMLGYWDDPEKTAE 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1206 AFiddpawllegyeghagrRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhhvrECLPEARQLA-VEVI 1284
Cdd:PRK08316   391 AF-----------------RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVE----EALYTHPAVAeVAVI 449
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1285 -LPSGQKEHAlLAAFIQLDKGnhnalfeEKASGEDSMAQVvfltgveeelAKRLPEHMVPTILFTVKAMPITTSGKIDRK 1363
Cdd:PRK08316   450 gLPDPKWIEA-VTAVVVPKAG-------ATVTEDELIAHC----------RARLAGFKVPKRVIFVDELPRNPSGKILKR 511

                   ....
gi 1820002560 1364 RLQD 1367
Cdd:PRK08316   512 ELRE 515
PLN02246 PLN02246
4-coumarate--CoA ligase
7610-8122 1.46e-14

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 81.18  E-value: 1.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7610 HDLFAEQARARPGAPaiCAWDGE----LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFV 7685
Cdd:PLN02246    26 HDYCFERLSEFSDRP--CLIDGAtgrvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7686 PLDPDHPASrheEIFEQ---TGAQVVVASAQYSARWTSSSCH----VVTV-------------SKALSSQLPAVvdstnt 7745
Cdd:PLN02246   104 TANPFYTPA---EIAKQakaSGAKLIITQSCYVDKLKGLAEDdgvtVVTIddppegclhfselTQADENELPEV------ 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7746 SVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCL----GHGRAFGITNLSRVL----QFASYTFDaciaeiiTTLLCG- 7816
Cdd:PLN02246   175 EISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFHSDDVILcvlpMFHIYSLN-------SVLLCGl 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7817 --GCICVPSDSDRRNSLAKAISTMDVNWAFLTP----SVAR--LLDPGLIPSLKILAIG----GEQSSSADWNRWPGSV- 7883
Cdd:PLN02246   248 rvGAAILIMPKFEIGALLELIQRHKVTIAPFVPpivlAIAKspVVEKYDLSSIRMVLSGaaplGKELEDAFRAKLPNAVl 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7884 -QKihvYGPTE-------CCIFctgytTKQGFE--PSTIGTSV--ASVSwVVDPENHNRLaPLGSMGELLMEGPILARGY 7951
Cdd:PLN02246   328 gQG---YGMTEagpvlamCLAF-----AKEPFPvkSGSCGTVVrnAELK-IVDPETGASL-PRNQPGEICIRGPQIMKGY 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7952 LNDVDKTEAAfIDDPAWLlegypgHpgrqgrlykTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE-----Hhvre 8026
Cdd:PLN02246   398 LNDPEATANT-IDKDGWL------H---------TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEallisH---- 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8027 clPEARQLAVevilpSGQKNHAMLAV---FVQLGKGTHIAHLEEKaggeDSMA-QVVFLtgteeelaKRLPKhmvptVFF 8102
Cdd:PLN02246   458 --PSIADAAV-----VPMKDEVAGEVpvaFVVRSNGSEITEDEIK----QFVAkQVVFY--------KRIHK-----VFF 513
                          570       580
                   ....*....|....*....|
gi 1820002560 8103 AlLHFPMTTSGKADRKRLRE 8122
Cdd:PLN02246   514 V-DSIPKAPSGKILRKDLRA 532
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
315-375 1.48e-14

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 71.83  E-value: 1.48e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560  315 RTMQQLWARVLGIEPDSIGLDDSFFRLGGDSIAAIKLVGEARRT-GLQPSVADIFRHPTLAA 375
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
7616-8123 1.49e-14

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 80.78  E-value: 1.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7616 QARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpdHPASR 7695
Cdd:PRK03640    11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN--TRLSR 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7696 HEEIF--EQTGAQVVVASAQYSARwtssschVVTVSKALSSQLPAVVDSTNTSVRP---ENAAYIIFTSGSTGVPKGVVL 7770
Cdd:PRK03640    89 EELLWqlDDAEVKCLITDDDFEAK-------LIPGISVKFAELMNGPKEEAEIQEEfdlDEVATIMYTSGTTGKPKGVIQ 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7771 ---EHRAVATSC---LG-HGR--------AFGITNLSRVLQFASY--------TFDaciAEIITTLLCGGcicvpsdsdr 7827
Cdd:PRK03640   162 tygNHWWSAVGSalnLGlTEDdcwlaavpIFHISGLSILMRSVIYgmrvvlveKFD---AEKINKLLQTG---------- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7828 rnslakAISTMDVNWAFLTPSVARLLDPGLIPSLKILAIGG--------EQsssadwnrwpgSVQK----IHVYGPTECC 7895
Cdd:PRK03640   229 ------GVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGgpapkpllEQ-----------CKEKgipvYQSYGMTETA 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7896 --IfCTgyttkqgFEPSTIGTSVASV-----SWVVDPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdpAW 7968
Cdd:PRK03640   292 sqI-VT-------LSPEDALTKLGSAgkplfPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD--GW 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7969 LlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHhvreclpearqlaveVILpsgqkNHA 8048
Cdd:PRK03640   362 F---------------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEE---------------VLL-----SHP 406
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8049 MLAVFVQLGKgthiahlEEKAGGEDSMAQVVFLTG-TEEELA----KRLPKHMVPTVFFALLHFPMTTSGKADRKRLREI 8123
Cdd:PRK03640   407 GVAEAGVVGV-------PDDKWGQVPVAFVVKSGEvTEEELRhfceEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7749-8121 1.71e-14

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 79.24  E-value: 1.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7749 PENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRV-LQFASYTFDACIAEIITTLLCGGCICVPSDS-D 7826
Cdd:cd05917      1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcIPVPLFHCFGSVLGVLACLTHGATMVFPSPSfD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7827 RRNSLAkAISTMDVNWAFLTPS--VARLLDPGL----IPSLKILAIGGEQSSSADWNRwpgSVQKIH------VYGPTEC 7894
Cdd:cd05917     81 PLAVLE-AIEKEKCTALHGVPTmfIAELEHPDFdkfdLSSLRTGIMAGAPCPPELMKR---VIEVMNmkdvtiAYGMTET 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7895 CIFCTgyttkQGFEPSTIGTSVASV--------SWVVDPENhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAfIDDP 7966
Cdd:cd05917    157 SPVST-----QTRTDDSIEKRVNTVgrimphteAKIVDPEG-GIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA-IDGD 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7967 AWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGR-KDsqVKVRGqrvelGE--VEHHVRECL---PEARQlaVEVIl 8040
Cdd:cd05917    230 GW---------------LHTGDLAVMDEDGYCRIVGRiKD--MIIRG-----GEniYPREIEEFLhthPKVSD--VQVV- 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8041 psGQKNHAM---LAVFVQLGKGTHIahleekaggedsmaqvvfltgTEEELAK----RLPKHMVPTVFFALLHFPMTTSG 8113
Cdd:cd05917    285 --GVPDERYgeeVCAWIRLKEGAEL---------------------TEEDIKAyckgKIAHYKVPRYVFFVDEFPLTVSG 341

                   ....*...
gi 1820002560 8114 KADRKRLR 8121
Cdd:cd05917    342 KIQKFKLR 349
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
837-1367 1.88e-14

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 80.87  E-value: 1.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  837 QQLWVWN--ADMPPAVD----RCIHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLV-QLGVKREDVVPLCF 909
Cdd:PRK08974     2 EKVWLNRypADVPAEINpdryQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  910 EKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSQHA-----MLFASSERHqVTVSKVStSQLP-- 982
Cdd:PRK08974    82 PNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAhtlekVVFKTPVKH-VILTRMG-DQLSta 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  983 --TVVNFA--------------------------------KSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHG 1028
Cdd:PRK08974   160 kgTLVNFVvkyikrlvpkyhlpdaisfrsalhkgrrmqyvKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAK 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1029 EAFGYTDHAR----VLQFASYTFDACIAEIITTLLYGGC---ICVPSESDRR-NNLAK----AIStmDVNC---ALLTPS 1093
Cdd:PRK08974   240 AAYGPLLHPGkelvVTALPLYHIFALTVNCLLFIELGGQnllITNPRDIPGFvKELKKypftAIT--GVNTlfnALLNNE 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1094 VARLLEPSavpSLKRLVLQGEQVSFADWNRWPGSVQT--INGYGPTECS--VCCNTYSGKQgfKSGIIGTSVAS--LSWV 1167
Cdd:PRK08974   318 EFQELDFS---SLKLSVGGGMAVQQAVAERWVKLTGQylLEGYGLTECSplVSVNPYDLDY--YSGSIGLPVPSteIKLV 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1168 VDAGNhnrLAPLGSIGELLVEGPILARGYLNDIDKTeAAFIDDpAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLG 1247
Cdd:PRK08974   393 DDDGN---EVPPGEPGELWVKGPQVMLGYWQRPEAT-DEVIKD-GWL---------------ATGDIAVMDEEGFLRIVD 452
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1248 RKDSQVKVRGQRVELGEIEHHVrecLPEARQLAVEVI-LPSgqkehallaafiqldkgnhnalfeeKASGEDSMAQVV-- 1324
Cdd:PRK08974   453 RKKDMILVSGFNVYPNEIEDVV---MLHPKVLEVAAVgVPS-------------------------EVSGEAVKIFVVkk 504
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 1325 --FLTgvEEELAKRLPEHM----VPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:PRK08974   505 dpSLT--EEELITHCRRHLtgykVPKLVEFRDELPKSNVGKILRRELRD 551
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
4566-4993 1.94e-14

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 80.59  E-value: 1.94e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4566 ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLAS 4645
Cdd:cd05932      6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4646 A--QYATLWTSLGRSVVIVSEASTSQLPV------VTKTADPSVN-----PGNAAYAIFTSGSTGIPKGVVLEHKAVVTS 4712
Cdd:cd05932     86 KldDWKAMAPGVPEGLISISLPPPSAANCqyqwddLIAQHPPLEErptrfPEQLATLIYTSGTTGQPKGVMLTFGSFAWA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4713 CLGHGQAFGITDHTRVLqfaSYTFDACIAE---IITTLLCCGCICV--------PSDSDR----------------RNNL 4765
Cdd:cd05932    166 AQAGIEHIGTEENDRML---SYLPLAHVTErvfVEGGSLYGGVLVAfaesldtfVEDVQRarptlffsvprlwtkfQQGV 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4766 AKAINAMDVNWALLTPSVARMLDPCVVQSLKI----LVLGGEQVNSADWDRWPKSI--QTINAYGPTE-CSICCTTYSGK 4838
Cdd:cd05932    243 QDKIPQQKLNLLLKIPVVNSLVKRKVLKGLGLdqcrLAGCGSAPVPPALLEWYRSLglNILEAYGMTEnFAYSHLNYPGR 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4839 QgfKSGTIGTSIVSVSWVVDPEnhnrlaplgsiGELLVEGPILARGYLNDMEKTEAAFIDDpAWLlegygghsgrqgrly 4918
Cdd:cd05932    323 D--KIGTVGNAGPGVEVRISED-----------GEILVRSPALMMGYYKDPEATAEAFTAD-GFL--------------- 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4919 KTGDLVRYDADGNLVYLGRKDSQVKL-RGQRVELGEVEHHVreclteAKQLAVEVIVPEGEG-----GYAMLAAFVQLGD 4992
Cdd:cd05932    374 RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKL------AEHDRVEMVCVIGSGlpaplALVVLSEEARLRA 447

                   .
gi 1820002560 4993 D 4993
Cdd:cd05932    448 D 448
PLN02574 PLN02574
4-coumarate--CoA ligase-like
3472-3875 1.95e-14

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 81.04  E-value: 1.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3472 KARPHAPA-ICAWDGE-LTYGELDALSSKLASHLVQ-LGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPdhpAS 3548
Cdd:PLN02574    50 HNHNGDTAlIDSSTGFsISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP---SS 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3549 RHEEIFEQ---TGAQVVVASAQYSARWTSSSCHVVTVSKALSSQLPAVVDSTNTS-------------VRPENAAYIIFT 3612
Cdd:PLN02574   127 SLGEIKKRvvdCSVGLAFTSPENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFYElikedfdfvpkpvIKQDDVAAIMYS 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3613 SGSTGVPKGVVLEHRAVatsclghgrafgITNLSRVLQF--ASYTFDAC---------------IAEIITTLLCGGCICV 3675
Cdd:PLN02574   207 SGTTGASKGVVLTHRNL------------IAMVELFVRFeaSQYEYPGSdnvylaalpmfhiygLSLFVVGLLSLGSTIV 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3676 PSDSDRRNSLAKAISTMDVNWAFLTPSV-------ARLLDPGLIPSLKILAIGGEQSSSA---DWNRWPGSVQKIHVYGP 3745
Cdd:PLN02574   275 VMRRFDASDMVKVIDRFKVTHFPVVPPIlmaltkkAKGVCGEVLKSLKQVSCGAAPLSGKfiqDFVQTLPHVDFIQGYGM 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3746 TECCIFCT-GYTTKQGFEPSTIGTSVASV-SWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpAWL 3823
Cdd:PLN02574   355 TESTAVGTrGFNTEKLSKYSSVGLLAPNMqAKVVDWSTGCLLPP-GNCGELWIQGPGVMKGYLNNPKATQSTIDKD-GWL 432
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 3824 legypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 3875
Cdd:PLN02574   433 ---------------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLE 469
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
5616-6042 2.16e-14

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 80.83  E-value: 2.16e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5616 VPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKA 5695
Cdd:PRK07059    17 IDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5696 GGAFVPLDPDHPASRHEDTFRHTGAQVVV------TSAQHSARWIGTNHQVVTVSAGSLGQLSTLVNPV----------- 5758
Cdd:PRK07059    97 GYVVVNVNPLYTPRELEHQLKDSGAEAIVvlenfaTTVQQVLAKTAVKHVVVASMGDLLGFKGHIVNFVvrrvkkmvpaw 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5759 GLP-AIPENAV--------------------YIMFTSGSTGIPKGVVLEHRAVVT-----SCW---GRGRAFGITNLSRV 5809
Cdd:PRK07059   177 SLPgHVRFNDAlaegarqtfkpvklgpddvaFLQYTGGTTGVSKGATLLHRNIVAnvlqmEAWlqpAFEKKPRPDQLNFV 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5810 LQFASYTFDACMDEIITTLMYGGC-ICVPSDSDRRNdLVKAISTMDVSC---------ALLTPSVARLLEPSSvptLQML 5879
Cdd:PRK07059   257 CALPLYHIFALTVCGLLGMRTGGRnILIPNPRDIPG-FIKELKKYQVHIfpavntlynALLNNPDFDKLDFSK---LIVA 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5880 VLQGEQVSFADWNRWPASVQT--INGYGPTECS--ICCNTYSGKQgFkSGIIGTSVASVSWVVDPENHDRLaPLGSIGEL 5955
Cdd:PRK07059   333 NGGGMAVQRPVAERWLEMTGCpiTEGYGLSETSpvATCNPVDATE-F-SGTIGLPLPSTEVSIRDDDGNDL-PLGEPGEI 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5956 LVEGPILARGYLNDIQKTAAVFIDDpawlleGYpghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEV 6035
Cdd:PRK07059   410 CIRGPQVMAGYWNRPDETAKVMTAD------GF----------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEI 473

                   ....*..
gi 1820002560 6036 EHHVREC 6042
Cdd:PRK07059   474 EEVVASH 480
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
6706-7042 2.26e-14

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 80.30  E-value: 2.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6706 DLFTEQALARPNAPAvCAWDGE-LTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 6784
Cdd:cd05936      3 DLLEEAARRFPDKTA-LIFMGRkLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6785 DHPASRHEDILRQTGAQVI---------LASAQN--------------------TT------------------------ 6811
Cdd:cd05936     82 LYTPRELEHILNDSGAKALivavsftdlLAAGAPlgervaltpedvavlqytsgTTgvpkgamlthrnlvanalqikawl 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6812 ---------------LFQSSNQTVV----TVNRSSYILFP---DEN---------------------------------- 6835
Cdd:cd05936    162 edllegddvvlaalpLFHVFGLTVAlllpLALGATIVLIPrfrPIGvlkeirkhrvtifpgvptmyiallnapefkkrdf 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6836 -----------------------------REAY------------PFVRPS-------------------NAALAPLGSI 6855
Cdd:cd05936    242 sslrlcisggaplpvevaerfeeltgvpiVEGYgltetspvvavnPLDGPRkpgsigiplpgtevkivddDGEELPPGEV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6856 GELLVEGPILARGYLNDADKTAAAFVNDpaWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVEL 6935
Cdd:cd05936    322 GELWVRGPQVMKGYWNRPEETAEAFVDG--WL---------------RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYP 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6936 GEIENRLREcmPRATQMAVEVISPagaAEQAKTMVVAFLQLNDEArdallggnvpnddNLSAQvvfpaKVDEKLSNLLPS 7015
Cdd:cd05936    385 REVEEVLYE--HPAVAEAAVVGVP---DPYSGEAVKAFVVLKEGA-------------SLTEE-----EIIAFCREQLAG 441
                          490       500
                   ....*....|....*....|....*...
gi 1820002560 7016 YMMP-EVYFaVPQLPMMISGKTDRKRLR 7042
Cdd:cd05936    442 YKVPrQVEF-RDELPKSAVGKILRRELR 468
PRK06188 PRK06188
acyl-CoA synthetase; Validated
1933-2444 2.35e-14

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 80.42  E-value: 2.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpd 2012
Cdd:PRK06188    16 HLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL--- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2013 HP-ASR--HEDIFRQTGAQV-VVTSAQHSARWIGTNHQVVTV----SAGSLEQFSTLVN--------PVDLPAKPENAAY 2076
Cdd:PRK06188    93 HPlGSLddHAYVLEDAGISTlIVDPAPFVERALALLARVPSLkhvlTLGPVPDGVDLLAaaakfgpaPLVAAALPPDIAG 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2077 VMFTSGSTGTPKGVVLEHRAVVTsclghgqafgvtnlLRALQFTAY------TFDVCI-------AEIITTLVHGGCICV 2143
Cdd:PRK06188   173 LAYTGGTTGKPKGVMGTHRSIAT--------------MAQIQLAEWewpadpRFLMCTplshaggAFFLPTLLRGGTVIV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2144 PS--DSERrdnLAKAITDMQVNWGYLTSS-VARLLD-PCL----VPSLKVLVLGGEQVNSTD-------WGkwPSSVQTi 2208
Cdd:PRK06188   239 LAkfDPAE---VLRAIEEQRITATFLVPTmIYALLDhPDLrtrdLSSLETVYYGASPMSPVRlaeaierFG--PIFAQY- 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2209 ngYGPTECCVFCTGYTGIQGFQS-----GNIGTSIASVSWVVDPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAA 2283
Cdd:PRK06188   313 --YGQTEAPMVITYLRKRDHDPDdpkrlTSCGRPTPGLRVALLDED-GREVAQGEVGEICVRGPLVMDGYWNRPEETAEA 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2284 FIDDpaWLlegypgHegrqgrlykTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHhmrkCL---PEANQLAVEV 2360
Cdd:PRK06188   390 FRDG--WL------H---------TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVED----VLaehPAVAQVAVIG 448
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2361 VPPS--GERDHAMlaafirlddetrnspLIIKYAEDNSTAQIVfltgieEELSERLPQHMVP-TVFFAlVHFPTTTSGKT 2437
Cdd:PRK06188   449 VPDEkwGEAVTAV---------------VVLRPGAAVDAAELQ------AHVKERKGSVHAPkQVDFV-DSLPLTALGKP 506

                   ....*..
gi 1820002560 2438 DRKRLRE 2444
Cdd:PRK06188   507 DKKALRA 513
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
3486-3976 2.41e-14

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 79.70  E-value: 2.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3486 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDhpASRHEEIFEQTGAQVVVas 3565
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR--LTPNELAFQLKDSDVKL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3566 aqysarwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVL---EHRAVATSC---LGHGRA 3639
Cdd:cd05912     77 --------------------------------------DDIATIMYTSGTTGKPKGVQQtfgNHWWSAIGSalnLGLTED 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3640 ---------FGITNLSRVLQFASYTFDACI-----AEIITTLLCGGCICVPSdsdrrnslakAISTMdvnwafltpsVAR 3705
Cdd:cd05912    119 dnwlcalplFHISGLSILMRSVIYGMTVYLvdkfdAEQVLHLINSGKVTIIS----------VVPTM----------LQR 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3706 LLDPGLI---PSLKILAIGGEqssSADWNRWPGSVQK----IHVYGPTECCI-FCTgytTKQGFEPSTIGtSVASVSWVV 3777
Cdd:cd05912    179 LLEILGEgypNNLRCILLGGG---PAPKPLLEQCKEKgipvYQSYGMTETCSqIVT---LSPEDALNKIG-SAGKPLFPV 251
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3778 DPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGR 3857
Cdd:cd05912    252 ELKIEDDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENG--WF---------------KTGDIGYLDEEGFLYVLDR 314
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3858 KDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHAMLAAFVQLEEGTQNALLDkeaggedsmaqvvFLas 3937
Cdd:cd05912    315 RSDLIISGGENIYPAEIEEVLLS-HPAIKEAGV-VGIPDDKWGQVPVAFVVSERPISEEELIA-------------YC-- 377
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1820002560 3938 vEEELAKrlpeHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:cd05912    378 -SEKLAK----YKVPKKIYFVDELPRTASGKLLRHELKQ 411
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
4526-5056 2.68e-14

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 80.48  E-value: 2.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4526 QQLWAWN--QDVPPAIERcvhDQFA------EQARAR-PDTPAICAWDGELTYGELDTLSSKLASHLV-QLGVKPEDMVP 4595
Cdd:PRK08974     2 EKVWLNRypADVPAEINP---DRYQslvdmfEQAVARyADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4596 LCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLASAQYA-TL-------------WTSLG----- 4656
Cdd:PRK08974    79 LMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAhTLekvvfktpvkhviLTRMGdqlst 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4657 --RSVV------------------IVSEASTSQLPVVTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSC--- 4713
Cdd:PRK08974   159 akGTLVnfvvkyikrlvpkyhlpdAISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqa 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4714 -------LGHGQAFGITD----HTRVLQFASYTFdacIAEIITTLLccgcICVPSDSDRR-NNLAK----AINAmdVNW- 4776
Cdd:PRK08974   239 kaaygplLHPGKELVVTAlplyHIFALTVNCLLF---IELGGQNLL----ITNPRDIPGFvKELKKypftAITG--VNTl 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4777 --ALLTPSVARMLDpcvVQSLKILVLGGEQVNSADWDRWPKSIQT--INAYGPTECS--ICCTTYSGKQgfKSGTIGTSI 4850
Cdd:PRK08974   310 fnALLNNEEFQELD---FSSLKLSVGGGMAVQQAVAERWVKLTGQylLEGYGLTECSplVSVNPYDLDY--YSGSIGLPV 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4851 VSVS-WVVDPENHNrlAPLGSIGELLVEGPILARGYLNDMEKTeAAFIDDpAWLlegygghsgrqgrlyKTGDLVRYDAD 4929
Cdd:PRK08974   385 PSTEiKLVDDDGNE--VPPGEPGELWVKGPQVMLGYWQRPEAT-DEVIKD-GWL---------------ATGDIAVMDEE 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4930 GNLVYLGRKDSQVKLRGQRVELGEVEHHVrecLTEAKQLAVEVI-VPEGEGGyAMLAAFVQLGDdtyntlvkekaggDSL 5008
Cdd:PRK08974   446 GFLRIVDRKKDMILVSGFNVYPNEIEDVV---MLHPKVLEVAAVgVPSEVSG-EAVKIFVVKKD-------------PSL 508
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 5009 TvqvvfldrvEEELAKRVPEHmmLTTF-------FTLEaMPTTTSGKIDRKRLRE 5056
Cdd:PRK08974   509 T---------EEELITHCRRH--LTGYkvpklveFRDE-LPKSNVGKILRRELRD 551
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
7599-8035 2.73e-14

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 80.58  E-value: 2.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7599 ADVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQL-GVNPEDVVPLCFEKSMWTVVAMLAV 7677
Cdd:PRK05677    16 AEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGA 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7678 LKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARWT-----SSSCHVV-----------------TVSKALSSQ 7735
Cdd:PRK05677    96 MRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEkvlpkTGVKHVIvtevadmlpplkrllinAVVKHVKKM 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7736 LPAV-----------------VDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHR----------AVATSCLGHGRAFGI 7788
Cdd:PRK05677   176 VPAYhlpqavkfndalakgagQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRnlvanmlqcrALMGSNLNEGCEILI 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7789 TNLSrVLQFASYTFDaCIAeiitTLLCGG---CICVPSDSDrrnSLAKAIStmdvNWAFL------TPSVA-------RL 7852
Cdd:PRK05677   256 APLP-LYHIYAFTFH-CMA----MMLIGNhniLISNPRDLP---AMVKELG----KWKFSgfvglnTLFVAlcnneafRK 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7853 LDpglIPSLKILAIGGEQSSSADWNRWPGsvqkihVYGptecCIFCTGY-----------TTKQGFEPSTIGTSVASVSW 7921
Cdd:PRK05677   323 LD---FSALKLTLSGGMALQLATAERWKE------VTG----CAICEGYgmtetspvvsvNPSQAIQVGTIGIPVPSTLC 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7922 -VVDPENHNrlAPLGSMGELLMEGPILARGYLNDVDKTEAAFiDDPAWLlegypghpgrqgrlyKTGDLVQYNADGNLVY 8000
Cdd:PRK05677   390 kVIDDDGNE--LPLGEVGELCVKGPQVMKGYWQRPEATDEIL-DSDGWL---------------KTGDIALIQEDGYMRI 451
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1820002560 8001 LGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLA 8035
Cdd:PRK05677   452 VDRKKDMILVSGFNVYPNELE-DVLAALPGVLQCA 485
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1936-2445 2.85e-14

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 80.01  E-value: 2.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1936 TEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpdHPA 2015
Cdd:PRK03640     9 KQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN--TRL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2016 SRHEDIFR--QTGAQVVVTSAQHSARWIGtnHQVVTVSAGSLEQFS--TLVNPVDLpakpENAAYVMFTSGSTGTPKGVV 2091
Cdd:PRK03640    87 SREELLWQldDAEVKCLITDDDFEAKLIP--GISVKFAELMNGPKEeaEIQEEFDL----DEVATIMYTSGTTGKPKGVI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2092 L---EHRA-VVTSCLGHG--------------QAFGVTNLLRALQF--TAY---TFDVciAEIITTLVHGGcicvpsdse 2148
Cdd:PRK03640   161 QtygNHWWsAVGSALNLGlteddcwlaavpifHISGLSILMRSVIYgmRVVlveKFDA--EKINKLLQTGG--------- 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2149 rrdnlakaITDMQVNWGYLTSSVARLLDPCLVPSLKVLVLGGeqvnstdwGkwPSSVQT-----------INGYGPTECC 2217
Cdd:PRK03640   230 --------VTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGG--------G--PAPKPLleqckekgipvYQSYGMTETA 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2218 vfctgyTGIQGFQSGNIGTSIASV-----SWVVDPENHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDdpAWLl 2292
Cdd:PRK03640   292 ------SQIVTLSPEDALTKLGSAgkplfPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD--GWF- 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2293 egypghegrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMrkclpeANQLAVEVVPPSGERDH--- 2369
Cdd:PRK03640   363 --------------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL------LSHPGVAEAGVVGVPDDkwg 422
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2370 AMLAAFIRLDDEtrnspliikyaednstaqivfLTgiEEEL----SERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREI 2445
Cdd:PRK03640   423 QVPVAFVVKSGE---------------------VT--EEELrhfcEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4691-5055 3.04e-14

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 78.47  E-value: 3.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4691 FTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLqfASYTFDACIAEIITTLLCC--GCICV-PSDS-DRRNNLA 4766
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLC--IPVPLFHCFGSVLGVLACLthGATMVfPSPSfDPLAVLE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4767 kAIN-----------AMDVnwALLTPSVARMLDPcvvQSLKILVLGGEQVNSADWDRwpkSIQTIN------AYGPTECS 4829
Cdd:cd05917     87 -AIEkekctalhgvpTMFI--AELEHPDFDKFDL---SSLRTGIMAGAPCPPELMKR---VIEVMNmkdvtiAYGMTETS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4830 ICCTtysgkQGFKSGTIGTSIVSV--------SWVVDPENhNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAfIDDPA 4901
Cdd:cd05917    158 PVST-----QTRTDDSIEKRVNTVgrimphteAKIVDPEG-GIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA-IDGDG 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4902 WllegygghsgrqgrlYKTGDLVRYDADGNLVYLGR-KDSQVKlRGQRVELGEVEhhvrECL-TEAKQLAVEVI-VPE-- 4976
Cdd:cd05917    231 W---------------LHTGDLAVMDEDGYCRIVGRiKDMIIR-GGENIYPREIE----EFLhTHPKVSDVQVVgVPDer 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4977 -GEggyaMLAAFVQLGDdtyntlvkekagGDSLTVQVVfLDRVEEELAK-RVPEHmmlttFFTLEAMPTTTSGKIDRKRL 5054
Cdd:cd05917    291 yGE----EVCAWIRLKE------------GAELTEEDI-KAYCKGKIAHyKVPRY-----VFFVDEFPLTVSGKIQKFKL 348

                   .
gi 1820002560 5055 R 5055
Cdd:cd05917    349 R 349
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
4568-5056 3.17e-14

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 80.02  E-value: 3.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4568 TYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLASAQ 4647
Cdd:PLN02330    57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4648 YATLWTSLGRSVVIVSEASTSQ-------LPVVTKTADPSVNP----GNAAYAIFTSGSTGIPKGVVLEHKAVVTS-Clg 4715
Cdd:PLN02330   137 NYGKVKGLGLPVIVLGEEKIEGavnwkelLEAADRAGDTSDNEeilqTDLCALPFSSGTTGISKGVMLTHRNLVANlC-- 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4716 hGQAFGITDHTrVLQFASYTFDACIAEIITTLLCC------GCICVPSDSDRRNNLaKAINAMDVNWALLTPSVARML-- 4787
Cdd:PLN02330   215 -SSLFSVGPEM-IGQVVTLGLIPFFHIYGITGICCatlrnkGKVVVMSRFELRTFL-NALITQEVSFAPIVPPIILNLvk 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4788 DPcVVQSLKILVLGGEQVNSADWDRWPK----------SIQTINAYGPTECSiCCTTYSGK----QGF-KSGTIGTSIVS 4852
Cdd:PLN02330   292 NP-IVEEFDLSKLKLQAIMTAAAPLAPElltafeakfpGVQVQEAYGLTEHS-CITLTHGDpekgHGIaKKNSVGFILPN 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4853 VSW-VVDPENHNRLaPLGSIGELLVEGPILARGYLNDMEKTEAAfIDDPAWLlegygghsgrqgrlyKTGDLVRYDADGN 4931
Cdd:PLN02330   370 LEVkFIDPDTGRSL-PKNTPGELCVRSQCVMQGYYNNKEETDRT-IDEDGWL---------------HTGDIGYIDDDGD 432
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4932 LVYLGRKDSQVKLRGQRVELGEVEhhvreclteakqlAVEVIVPEGEGgyamlAAFVQLGDdtyntlvkEKAGGDSLTVQ 5011
Cdd:PLN02330   433 IFIVDRIKELIKYKGFQVAPAELE-------------AILLTHPSVED-----AAVVPLPD--------EEAGEIPAACV 486
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 5012 VVFLDRVEEE------LAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:PLN02330   487 VINPKAKESEedilnfVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
1954-2445 3.81e-14

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 79.88  E-value: 3.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1954 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTS 2033
Cdd:cd17642     44 NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2034 AQHSARWIGTNHQVVTVSA-------------GSLEQFSTLVNPVDLPA---------KPENAAYVMFTSGSTGTPKGVV 2091
Cdd:cd17642    124 KKGLQKVLNVQKKLKIIKTiiildskedykgyQCLYTFITQNLPPGFNEydfkppsfdRDEQVALIMNSSGSTGLPKGVQ 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2092 LEHRAVVTScLGH-------GQAFGVTNLLRALQFTaYTFDvcIAEIITTLVHGGCICVPSDSERRDNLaKAITDMQVNW 2164
Cdd:cd17642    204 LTHKNIVAR-FSHardpifgNQIIPDTAILTVIPFH-HGFG--MFTTLGYLICGFRVVLMYKFEEELFL-RSLQDYKVQS 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2165 GYLTSSV------ARLLDPCLVPSLKVLVLGG--------EQVNSTdwGKWPSSVQtinGYGPTEC--CVFCTGYTGIQG 2228
Cdd:cd17642    279 ALLVPTLfaffakSTLVDKYDLSNLHEIASGGaplskevgEAVAKR--FKLPGIRQ---GYGLTETtsAILITPEGDDKP 353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2229 FQSGNIGTSIASVswVVDPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAfIDDPAWLlegypghegrqgrlyKT 2308
Cdd:cd17642    354 GAVGKVVPFFYAK--VVDLDT-GKTLGPNERGELCVKGPMIMKGYVNNPEATKAL-IDKDGWL---------------HS 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2309 GDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKClPEANQLAVEVVP--PSGErdhaMLAAFIRLD-DETRNS 2385
Cdd:cd17642    415 GDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQH-PKIFDAGVAGIPdeDAGE----LPAAVVVLEaGKTMTE 489
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2386 PLIIKYAEDNSTAqivfltgieeelSERLPQhmvpTVFFaLVHFPTTTSGKTDRKRLREI 2445
Cdd:cd17642    490 KEVMDYVASQVST------------AKRLRG----GVKF-VDEVPKGLTGKIDRRKIREI 532
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
4547-5056 3.85e-14

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 80.08  E-value: 3.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQARAR-PDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 4625
Cdd:PRK06710    29 YVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4626 PASRHEHIFRQTGAQVVL---------ASAQYAT--------------------LWTSLGRS----VVIVSEASTSQL-P 4671
Cdd:PRK06710   109 TERELEYQLHDSGAKVILcldlvfprvTNVQSATkiehvivtriadflpfpknlLYPFVQKKqsnlVVKVSESETIHLwN 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4672 VVTKTADPSV----NPGN-AAYAIFTSGSTGIPKGVVLEHKAVVTSCL-GHGQAFGITDHTRVLQ-----FASYTFDACI 4740
Cdd:PRK06710   189 SVEKEVNTGVevpcDPENdLALLQYTGGTTGFPKGVMLTHKNLVSNTLmGVQWLYNCKEGEEVVLgvlpfFHVYGMTAVM 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4741 AeiITTLLCCGCICVPS-------DSDRRNNLAKAINAMDVNWALLTPSVARMLDpcvVQSLKILVLGGEQVNSADWDRW 4813
Cdd:PRK06710   269 N--LSIMQGYKMVLIPKfdmkmvfEAIKKHKVTLFPGAPTIYIALLNSPLLKEYD---ISSIRACISGSAPLPVEVQEKF 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4814 PKSI--QTINAYGPTECSICCTTYSGKQGFKSGTIGtsivsVSW------VVDPENHNRLAPlGSIGELLVEGPILARGY 4885
Cdd:PRK06710   344 ETVTggKLVEGYGLTESSPVTHSNFLWEKRVPGSIG-----VPWpdteamIMSLETGEALPP-GEIGEIVVKGPQIMKGY 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4886 LNDMEKTEAAFIDdpAWLlegygghsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREclTEA 4965
Cdd:PRK06710   418 WNKPEETAAVLQD--GWL---------------HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYE--HEK 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4966 KQLAVEVIVPEGEGGyAMLAAFVQLGDDTYNTlvKEKaggdsltvqvvfLDRVEEEL--AKRVPEhmmltTFFTLEAMPT 5043
Cdd:PRK06710   479 VQEVVTIGVPDPYRG-ETVKAFVVLKEGTECS--EEE------------LNQFARKYlaAYKVPK-----VYEFRDELPK 538
                          570
                   ....*....|...
gi 1820002560 5044 TTSGKIDRKRLRE 5056
Cdd:PRK06710   539 TTVGKILRRVLIE 551
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
445-795 4.90e-14

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 78.57  E-value: 4.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  445 YIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHsELGLLQVVVEEK---MQWT-------ESESLEEYLNEDKA 514
Cdd:cd19533     24 YNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWIDPYTpvpIRHIdlsgdpdPEGAAQQWMQEDLR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  515 ASMGLGDR-LARYALIKesCGGKRWFVW-TIHHALYDGWSLPLVLDAVKQVYSGAALERQP---SFNTFIQYV-SQQDVK 588
Cdd:cd19533    103 KPLPLDNDpLFRHALFT--LGDNRHFWYqRVHHIVMDGFSFALFGQRVAEIYTALLKGRPAppaPFGSFLDLVeEEQAYR 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  589 AA------AAYWQTALADC-EAVLF-PPLPSTVTQPVADTTVkyqCPPSPEVT------SSNITTSTLIRAAWAIIASRY 654
Cdd:cd19533    181 QSerferdRAFWTEQFEDLpEPVSLaRRAPGRSLAFLRRTAE---LPPELTRTlleaaeAHGASWPSFFIALVAAYLHRL 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  655 TSSEDIVFGTTVTGRnapiTGVEA--MVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIA-----YEQtgLQRIMKM 727
Cdd:cd19533    258 TGANDVVLGVPVMGR----LGAAArqTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRhqryrYED--LRRDLGL 331
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  728 GPGPQHAcgFQTLLVVHPTDDVLSSDDTLGEWHSrsdselqYFT--TYALTIQCTLAVEGVQITASFDAR 795
Cdd:cd19533    332 TGELHPL--FGPTVNYMPFDYGLDFGGVVGLTHN-------LSSgpTNDLSIFVYDRDDESGLRIDFDAN 392
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
5647-6138 4.94e-14

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 79.49  E-value: 4.94e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5647 ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTS 5726
Cdd:cd17642     44 NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5727 AQHSARWIGTNHQVVTV-------SAGSLGQLSTLVNPVGLPAIPENAVY---------------IMFTSGSTGIPKGVV 5784
Cdd:cd17642    124 KKGLQKVLNVQKKLKIIktiiildSKEDYKGYQCLYTFITQNLPPGFNEYdfkppsfdrdeqvalIMNSSGSTGLPKGVQ 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5785 LEHRAVVT---SCwgRGRAFG--ITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRNDLvKAISTMDVSCAL 5859
Cdd:cd17642    204 LTHKNIVArfsHA--RDPIFGnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFL-RSLQDYKVQSAL 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5860 LTPSV------ARLLEPSSVPTLQMLVLQGEQVS------FADWNRWPASVQtinGYGPTECSICcnTYSGKQGF-KSGI 5926
Cdd:cd17642    281 LVPTLfaffakSTLVDKYDLSNLHEIASGGAPLSkevgeaVAKRFKLPGIRQ---GYGLTETTSA--ILITPEGDdKPGA 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5927 IGTSVASVSW-VVDPENHDRLAPlGSIGELLVEGPILARGYLNDIQKTAAVfIDDPAWLlegypghpgrqgrlyKTGDLV 6005
Cdd:cd17642    356 VGKVVPFFYAkVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEATKAL-IDKDGWL---------------HSGDIA 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6006 RYDANGNLVCLGRKDSQVKLRGQRVELGEVE----HHvreclPEARQLAVevilpSGQKDHA---MLAAFVQLEEGTQna 6078
Cdd:cd17642    419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELEsillQH-----PKIFDAGV-----AGIPDEDageLPAAVVVLEAGKT-- 486
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6079 LLDKEasgedsmaqVVFLASVEEELAKRLPEhmvpTVFFsLLHFPTTTSGKTDRKRLREI 6138
Cdd:cd17642    487 MTEKE---------VMDYVASQVSTAKRLRG----GVKF-VDEVPKGLTGKIDRRKIREI 532
PRK07470 PRK07470
acyl-CoA synthetase; Validated
4546-5056 5.10e-14

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 79.31  E-value: 5.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4546 QFAEQARAR-PDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVP---- 4620
Cdd:PRK07470    11 HFLRQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPtnfr 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4621 LDPDHPAsrheHIFRQTGAQVVLASAQY-----ATLWTSLGRSVVIVSEASTSQLPVVT--------KTADPSVNPGNAA 4687
Cdd:PRK07470    91 QTPDEVA----YLAEASGARAMICHADFpehaaAVRAASPDLTHVVAIGGARAGLDYEAlvarhlgaRVANAAVDHDDPC 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4688 YAIFTSGSTGIPKGVVLEHKA---VVTSCLGHGQAfGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNN 4764
Cdd:PRK07470   167 WFFFTSGTTGRPKAAVLTHGQmafVITNHLADLMP-GTTEQDASLVVAPLSHGAGIHQLCQVARGAATVLLPSERFDPAE 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4765 LAKAINAMDVNWALLTPSVARML--DPCVVQ----SLKILVLGGEQVNSADWDRwpkSIQTINA-----YGPTECSICCT 4833
Cdd:PRK07470   246 VWALVERHRVTNLFTVPTILKMLveHPAVDRydhsSLRYVIYAGAPMYRADQKR---ALAKLGKvlvqyFGLGEVTGNIT 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4834 T-----YSGKQG--FKSGTIGTSIVSVSWVVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAFIDDpaWlleg 4906
Cdd:PRK07470   323 VlppalHDAEDGpdARIGTCGFERTGMEVQIQDDEGRELPP-GETGEICVIGPAVFAGYYNNPEANAKAFRDG--W---- 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4907 ygghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVrecLTEAKQLAVEVI-VPE---GEGGYA 4982
Cdd:PRK07470   396 -----------FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKL---LTHPAVSEVAVLgVPDpvwGEVGVA 461
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 4983 MLAAfvqlgddtyntlvkeKAGGDsltvqvVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:PRK07470   462 VCVA---------------RDGAP------VDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
27-284 5.28e-14

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 78.49  E-value: 5.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   27 LVMGGEqVNSADWDRWPS--SVQTINGYGPTECcIVCTGYTSEQDFTTGTIGTSIASVSW-VVDpkDHGRLAPLGSVGEL 103
Cdd:cd05934    200 AAYGAP-NPPELHEEFEErfGVRLLEGYGMTET-IVGVIGPRDEPRRPGSIGRPAPGYEVrIVD--DDGQELPAGEPGEL 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  104 LV---EGPILARGYLSDPEKTAAVFINnpAWLLeghggyagrqgrlykTGDLVRYDADGNLVCLGRKDSQVKLRGQRVEL 180
Cdd:cd05934    276 VIrglRGWGFFKGYYNMPEATAEAMRN--GWFH---------------TGDLGYRDADGFFYFVDRKKDMIRRRGENISS 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  181 GEVE-----HhvreclPEAKQLAVeVVLPlGQKNHATLAAFIQLDKGthnallkekvGGDDSIARVVFLAGveeelakRL 255
Cdd:cd05934    339 AEVErailrH------PAVREAAV-VAVP-DEVGEDEVKAVVVLRPG----------ETLDPEELFAFCEG-------QL 393
                          250       260
                   ....*....|....*....|....*....
gi 1820002560  256 PKHMVPTVFFALLHFPTTTSGKTDRKRLR 284
Cdd:cd05934    394 AYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
8152-8210 5.32e-14

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 69.90  E-value: 5.32e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8152 QTMQQLWARVLGIDADIIGLDDSFFRLGGDSIAAMKLVGEARRT-GLQLSVADIFRHPRL 8210
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTL 60
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
877-1266 5.59e-14

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 79.02  E-value: 5.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPAsrhEEIfkqigaQVVLTS 956
Cdd:cd05914      7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTA---DEV------HHILNH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  957 SQHAMLFASserhqvtvskvstsqlptvvnfakspvDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDH 1036
Cdd:cd05914     78 SEAKAIFVS---------------------------DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKG 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1037 ARVLQFA--SYTFdACIAEIITTLLYGGCICVPSE--SDRRNNLAKAISTMDVN-CALLT----------PSVA------ 1095
Cdd:cd05914    131 DKILSILplHHIY-PLTFTLLLPLLNGAHVVFLDKipSAKIIALAFAQVTPTLGvPVPLViekifkmdiiPKLTlkkfkf 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1096 RLLEPSAVPSLKRLVLQGEQVSFADWNRWPGS------------VQTIN-----GYGPTECS--VCcntYSGKQGFKSGI 1156
Cdd:cd05914    210 KLAKKINNRKIRKLAFKKVHEAFGGNIKEFVIggakinpdveefLRTIGfpytiGYGMTETApiIS---YSPPNRIRLGS 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1157 IGTSVASLSWVVDAGNhnrlaPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpAWLlegyeghagrrgrlyKTGDLVR 1236
Cdd:cd05914    287 AGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKD-GWF---------------HTGDLGK 345
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1820002560 1237 CDADGNLVCLGRKDSQ-VKVRGQRVELGEIE 1266
Cdd:cd05914    346 IDAEGYLYIRGRKKEMiVLSSGKNIYPEEIE 376
PRK08315 PRK08315
AMP-binding domain protein; Validated
844-1371 5.74e-14

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 79.47  E-value: 5.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  844 ADMPPAVDRCIHDLFAEQARARPDASAVCAWDGEL--TYGELDELSSKLAAHLVQLGVKREDVV----PLCFEksmWTVV 917
Cdd:PRK08315     8 PTDVPLLEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVgiwaPNVPE---WVLT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  918 aMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVL------TSSQHAML------FASSERHQVTVSKVstSQLPTVV 985
Cdd:PRK08315    85 -QFATAKIGAILVTINPAYRLSELEYALNQSGCKALIaadgfkDSDYVAMLyelapeLATCEPGQLQSARL--PELRRVI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  986 -----------NFAK--------------------SPVDPGNtayIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYT 1034
Cdd:PRK08315   162 flgdekhpgmlNFDEllalgravddaelaarqatlDPDDPIN---IQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLT 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1035 DHAR----------------VLqfasytfdACIAeiittllYGGCICVPSES-DRRNNLAkAIS-----------TMDVn 1086
Cdd:PRK08315   239 EEDRlcipvplyhcfgmvlgNL--------ACVT-------HGATMVYPGEGfDPLATLA-AVEeerctalygvpTMFI- 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1087 cALLT-PSVARL----LE-------PSAVPSLKRLVlqgEQVSFADwnrwpgsvQTInGYGPTECS-VCCNTYSG----K 1149
Cdd:PRK08315   302 -AELDhPDFARFdlssLRtgimagsPCPIEVMKRVI---DKMHMSE--------VTI-AYGMTETSpVSTQTRTDdpleK 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1150 QGFKSGII--GTSVAslswVVDAGNhNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAfIDDPAWLlegyegHagrrgr 1227
Cdd:PRK08315   369 RVTTVGRAlpHLEVK----IVDPET-GETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDADGWM------H------ 430
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1228 lykTGDLVRCDADGNLVCLGR-KDsqVKVRGqrvelG------EIE----HHvreclPEArqLAVEVI-LPSgQKEHALL 1295
Cdd:PRK08315   431 ---TGDLAVMDEEGYVNIVGRiKD--MIIRG-----GeniyprEIEeflyTH-----PKI--QDVQVVgVPD-EKYGEEV 492
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 1296 AAFIQLDKGnhnalfeEKASGEDSMAqvvFLTGveeelakRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDIGAS 1371
Cdd:PRK08315   493 CAWIILRPG-------ATLTEEDVRD---FCRG-------KIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIE 551
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
23-285 5.79e-14

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 79.18  E-value: 5.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRWPSS--VQTI-NGYGPTECCIVCTGYTSEQDFTT--GTIGTSIASVSW-VVDPkdHGRLAP 96
Cdd:PRK07656   282 SLRLAVTGAASMPVALLERFESElgVDIVlTGYGLSEASGVTTFNRLDDDRKTvaGTIGTAIAGVENkIVNE--LGEEVP 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   97 LGSVGELLVEGPILARGYLSDPEKTAAVfINNPAWLlegHggyagrqgrlykTGDLVRYDADGNLVCLGRKDSQVKLRGQ 176
Cdd:PRK07656   360 VGEVGELLVRGPNVMKGYYDDPEATAAA-IDADGWL---H------------TGDLGRLDEEGYLYIVDRKKDMFIVGGF 423
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  177 RVELGEVEhhvrECL---PEAKQLAVeVVLP---LGQKNHatlaAFIQLDKGthnallkekvggddsiARVvflagVEEE 250
Cdd:PRK07656   424 NVYPAEVE----EVLyehPAVAEAAV-IGVPderLGEVGK----AYVVLKPG----------------AEL-----TEEE 473
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1820002560  251 L----AKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:PRK07656   474 LiaycREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
7623-8121 5.93e-14

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 78.67  E-value: 5.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7623 APAICAWDGELTYGELDVLSSNLAGHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFE 7701
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7702 QTGAQVVVASAQYSARwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVLEHRAVATSCLG 7781
Cdd:cd05958     81 KARITVALCAHALTAS--------------------------------DDICILAFTSGTTGAPKATMHFHRDPLASADR 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7782 HGR-AFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAKAISTMDVNWAFLTPSVAR----LLDPG 7856
Cdd:cd05958    129 YAVnVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRamlaHPDAA 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7857 --LIPSLKILAIGGEQSSSADWNRWPGS--VQKIHVYGPTECC-IFCTgyTTKQGFEPSTIGTSVASVSW-VVDPENhnR 7930
Cdd:cd05958    209 gpDLSSLRKCVSAGEALPAALHRAWKEAtgIPIIDGIGSTEMFhIFIS--ARPGDARPGATGKPVPGYEAkVVDDEG--N 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7931 LAPLGSMGELLMEGPIlarGYLNDVDKTEAAFIDDpAWLLegypghpgrqgrlykTGDLVQYNADGNLVYLGRKDSQVKV 8010
Cdd:cd05958    285 PVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQG-GWNI---------------TGDTYSRDPDGYFRHQGRSDDMIVS 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8011 RGQRVELGEVEhhvrECL---PEARQLAVevilpSGQKNHAMLAV---FVQLGKGthiahleeKAGGEDSMAQVvfltgt 8084
Cdd:cd05958    346 GGYNIAPPEVE----DVLlqhPAVAECAV-----VGHPDESRGVVvkaFVVLRPG--------VIPGPVLAREL------ 402
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1820002560 8085 eEELAKR-LPKHMVPTVFFALLHFPMTTSGKADRKRLR 8121
Cdd:cd05958    403 -QDHAKAhIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
8279-8514 6.12e-14

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 78.60  E-value: 6.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8279 PREAFNYPF-IDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVI-PRHQDLPFSIFEV------NGALAEESQ 8350
Cdd:cd19066     20 DPSAFNVAIeMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVlDKTVRFRIEIIDLrnladpEARLLELID 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8351 AIHIRDLDQTSPlglPTSF-TLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIY------QQEPLLSTTGFHSYLAY 8423
Cdd:cd19066    100 QIQQTIYDLERG---PLVRvALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYdaaerqKPTLPPPVGSYADYAAW 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8424 VHNQRS-----ASINYWSRLLKGSHITNITSKL-RPKLGKDTTIRSVK----VERVIRTPQLPT--GLTMASLVSSAWAV 8491
Cdd:cd19066    177 LEKQLEseaaqADLAYWTSYLHGLPPPLPLPKAkRPSQVASYEVLTLEfflrSEETKRLREVAResGTTPTQLLLAAFAL 256
                          250       260
                   ....*....|....*....|...
gi 1820002560 8492 VLSHISGEEDVVYGLVVAGRNSD 8514
Cdd:cd19066    257 ALKRLTASIDVVIGLTFLNRPDE 279
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
5626-6036 6.93e-14

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 78.94  E-value: 6.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFtEQAKAR-PHAPAICAWDGELTYGELDALSSKLAGHL-TQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 5703
Cdd:PRK08974    27 DMF-EQAVARyADQPAFINMGEVMTFRKLEERSRAFAAYLqNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVN 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5704 PDHPASRHEDTFRHTGAQ--VVVTSAQHSARWIGTNHQVVTVSAGSLG-QLS----TLVNPV-----------GLP-AI- 5763
Cdd:PRK08974   106 PLYTPRELEHQLNDSGAKaiVIVSNFAHTLEKVVFKTPVKHVILTRMGdQLStakgTLVNFVvkyikrlvpkyHLPdAIs 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5764 -------------------PENAVYIMFTSGSTGIPKGVVLEHRAVVTSC----WG------RGRAFGITNLSRVLQFAS 5814
Cdd:PRK08974   186 frsalhkgrrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqakAAygpllhPGKELVVTALPLYHIFAL 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5815 ytfdacmdeIITTLMY---GGC---ICVPSDSDrrnDLVKAISTMDVSC---------ALLTPSVARLLEPSSvptLQML 5879
Cdd:PRK08974   266 ---------TVNCLLFielGGQnllITNPRDIP---GFVKELKKYPFTAitgvntlfnALLNNEEFQELDFSS---LKLS 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5880 VLQGEQVSFADWNRWPASVQT--INGYGPTECS--ICCNTYSGKQgfKSGIIGTSVASVS-WVVDPENHDrlAPLGSIGE 5954
Cdd:PRK08974   331 VGGGMAVQQAVAERWVKLTGQylLEGYGLTECSplVSVNPYDLDY--YSGSIGLPVPSTEiKLVDDDGNE--VPPGEPGE 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5955 LLVEGPILARGYLNDIQKTAAVFIDdpAWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGE 6034
Cdd:PRK08974   407 LWVKGPQVMLGYWQRPEATDEVIKD--GWL---------------ATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNE 469

                   ..
gi 1820002560 6035 VE 6036
Cdd:PRK08974   470 IE 471
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
4579-5055 7.15e-14

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 79.07  E-value: 7.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4579 LASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD------------------------------PDHPAS 4628
Cdd:PLN02860    45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNyrwsfeeaksamllvrpvmlvtdetcsswyEELQND 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4629 RhehiFRQTGAQVVLASaqyatlwTSLGRSVVIVSEASTS---QLPVVTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLE 4705
Cdd:PLN02860   125 R----LPSLMWQVFLES-------PSSSVFIFLNSFLTTEmlkQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTIS 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4706 HKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGC-ICVPS-------DSDRRNNLAKAIN--AMDVN 4775
Cdd:PLN02860   194 HSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAChVLLPKfdakaalQAIKQHNVTSMITvpAMMAD 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4776 waLLTPSVARMLDPCVVQSLKILVLGGeqvnSADWDRWPKSIQT------INAYGPTE-CSICC--TTYSGKQGFKSGTI 4846
Cdd:PLN02860   274 --LISLTRKSMTWKVFPSVRKILNGGG----SLSSRLLPDAKKLfpnaklFSAYGMTEaCSSLTfmTLHDPTLESPKQTL 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4847 GTSIVSVSWVVD-----------PENHNRLAPLGS--IGELLVEGPILARGYLnDMEKTEAAFIDDPAWLlegygghsgr 4913
Cdd:PLN02860   348 QTVNQTKSSSVHqpqgvcvgkpaPHVELKIGLDESsrVGRILTRGPHVMLGYW-GQNSETASVLSNDGWL---------- 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4914 qgrlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREcltEAKQLAVEVI-VPEGEGGyAMLAAFVQLGD 4992
Cdd:PLN02860   417 -----DTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQ---HPGVASVVVVgVPDSRLT-EMVVACVRLRD 487
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4993 DTYNTLVKEKAGGDSLTVQvvfldrvEEELAKRVPEhMMLTTF-----FTL--EAMPTTTSGKIDRKRLR 5055
Cdd:PLN02860   488 GWIWSDNEKENAKKNLTLS-------SETLRHHCRE-KNLSRFkipklFVQwrKPFPLTTTGKIRRDEVR 549
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
3465-3983 7.61e-14

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 78.88  E-value: 7.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAkaRPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPED--VVPLCFEKSMWtvVAMLAVLKAGgaFVPLD 3542
Cdd:PRK10946    29 DILTRHA--ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDtaLVQLGNVAEFY--ITFFALLKLG--VAPVN 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3543 PDHPASRHE--EIFEQTGAQVVVASAQYS-----------ARWTSSSCHVVTVSKALSSQLPAVV-----DSTNTSVRPE 3604
Cdd:PRK10946   103 ALFSHQRSElnAYASQIEPALLIADRQHAlfsdddflntlVAEHSSLRVVLLLNDDGEHSLDDAInhpaeDFTATPSPAD 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3605 NAAYIIFTSGSTGVPKGVVLEH-------RAVATSClghgrafGITNLSRVLQF--ASYTFDACIAEIITTLLCGGCICV 3675
Cdd:PRK10946   183 EVAFFQLSGGSTGTPKLIPRTHndyyysvRRSVEIC-------GFTPQTRYLCAlpAAHNYPMSSPGALGVFLAGGTVVL 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3676 PSDSDRRNSLAkAISTMDVNWAFLTPSVARL-----LDPG---LIPSLKILAIGGEQSSSADWNRWPGSV--QKIHVYGP 3745
Cdd:PRK10946   256 APDPSATLCFP-LIEKHQVNVTALVPPAVSLwlqaiAEGGsraQLASLKLLQVGGARLSETLARRIPAELgcQLQQVFGM 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3746 TECCIfctGYTTKQGFEPSTIGTSVASVS-----WVVDpENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFiDDp 3820
Cdd:PRK10946   335 AEGLV---NYTRLDDSDERIFTTQGRPMSpddevWVAD-ADGNPLPQ-GEVGRLMTRGPYTFRGYYKSPQHNASAF-DA- 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3821 awllEGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHhvreclpearqlaveVILpsgQKD 3900
Cdd:PRK10946   408 ----NGF----------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIEN---------------LLL---RHP 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3901 HAMLAAFVQLEEgtqnalldkEAGGEDSMAqvvFLASVEE----ELAKRLPEHMV-----PTVFFSLLHFPTTTSGKTDR 3971
Cdd:PRK10946   456 AVIHAALVSMED---------ELMGEKSCA---FLVVKEPlkavQLRRFLREQGIaefklPDRVECVDSLPLTAVGKVDK 523
                          570
                   ....*....|..
gi 1820002560 3972 KRLREIGASFTA 3983
Cdd:PRK10946   524 KQLRQWLASRAS 535
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
3465-3647 7.83e-14

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 79.15  E-value: 7.83e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGG--AFV--- 3539
Cdd:PRK08279    41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLntq 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3540 ----PL-------DPDHPASRHE--EIFEQTGAQVVVASAQYSArWTSSSCHVVTVS--KALSSQLPAVVDSTNTSVRPE 3604
Cdd:PRK08279   121 qrgaVLahslnlvDAKHLIVGEElvEAFEEARADLARPPRLWVA-GGDTLDDPEGYEdlAAAAAGAPTTNPASRSGVTAK 199
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 3605 NAAYIIFTSGSTGVPKGVVLEHRAVATSclghGRAFG-ITNLSR 3647
Cdd:PRK08279   200 DTAFYIYTSGTTGLPKAAVMSHMRWLKA----MGGFGgLLRLTP 239
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
7632-8122 7.87e-14

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 78.16  E-value: 7.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7632 ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDhpASRHEEIFEQTGAQVVVas 7711
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR--LTPNELAFQLKDSDVKL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7712 aqysarwtssschvvtvskalssqlpavvdstntsvrpENAAYIIFTSGSTGVPKGVVL---EHRAVATSC---LGHGRA 7785
Cdd:cd05912     77 --------------------------------------DDIATIMYTSGTTGKPKGVQQtfgNHWWSAIGSalnLGLTED 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7786 ---------FGITNLSRVLQFASYTFDACI-----AEIITTLLCGGCICVPSdsdrrnslakAISTMdvnwafltpsVAR 7851
Cdd:cd05912    119 dnwlcalplFHISGLSILMRSVIYGMTVYLvdkfdAEQVLHLINSGKVTIIS----------VVPTM----------LQR 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7852 LLDPGLI---PSLKILAIGGEqssSADWNRWPGSVQK----IHVYGPTECCI-FCTgytTKQGFEPSTIGtSVASVSWVV 7923
Cdd:cd05912    179 LLEILGEgypNNLRCILLGGG---PAPKPLLEQCKEKgipvYQSYGMTETCSqIVT---LSPEDALNKIG-SAGKPLFPV 251
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7924 DPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGR 8003
Cdd:cd05912    252 ELKIEDDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENG--WF---------------KTGDIGYLDEEGFLYVLDR 314
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8004 KDSQVKVRGQRVELGEVEHHVREcLPEARQLAVevilpsgqknhamlavfvqlgkgthIAHLEEKAGgedsMAQVVFLTG 8083
Cdd:cd05912    315 RSDLIISGGENIYPAEIEEVLLS-HPAIKEAGV-------------------------VGIPDDKWG----QVPVAFVVS 364
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 8084 ----TEEELA----KRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:cd05912    365 erpiSEEELIaycsEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
3468-3977 7.99e-14

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 78.47  E-value: 7.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3468 TEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpdHPA 3547
Cdd:PRK03640     9 KQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN--TRL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3548 SRHEEIF--EQTGAQVVVASAQYSARwtssschVVTVSKALSSQLPAVVDSTNTSVRP---ENAAYIIFTSGSTGVPKGV 3622
Cdd:PRK03640    87 SREELLWqlDDAEVKCLITDDDFEAK-------LIPGISVKFAELMNGPKEEAEIQEEfdlDEVATIMYTSGTTGKPKGV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3623 VL---EHRAVATSC---LG-HGR--------AFGITNLSRVLQFASY--------TFDaciAEIITTLLCGGcicvpsds 3679
Cdd:PRK03640   160 IQtygNHWWSAVGSalnLGlTEDdcwlaavpIFHISGLSILMRSVIYgmrvvlveKFD---AEKINKLLQTG-------- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3680 drrnslakAISTMDVNWAFLTPSVARLLDPGLIPSLKILAIGG--------EQsssadwnrwpgSVQK----IHVYGPTE 3747
Cdd:PRK03640   229 --------GVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGgpapkpllEQ-----------CKEKgipvYQSYGMTE 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3748 CC--IfCTgyttkqgFEPSTIGTSVASV-----SWVVDPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdp 3820
Cdd:PRK03640   290 TAsqI-VT-------LSPEDALTKLGSAgkplfPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD-- 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3821 AWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPearqlAVEVILPSGQKD 3900
Cdd:PRK03640   360 GWF---------------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE-EVLLSHP-----GVAEAGVVGVPD 418
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3901 H---AMLAAFVQLEEG-TQNALLDkeaggedsmaqvvFLasvEEELAKrlpeHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:PRK03640   419 DkwgQVPVAFVVKSGEvTEEELRH-------------FC---EEKLAK----YKVPKRFYFVEELPRNASGKLLRHELKQ 478

                   .
gi 1820002560 3977 I 3977
Cdd:PRK03640   479 L 479
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
998-1367 8.38e-14

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 76.60  E-value: 8.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  998 AYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGE--AFGYTDHARVLQFASYTfdACIAEIITTLLYGGcicVPSESDRRNN 1075
Cdd:cd17630      3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSrlGFGGGDSWLLSLPLYHV--GGLAILVRSLLAGA---ELVLLERNQA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1076 LAKAISTMDVNCALLTPS-VARLLE----PSAVPSLKRLVLQG--------EQVSFADWNRWPGsvqtingYGPTECSVC 1142
Cdd:cd17630     78 LAEDLAPPGVTHVSLVPTqLQRLLDsgqgPAALKSLRAVLLGGapippellERAADRGIPLYTT-------YGMTETASQ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1143 cntysgkqgfksgiIGTSVASLSWVVDAGNHNRLAPLGSI--GELLVEGPILARGYLNDIDKTEAafiDDPAWllegyeg 1220
Cdd:cd17630    151 --------------VATKRPDGFGRGGVGVLLPGRELRIVedGEIWVGGASLAMGYLRGQLVPEF---NEDGW------- 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1221 hagrrgrlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIE------HHVREC----LPEAR--QLAVEVILPSG 1288
Cdd:cd17630    207 --------FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEaalaahPAVRDAfvvgVPDEElgQRPVAVIVGRG 278
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 1289 QKEHALLAAFiqldkgnhnalfeekasgedsmaqvvfltgveeeLAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQD 1367
Cdd:cd17630    279 PADPAELRAW----------------------------------LKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
1967-2443 9.74e-14

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 78.69  E-value: 9.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1967 LASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVT--SAQH-------- 2036
Cdd:PLN02860    45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTdeTCSSwyeelqnd 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2037 ---SARW---IGTNHQVVTVSAGSLEQFSTLVNPV------DLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGH 2104
Cdd:PLN02860   125 rlpSLMWqvfLESPSSSVFIFLNSFLTTEMLKQRAlgttelDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAK 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2105 GQAFGVTNLLRALqftaYTFDVC----IAEIITTLVHGGC-ICVPS-------DSERRDNLAKAIT--DMQVNwgyLTSS 2170
Cdd:PLN02860   205 IAIVGYGEDDVYL----HTAPLChiggLSSALAMLMVGAChVLLPKfdakaalQAIKQHNVTSMITvpAMMAD---LISL 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2171 VARLLDPCLVPSLKVLVLGGEQVNStdwGKWPSSVQT------INGYGPTECC---VFCTGYTGIQGFQSGNIGTSIASV 2241
Cdd:PLN02860   278 TRKSMTWKVFPSVRKILNGGGSLSS---RLLPDAKKLfpnaklFSAYGMTEACsslTFMTLHDPTLESPKQTLQTVNQTK 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2242 SWVVDPENH---GRLAP----------LGSIGELLVEGPILARGYLnDVDKTQAAFIDDPAWLlegypghegrqgrlyKT 2308
Cdd:PLN02860   355 SSSVHQPQGvcvGKPAPhvelkigldeSSRVGRILTRGPHVMLGYW-GQNSETASVLSNDGWL---------------DT 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2309 GDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKclpEANQLAVEVVPPSGERDHAMLAAFIRLDDETRNSpli 2388
Cdd:PLN02860   419 GDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQ---HPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWS--- 492
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 2389 IKYAEDNSTAQIVfltgIEEEL-----SERLPQHMVPTVFFALVH-FPTTTSGKTDRKRLR 2443
Cdd:PLN02860   493 DNEKENAKKNLTL----SSETLrhhcrEKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVR 549
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
3487-3875 9.93e-14

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 78.17  E-value: 9.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVasa 3566
Cdd:cd17640      6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3567 qysarwtssschvvtvskalssqlpavVDStntsvRPENAAYIIFTSGSTGVPKGVVLEHRAVAtsclghgraFGITNLS 3646
Cdd:cd17640     83 ---------------------------VEN-----DSDDLATIIYTSGTTGNPKGVMLTHANLL---------HQIRSLS 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3647 ---------RVLQF----------ASYTFDAC-IAEIITTLlcggcICVPSDSDRRN------------SLAKAISTMDV 3694
Cdd:cd17640    122 divppqpgdRFLSIlpiwhsyersAEYFIFACgCSQAYTSI-----RTLKDDLKRVKphyivsvprlweSLYSGIQKQVS 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3695 NWAFLTPSVARLLDPGLIpsLKILAIGGeqsssadwNRWPGSVQK------IHV---YGPTECcifcTGYTTKQGFEPST 3765
Cdd:cd17640    197 KSSPIKQFLFLFFLSGGI--FKFGISGG--------GALPPHVDTffeaigIEVlngYGLTET----SPVVSARRLKCNV 262
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3766 IGTSVA----SVSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTG 3841
Cdd:cd17640    263 RGSVGRplpgTEIKIVDPEGNVVLPP-GEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDGWF---------------NTG 325
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1820002560 3842 DLVQYNADGNLVYLGR-KDSQVKVRGQRVELGEVE 3875
Cdd:cd17640    326 DLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIE 360
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
7589-8122 1.05e-13

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 78.38  E-value: 1.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7589 EDRQQLWAWNADVPPAIE----RCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLV-QLGVNPEDVVPLC 7663
Cdd:PRK08751     3 QARPWLQSYPAGVAAEIDleqfRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALM 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7664 FEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS--RHEEIFEQTGAQVVVASAQYSARWTSSSC---HVVT--VSKALSSQL 7736
Cdd:PRK08751    83 MPNCLQYPIATFGVLRAGLTVVNVNPLYTPRelKHQLIDSGASVLVVIDNFGTTVQQVIADTpvkQVITtgLGDMLGFPK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7737 PAVVD-------------STNTSVR-------------------PENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGR 7784
Cdd:PRK08751   163 AALVNfvvkyvkklvpeyRINGAIRfrealalgrkhsmptlqiePDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7785 AFGITNLSR------VLQFASYTFDACIAEIITTLLCGGC---ICVPSD--------SDRRNSLAKAISTMdVNWAFLTP 7847
Cdd:PRK08751   243 WLAGTGKLEegcevvITALPLYHIFALTANGLVFMKIGGCnhlISNPRDmpgfvkelKKTRFTAFTGVNTL-FNGLLNTP 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7848 SVARLlDpglIPSLKILAIGG---EQSSSADWNRWPGsVQKIHVYGPTECC-IFCTGYTTKQGFEPStIGTSVASVSWVV 7923
Cdd:PRK08751   322 GFDQI-D---FSSLKMTLGGGmavQRSVAERWKQVTG-LTLVEAYGLTETSpAACINPLTLKEYNGS-IGLPIPSTDACI 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7924 DpENHNRLAPLGSMGELLMEGPILARGYLNDVDKTeAAFIDDPAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGR 8003
Cdd:PRK08751   396 K-DDAGTVLAIGEIGELCIKGPQVMKGYWKRPEET-AKVMDADGWL---------------HTGDIARMDEQGFVYIVDR 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8004 KDSQVKVRGQRVELGEVEhHVRECLPEARQLAVeVILPSGQKNHAMLAVFVQlgKGTHIAHLEEKAGGEDSmaqvvfLTG 8083
Cdd:PRK08751   459 KKDMILVSGFNVYPNEIE-DVIAMMPGVLEVAA-VGVPDEKSGEIVKVVIVK--KDPALTAEDVKAHARAN------LTG 528
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 8084 TEE----ELAKRLPKhmvptvffallhfpmTTSGKADRKRLRE 8122
Cdd:PRK08751   529 YKQpriiEFRKELPK---------------TNVGKILRRELRD 556
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5647-6023 1.16e-13

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 77.89  E-value: 1.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5647 ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDhpasrhedtfrhtgaqvvvts 5726
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG--------------------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5727 aqhsarwIGTNHqvvtvsagsLGQLSTLVNP---VGLPAIPENAVyIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGI 5803
Cdd:cd05910     61 -------MGRKN---------LKQCLQEAEPdafIGIPKADEPAA-ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5804 TNLSRVLQ----FAsyTFDACMDeiITTLMYGGCICVPSDSDRRnDLVKAISTMDVSCALLTPSVARLL------EPSSV 5873
Cdd:cd05910    124 RPGEVDLAtfplFA--LFGPALG--LTSVIPDMDPTRPARADPQ-KLVGAIRQYGVSIVFGSPALLERVarycaqHGITL 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5874 PTLQMLVLQGEQVSFADWNRW----PASVQTINGYGPTEC---------SICCNTYSGKQGFKSGIIGTSVASVSWVVDP 5940
Cdd:cd05910    199 PSLRRVLSAGAPVPIALAARLrkmlSDEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTCVGRPIPGVRVRIIE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5941 EN--------HDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDPawllegypghpgRQGRLYKTGDLVRYDANGN 6012
Cdd:cd05910    279 IDdepiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN------------SEGFWHRMGDLGYLDDEGR 346
                          410
                   ....*....|.
gi 1820002560 6013 LVCLGRKDSQV 6023
Cdd:cd05910    347 LWFCGRKAHRV 357
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
4116-4409 1.22e-13

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 77.41  E-value: 1.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4116 YPCSPLQEGlMSLTAKRAGD---YIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHsELGLLQVVVEER----- 4187
Cdd:cd19533      2 LPLTSAQRG-VWFAEQLDPEgsiYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWIDPYTpvpir 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4188 -IQWTESESLEE----YPRED--KAVSMGvGDRLARYALIKepYDGGKRWFVWTMHHALYDGWSLPRILHAVKQAYSGVV 4260
Cdd:cd19533     80 hIDLSGDPDPEGaaqqWMQEDlrKPLPLD-NDPLFRHALFT--LGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4261 LERQPSFNAFIQYLSQQDPEAA----------AAYWqtalvdckAALFPTLPPTVT------QPVADTTVEYQCPPPSQ- 4323
Cdd:cd19533    157 KGRPAPPAPFGSFLDLVEEEQAyrqserferdRAFW--------TEQFEDLPEPVSlarrapGRSLAFLRRTAELPPELt 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4324 -------SATDITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRnapiAGGEAI--VGPTIATVPVRLRVQRDQTVFAFL 4394
Cdd:cd19533    229 rtlleaaEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR----LGAAARqtPGMVANTLPLRLTVDPQQTFAELV 304
                          330
                   ....*....|....*
gi 1820002560 4395 QGVQQQATDMIAHEQ 4409
Cdd:cd19533    305 AQVSRELRSLLRHQR 319
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
1922-2443 1.24e-13

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 78.14  E-value: 1.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1922 EVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLK 2001
Cdd:PRK07059    16 EIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLR 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2002 AGGAFVPLDPDHPASRHEDIFRQTGAQVVV------TSAQHSARWIGTNHQVVTvSAGSLEQFS-TLVNPV--------- 2065
Cdd:PRK07059    96 AGYVVVNVNPLYTPRELEHQLKDSGAEAIVvlenfaTTVQQVLAKTAVKHVVVA-SMGDLLGFKgHIVNFVvrrvkkmvp 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2066 --DLPAK---------------------PENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLG----HGQAFG------VTN 2112
Cdd:PRK07059   175 awSLPGHvrfndalaegarqtfkpvklgPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQmeawLQPAFEkkprpdQLN 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2113 LLRALQ-FTAYTFDVCiaeIITTLVHGGC-ICVPSDserRD--NLAKAITDMQVNW---------GYLTSSVARLLDpcl 2179
Cdd:PRK07059   255 FVCALPlYHIFALTVC---GLLGMRTGGRnILIPNP---RDipGFIKELKKYQVHIfpavntlynALLNNPDFDKLD--- 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2180 VPSLKVLVLGGEQVNSTDWGKWPSSVQT--INGYGPTEC--CVFCTGYTGIQgFqSGNIGTSIASvSWVVDPENHGRLAP 2255
Cdd:PRK07059   326 FSKLIVANGGGMAVQRPVAERWLEMTGCpiTEGYGLSETspVATCNPVDATE-F-SGTIGLPLPS-TEVSIRDDDGNDLP 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2256 LGSIGELLVEGPILARGYLNDVDKTQAAFIDDpawlleGYpghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQ 2335
Cdd:PRK07059   403 LGEPGEICIRGPQVMAGYWNRPDETAKVMTAD------GF----------FRTGDVGVMDERGYTKIVDRKKDMILVSGF 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2336 RVELGEVEHHMRKClPEANQLAVEVVPP--SGErdhaMLAAFIRLDDETRNSPLIIKYAEDNSTA-----QIVFLTgiee 2408
Cdd:PRK07059   467 NVYPNEIEEVVASH-PGVLEVAAVGVPDehSGE----AVKLFVVKKDPALTEEDVKAFCKERLTNykrpkFVEFRT---- 537
                          570       580       590
                   ....*....|....*....|....*....|....*
gi 1820002560 2409 ELserlpqhmvptvffalvhfPTTTSGKTDRKRLR 2443
Cdd:PRK07059   538 EL-------------------PKTNVGKILRRELR 553
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
6278-6556 1.25e-13

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 77.41  E-value: 1.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6278 YPCSPLQEGlMSLTAKRAGD---YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHsELGLLQVVVEEK----- 6349
Cdd:cd19533      2 LPLTSAQRG-VWFAEQLDPEgsiYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWIDPYTpvpir 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6350 -IQWTESKRLEE----YLREDKAVSMGL-GDPLARYAIIKeaWGGKRWFVW-TIHHALYDGWSLPRVLQAVKQAYNGAVL 6422
Cdd:cd19533     80 hIDLSGDPDPEGaaqqWMQEDLRKPLPLdNDPLFRHALFT--LGDNRHFWYqRVHHIVMDGFSFALFGQRVAEIYTALLK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6423 ETQPSFNAFIQYLSQQDLEAT----------AAYWQTALADCE--ATLFPPLPSSVKQLVADTTV----EHQCPLPSRST 6486
Cdd:cd19533    158 GRPAPPAPFGSFLDLVEEEQAyrqserferdRAFWTEQFEDLPepVSLARRAPGRSLAFLRRTAElppeLTRTLLEAAEA 237
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6487 SDTTTSTLIRAAWAIVASRYTSSDDVVFGTTITGRnAPVTSIDAiVGPTIATVPLRVRLQKDQTVSSFLG 6556
Cdd:cd19533    238 HGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR-LGAAARQT-PGMVANTLPLRLTVDPQQTFAELVA 305
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
7632-8087 1.27e-13

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 77.89  E-value: 1.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7632 ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVAS 7711
Cdd:cd05932      6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7712 A--QYSARWTSSSCHVVTVS-------------KALSSQLPAVVDSTNTSvrPENAAYIIFTSGSTGVPKGVVLEHRAVA 7776
Cdd:cd05932     86 KldDWKAMAPGVPEGLISISlpppsaancqyqwDDLIAQHPPLEERPTRF--PEQLATLIYTSGTTGQPKGVMLTFGSFA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7777 TSCLGHGRAFGITNLSRVLqfaSYTFDACIAEiiTTLLCGGCICvpsdSDRRNSLAKAISTM--DVNWAFLTP--SVAR- 7851
Cdd:cd05932    164 WAAQAGIEHIGTEENDRML---SYLPLAHVTE--RVFVEGGSLY----GGVLVAFAESLDTFveDVQRARPTLffSVPRl 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7852 -------------------LLDPGLIPSL---KIL-AIGGEQ-----SSSA-------DWNRWPGsVQKIHVYGPTECC- 7895
Cdd:cd05932    235 wtkfqqgvqdkipqqklnlLLKIPVVNSLvkrKVLkGLGLDQcrlagCGSApvppallEWYRSLG-LNILEAYGMTENFa 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7896 --IFCTGYTTKQGfepsTIGTSVASVSWVVDPEnhnrlaplgsmGELLMEGPILARGYLNDVDKTEAAFIDDpAWLlegy 7973
Cdd:cd05932    314 ysHLNYPGRDKIG----TVGNAGPGVEVRISED-----------GEILVRSPALMMGYYKDPEATAEAFTAD-GFL---- 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7974 pghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKV-RGQRVELGEVEHHVreclpeARQLAVEVILPSGQKNHAMLAV 8052
Cdd:cd05932    374 -----------RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKL------AEHDRVEMVCVIGSGLPAPLAL 436
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8053 fVQLGKGTHI---------------AHLEEKAGGEDSMAQVVFLTGTEEE 8087
Cdd:cd05932    437 -VVLSEEARLradafaraeleaslrAHLARVNSTLDSHEQLAGIVVVKDP 485
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
6298-6569 1.29e-13

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 77.40  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6298 YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSElGLLQVVVEE---KIQWTE---------SKRLEEYLRED 6365
Cdd:cd19531     24 YNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDG-EPVQVILPPlplPLPVVDlsglpeaerEAEAQRLAREE 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6366 KAVSMGLG-DPLARYAIIKEAwGGKRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSFNAF-IQY--------- 6434
Cdd:cd19531    103 ARRPFDLArGPLLRATLLRLG-EDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPPLpIQYadyavwqre 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6435 -LSQQDLEATAAYWQTALADCEATLfpPLPS-----SVKQLVADTtveHQCPLPsrstsdtttSTLIR------------ 6496
Cdd:cd19531    182 wLQGEVLERQLAYWREQLAGAPPVL--ELPTdrprpAVQSFRGAR---VRFTLP---------AELTAalralarregat 247
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 6497 ------AAWAIVASRYTSSDDVVFGTTITGRNAPvtSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEmiAYE 6569
Cdd:cd19531    248 lfmtllAAFQVLLHRYSGQDDIVVGTPVAGRNRA--ELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALE--AYA 322
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
858-1019 1.35e-13

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 77.60  E-value: 1.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  858 FAEQaraRPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHP 937
Cdd:PRK09029    12 WAQV---RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  938 ASRHEEIFKQIGAQvvltssqhamlFASSERHQVTVSKVSTSQLPTVVNFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQH 1017
Cdd:PRK09029    89 QPLLEELLPSLTLD-----------FALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTA 157

                   ..
gi 1820002560 1018 RA 1019
Cdd:PRK09029   158 QA 159
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
4553-5063 1.39e-13

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 78.11  E-value: 1.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4553 ARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPED--MVPLCFEKSMWtvVAMLAVLKAGgaFVPLDPDHPASRH 4630
Cdd:PRK10946    35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDtaLVQLGNVAEFY--ITFFALLKLG--VAPVNALFSHQRS 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4631 EHI--FRQTGAQVVLASAQYA---------TLWTSLG--RSVVIVSEASTSQL------PVVTKTADPSvNPGNAAYAIF 4691
Cdd:PRK10946   111 ELNayASQIEPALLIADRQHAlfsdddflnTLVAEHSslRVVLLLNDDGEHSLddainhPAEDFTATPS-PADEVAFFQL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4692 TSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQF--ASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLAkAI 4769
Cdd:PRK10946   190 SGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCAlpAAHNYPMSSPGALGVFLAGGTVVLAPDPSATLCFP-LI 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4770 NAMDVNW-ALLTPSVARMLDPCV-------VQSLKILVLGGEQVNSADWDRWPKSI--QTINAYGPTECSICCTTYSGKQ 4839
Cdd:PRK10946   269 EKHQVNVtALVPPAVSLWLQAIAeggsraqLASLKLLQVGGARLSETLARRIPAELgcQLQQVFGMAEGLVNYTRLDDSD 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4840 GFKSGTIGTSIVSVS--WVVDpENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAAFiDDpawllEGYgghsgrqgrl 4917
Cdd:PRK10946   349 ERIFTTQGRPMSPDDevWVAD-ADGNPLPQ-GEVGRLMTRGPYTFRGYYKSPQHNASAF-DA-----NGF---------- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4918 YKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVreclteakqLAVEVIVpegeggYAMLAAFV--QLGDDTY 4995
Cdd:PRK10946   411 YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLL---------LRHPAVI------HAALVSMEdeLMGEKSC 475
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 4996 NTLVKEKAggdsltVQVVFLDRVEEELAkrVPEHMMLTTFFTLEAMPTTTSGKIDRKRLREIGASFTA 5063
Cdd:PRK10946   476 AFLVVKEP------LKAVQLRRFLREQG--IAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
858-1365 1.41e-13

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 78.15  E-value: 1.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  858 FAEQARAR-PDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGH 936
Cdd:PRK06710    29 YVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  937 PASRHEEIFKQIGAQVVL---------TSSQHA--------------------MLFASSERHQVT-VSKVSTSQLPTVVN 986
Cdd:PRK06710   109 TERELEYQLHDSGAKVILcldlvfprvTNVQSAtkiehvivtriadflpfpknLLYPFVQKKQSNlVVKVSESETIHLWN 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  987 FAKS--------PVDPGNT-AYIIFTSGTTGIPKGVVLQHR-AVTTSCLGHGEAFGYTDHARVLQ-----FASYTFDACI 1051
Cdd:PRK06710   189 SVEKevntgvevPCDPENDlALLQYTGGTTGFPKGVMLTHKnLVSNTLMGVQWLYNCKEGEEVVLgvlpfFHVYGMTAVM 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1052 AeiiTTLLYGGCICVPSESDRRNnLAKAISTMDVNCALLTPSVARLLEPSavPSLKRLVLQGEQVSFADWNRWPGSVQT- 1130
Cdd:PRK06710   269 N---LSIMQGYKMVLIPKFDMKM-VFEAIKKHKVTLFPGAPTIYIALLNS--PLLKEYDISSIRACISGSAPLPVEVQEk 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1131 ---------INGYGPTECSVCCNTYSGKQGFKSGIIGTSVASLSWVVDAGNHNRLAPLGSIGELLVEGPILARGYLNDID 1201
Cdd:PRK06710   343 fetvtggklVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPE 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1202 KTEAAFIDdpAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREclPEARQLAV 1281
Cdd:PRK06710   423 ETAAVLQD--GWL---------------HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYE--HEKVQEVV 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1282 EVILPSGQKEHAlLAAFIQLDKGNHNAlfeekasgedsmaqvvfltgvEEEL----AKRLPEHMVPTILFTVKAMPITTS 1357
Cdd:PRK06710   484 TIGVPDPYRGET-VKAFVVLKEGTECS---------------------EEELnqfaRKYLAAYKVPKVYEFRDELPKTTV 541

                   ....*...
gi 1820002560 1358 GKIDRKRL 1365
Cdd:PRK06710   542 GKILRRVL 549
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
890-1366 1.42e-13

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 78.30  E-value: 1.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  890 LAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTSSQ----------- 958
Cdd:PLN02860    45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETcsswyeelqnd 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  959 -------HAMLFASSERHQVTVSKVSTSQLPTVVNFAKSPVD----PGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGH 1027
Cdd:PLN02860   125 rlpslmwQVFLESPSSSVFIFLNSFLTTEMLKQRALGTTELDyawaPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAK 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1028 GEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNNLaKAISTMDVNCALLTP-------SVARLLEP 1100
Cdd:PLN02860   205 IAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAAL-QAIKQHNVTSMITVPammadliSLTRKSMT 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1101 SAV-PSLKRLVLQGEQVSFadwNRWPGSVQT------INGYGPTE-CS---------VCCNTYSGKQGFKSGIIGTSVAS 1163
Cdd:PLN02860   284 WKVfPSVRKILNGGGSLSS---RLLPDAKKLfpnaklFSAYGMTEaCSsltfmtlhdPTLESPKQTLQTVNQTKSSSVHQ 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1164 L--SWVVDAGNHN--RLAPLGS--IGELLVEGPILARGYLnDIDKTEAAFIDDPAWLlegyeghagrrgrlyKTGDLVRC 1237
Cdd:PLN02860   361 PqgVCVGKPAPHVelKIGLDESsrVGRILTRGPHVMLGYW-GQNSETASVLSNDGWL---------------DTGDIGWI 424
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1238 DADGNLVCLGRKDSQVKVRGQRVELGEIE----HHvreclPEARQLAVEVILPSGQKEhaLLAAFIQLDKG---NHNALF 1310
Cdd:PLN02860   425 DKAGNLWLIGRSNDRIKTGGENVYPEEVEavlsQH-----PGVASVVVVGVPDSRLTE--MVVACVRLRDGwiwSDNEKE 497
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 1311 EEKASGEDSmaqvvfltgvEEEL-----AKRLPEHMVPTiLFTV--KAMPITTSGKIDRKRLQ 1366
Cdd:PLN02860   498 NAKKNLTLS----------SETLrhhcrEKNLSRFKIPK-LFVQwrKPFPLTTTGKIRRDEVR 549
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
3461-3875 1.48e-13

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 77.99  E-value: 1.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3461 RCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFV 3539
Cdd:PRK08751    25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3540 PLDPDHPAS--RHEEIFEQTGAQVVVASAQYSARWTSSSC---HVVT--VSKALSSQLPAVVD-------------STNT 3599
Cdd:PRK08751   105 NVNPLYTPRelKHQLIDSGASVLVVIDNFGTTVQQVIADTpvkQVITtgLGDMLGFPKAALVNfvvkyvkklvpeyRING 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3600 SVR-------------------PENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSR------VLQFASY 3654
Cdd:PRK08751   185 AIRfrealalgrkhsmptlqiePDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEegcevvITALPLY 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3655 TFDACIAEIITTLLCGGC---ICVPSD--------SDRRNSLAKAISTMdVNWAFLTPSVARLlDpglIPSLKILAIGG- 3722
Cdd:PRK08751   265 HIFALTANGLVFMKIGGCnhlISNPRDmpgfvkelKKTRFTAFTGVNTL-FNGLLNTPGFDQI-D---FSSLKMTLGGGm 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3723 --EQSSSADWNRWPGsVQKIHVYGPTECC-IFCTGYTTKQGFEPStIGTSVASVSWVVDpENHNRLAPLGSMGELLMEGP 3799
Cdd:PRK08751   340 avQRSVAERWKQVTG-LTLVEAYGLTETSpAACINPLTLKEYNGS-IGLPIPSTDACIK-DDAGTVLAIGEIGELCIKGP 416
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 3800 ILARGYLNDVDKTeAAFIDDPAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 3875
Cdd:PRK08751   417 QVMKGYWKRPEET-AKVMDADGWL---------------HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIE 476
PRK07798 PRK07798
acyl-CoA synthetase; Validated
1933-2343 1.48e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 78.00  E-value: 1.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 2012
Cdd:PRK07798     7 DLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2013 HPASRHEDIFRQTGAQVVVTSAQHSARWIGTNHQ------VVTVSAGSLEQFSTLVNP-----------VDLPAKPENAA 2075
Cdd:PRK07798    87 YVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRlpklrtLVVVEDGSGNDLLPGAVDyedalaagspeRDFGERSPDDL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2076 YVMFTSGSTGTPKGVVLEHRAVVTSCLGhGQAFGVTNLLRALQFTAY---------TFDVC-------IAEIITTLVHGG 2139
Cdd:PRK07798   167 YLLYTGGTTGMPKGVMWRQEDIFRVLLG-GRDFATGEPIEDEEELAKraaagpgmrRFPAPplmhgagQWAAFAALFSGQ 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2140 CICVPSDSE-RRDNLAKAITDMQVNWGYLT-SSVAR-LLD------PCLVPSLKVLVLGGEQVNST---DWGKWPSSVQT 2207
Cdd:PRK07798   246 TVVLLPDVRfDADEVWRTIEREKVNVITIVgDAMARpLLDaleargPYDLSSLFAIASGGALFSPSvkeALLELLPNVVL 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2208 INGYGPTEccvfcTGYTGIQGFQSGNIGTSIASV----SWVVDPENHGRLAPlGS--IGELLVEGPIlARGYLNDVDKTQ 2281
Cdd:PRK07798   326 TDSIGSSE-----TGFGGSGTVAKGAVHTGGPRFtigpRTVVLDEDGNPVEP-GSgeIGWIARRGHI-PLGYYKDPEKTA 398
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 2282 AAFiddpawllegyPGHEGRqgRLYKTGDLVRYSSDGNLVCLGRkDSQ-VKVRGQRVELGEVE 2343
Cdd:PRK07798   399 ETF-----------PTIDGV--RYAIPGDRARVEADGTITLLGR-GSVcINTGGEKVFPEEVE 447
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
5625-6036 1.61e-13

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 77.92  E-value: 1.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5625 HDLFTEQAKARPHAPAI--CAWDGE---LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAF 5699
Cdd:cd05970     20 YDVVDAMAKEYPDKLALvwCDDAGEeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5700 VPldPDHPASRHEDTFRHTGAQV--VVTSAQhsarwiGTNHQVVTVSAGSLGQLSTLVN-----PVGL-----------P 5761
Cdd:cd05970    100 IP--ATHQLTAKDIVYRIESADIkmIVAIAE------DNIPEEIEKAAPECPSKPKLVWvgdpvPEGWidfrkliknasP 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5762 AIP----------ENAVYIMFTSGSTGIPKGVvlEH-------RAVVTSCWGRGRAFGitnlsRVLQFASYTFDACMDEI 5824
Cdd:cd05970    172 DFErptansypcgEDILLVYFSSGTTGMPKMV--EHdftyplgHIVTAKYWQNVREGG-----LHLTVADTGWGKAVWGK 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5825 ITTLMYGGCICVPSDSDR--RNDLVKAISTMDVSCALLTPSVARLL-----EPSSVPTLQMLVLQGEQVSFADWNRWPA- 5896
Cdd:cd05970    245 IYGQWIAGAAVFVYDYDKfdPKALLEKLSKYGVTTFCAPPTIYRFLiredlSRYDLSSLRYCTTAGEALNPEVFNTFKEk 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5897 -SVQTINGYGPTECSICCNTYSGKQGfKSGIIGTSvaSVSWVVDPENHD-RLAPLGSIGELLV---EG-PI-LARGYLND 5969
Cdd:cd05970    325 tGIKLMEGFGQTETTLTIATFPWMEP-KPGSMGKP--APGYEIDLIDREgRSCEAGEEGEIVIrtsKGkPVgLFGGYYKD 401
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 5970 IQKTAAVFIDdpawlleGYpghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVE 6036
Cdd:cd05970    402 AEKTAEVWHD-------GY----------YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVE 451
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
309-377 1.62e-13

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 69.50  E-value: 1.62e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  309 PSTEAERTMQQLWARVLGIEPDSIGLDDSFFR-LGGDSIAAIKLVGEAR-RTGLQPSVADIFRHPTLAALA 377
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEeEFGIELPDTELFEYPTVADLA 72
PRK07798 PRK07798
acyl-CoA synthetase; Validated
854-1253 1.83e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 77.62  E-value: 1.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 933
Cdd:PRK07798     5 IADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 PGHPASRHEEIFKQIGAQVVLTSSQHAMLFA------SSERHQVTVSKVSTS-QLPTVVNF----AKSPVDPGNTA---- 998
Cdd:PRK07798    85 YRYVEDELRYLLDDSDAVALVYEREFAPRVAevlprlPKLRTLVVVEDGSGNdLLPGAVDYedalAAGSPERDFGErspd 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  999 --YIIFTSGTTGIPKGVVLQHRAVTTSCLGhGEAFG-------YTDHARVLQ--FASYTFDAC-------IAEIITTLLY 1060
Cdd:PRK07798   165 dlYLLYTGGTTGMPKGVMWRQEDIFRVLLG-GRDFAtgepiedEEELAKRAAagPGMRRFPAPplmhgagQWAAFAALFS 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1061 GGCICVPseSDRRNNLAKAISTMD---VNCALLT------PSVARLLEPSA--VPSLKRLVLQGEQVSFA---DWNRWPG 1126
Cdd:PRK07798   244 GQTVVLL--PDVRFDADEVWRTIErekVNVITIVgdamarPLLDALEARGPydLSSLFAIASGGALFSPSvkeALLELLP 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1127 SVQTINGYGPTECSVCCNTYSGKQGFKSGIIGTSVASLSWVVDAgNHNRLAPlGS--IGELLVEGPIlARGYLNDIDKTE 1204
Cdd:PRK07798   322 NVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRTVVLDE-DGNPVEP-GSgeIGWIARRGHI-PLGYYKDPEKTA 398
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 1205 AAF--IDdpawllegyeghaGRRGRLykTGDLVRCDADGNLVCLGRkDSQV 1253
Cdd:PRK07798   399 ETFptID-------------GVRYAI--PGDRARVEADGTITLLGR-GSVC 433
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
5647-6102 1.93e-13

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 77.51  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5647 ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVV-VT 5725
Cdd:cd05932      6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALfVG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5726 SAQHsarWIGTNHQV----VTVSAGSLG------QLSTLVN---PVG--LPAIPENAVYIMFTSGSTGIPKGVVLEHRAV 5790
Cdd:cd05932     86 KLDD---WKAMAPGVpeglISISLPPPSaancqyQWDDLIAqhpPLEerPTRFPEQLATLIYTSGTTGQPKGVMLTFGSF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5791 VTSCWGRGRAFGITNLSRVLqfaSYTFDACMDE---IITTLMYGGCICVPSDSDRR--NDLVKAISTMDVSCALL----- 5860
Cdd:cd05932    163 AWAAQAGIEHIGTEENDRML---SYLPLAHVTErvfVEGGSLYGGVLVAFAESLDTfvEDVQRARPTLFFSVPRLwtkfq 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5861 ------TPsVARLLEPSSVPTLQMLV----LQG---EQVSFA------------DWNRwPASVQTINGYGPTE-CSICCN 5914
Cdd:cd05932    240 qgvqdkIP-QQKLNLLLKIPVVNSLVkrkvLKGlglDQCRLAgcgsapvppallEWYR-SLGLNILEAYGMTEnFAYSHL 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5915 TYSGKQgfKSGIIGTSVASVSWVVDPEnhdrlaplgsiGELLVEGPILARGYLNDIQKTAAVFIDDpAWLlegypghpgr 5994
Cdd:cd05932    318 NYPGRD--KIGTVGNAGPGVEVRISED-----------GEILVRSPALMMGYYKDPEATAEAFTAD-GFL---------- 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5995 qgrlyKTGDLVRYDANGNLVCLGRKDSQVKL-RGQRVELGEVEH------HVREC------LPEARQLAVeviLPSGQKD 6061
Cdd:cd05932    374 -----RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENklaehdRVEMVcvigsgLPAPLALVV---LSEEARL 445
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 6062 HAMLAAFVQLEEGTQnALLDKEASGEDSMAQVVFLASVEEE 6102
Cdd:cd05932    446 RADAFARAELEASLR-AHLARVNSTLDSHEQLAGIVVVKDP 485
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
5622-6138 1.93e-13

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 77.79  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5622 RCVHDLFTEQAKARPHAPAICAWDGE------LTYGELDALSSKLAGHLTQLGVKPEDMVPlCFEKSMWTVVAM-LAVLK 5694
Cdd:PRK13295    24 RTINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVS-CQLPNWWEFTVLyLACSR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5695 AGGAFVPLDPDHpaSRHEDTF--RHTGAQVVVTSAQ-----HSA-------RWIGTNHQVVTVSAGSLGQLSTLVNPV-- 5758
Cdd:PRK13295   103 IGAVLNPLMPIF--RERELSFmlKHAESKVLVVPKTfrgfdHAAmarrlrpELPALRHVVVVGGDGADSFEALLITPAwe 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5759 ---GLPAI-------PENAVYIMFTSGSTGIPKGVVLEHRAVVTscwgrgrafGITNLSRVLQFASytfdacmDEII--- 5825
Cdd:PRK13295   181 qepDAPAIlarlrpgPDDVTQLIYTSGTTGEPKGVMHTANTLMA---------NIVPYAERLGLGA-------DDVIlma 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5826 ------TTLMYG-------GCICVPSDS---DRRNDLVK--AISTMDVSCALLTPSV-ARLLEPSSVPTLQMLVLQGEQV 5886
Cdd:PRK13295   245 spmahqTGFMYGlmmpvmlGATAVLQDIwdpARAAELIRteGVTFTMASTPFLTDLTrAVKESGRPVSSLRTFLCAGAPI 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5887 SFA----DWNRWPASVqtINGYGPTECSICCNTYSGKQGFKSgiIGTSVASVSW----VVDPENHDrlAPLGSIGELLVE 5958
Cdd:PRK13295   325 PGAlverARAALGAKI--VSAWGMTENGAVTLTKLDDPDERA--STTDGCPLPGvevrVVDADGAP--LPAGQIGRLQVR 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5959 GPILARGYLNDIQKTAavfIDDPAWllegypghpgrqgrlYKTGDLVRYDANGNLVCLGR-KDsqVKLRG-QRVELGEVE 6036
Cdd:PRK13295   399 GCSNFGGYLKRPQLNG---TDADGW---------------FDTGDLARIDADGYIRISGRsKD--VIIRGgENIPVVEIE 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6037 ----HHvreclPEARQLAVeVILPS---GQKdhamLAAFVQLEEGtqnalldkeaSGEDSMAQVVFLASveEELAKR-LP 6108
Cdd:PRK13295   459 allyRH-----PAIAQVAI-VAYPDerlGER----ACAFVVPRPG----------QSLDFEEMVEFLKA--QKVAKQyIP 516
                          570       580       590
                   ....*....|....*....|....*....|
gi 1820002560 6109 EHMVptVFFSLlhfPTTTSGKTDRKRLREI 6138
Cdd:PRK13295   517 ERLV--VRDAL---PRTPSGKIQKFRLREM 541
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
7613-7774 1.99e-13

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 77.22  E-value: 1.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7613 FAEQaraRPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHP 7692
Cdd:PRK09029    12 WAQV---RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7693 ASRHEEIFEqtgaqvvvasaQYSARWTSSSCHVVTVSKALSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEH 7772
Cdd:PRK09029    89 QPLLEELLP-----------SLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTA 157

                   ..
gi 1820002560 7773 RA 7774
Cdd:PRK09029   158 QA 159
PRK07514 PRK07514
malonyl-CoA synthase; Validated
1939-2095 2.23e-13

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 77.22  E-value: 2.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 2017
Cdd:PRK07514    12 AFADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2018 HEDIFRQTGAQVVVTsAQHSARWI-------GTNHqVVTVSA---GSLEQFSTLVNP--VDLPAKPENAAYVMFTSGSTG 2085
Cdd:PRK07514    92 LDYFIGDAEPALVVC-DPANFAWLskiaaaaGAPH-VETLDAdgtGSLLEAAAAAPDdfETVPRGADDLAAILYTSGTTG 169
                          170
                   ....*....|
gi 1820002560 2086 TPKGVVLEHR 2095
Cdd:PRK07514   170 RSKGAMLSHG 179
PRK07788 PRK07788
acyl-CoA synthetase; Validated
1939-2090 2.37e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 77.27  E-value: 2.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 2018
Cdd:PRK07788    59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2019 EDIFRQTGAQVVVTSAQHSAR-------------WIG--TNHQVVTVSAGSLEQFSTLVNPVDLPAKPENAAYVMFTSGS 2083
Cdd:PRK07788   139 AEVAAREGVKALVYDDEFTDLlsalppdlgrlraWGGnpDDDEPSGSTDETLDDLIAGSSTAPLPKPPKPGGIVILTSGT 218

                   ....*..
gi 1820002560 2084 TGTPKGV 2090
Cdd:PRK07788   219 TGTPKGA 225
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
5222-5490 2.75e-13

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 76.53  E-value: 2.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5222 VLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVE-----EKIQWTESK----RLEEYLREDKAVSMGLG 5292
Cdd:cd20483     29 VCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDpsfhlIVIDLSEAAdpeaALDQLVRNLRRQELDIE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5293 D-RLARYALIKEPYDggkRW-FVWTIHHALYDGWSLPRILQAVKQIYSGAVPER------QPSFNaFIQY-LGQQDLEAA 5363
Cdd:cd20483    109 EgEVIRGWLVKLPDE---EFaLVLASHHIAWDRGSSKSIFEQFTALYDALRAGRdlatvpPPPVQ-YIDFtLWHNALLQS 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5364 TL------YWQTALADckaalfptLPPTVT-QPVADTTVeyqcPPPSQSATDITTSTL---------------------- 5414
Cdd:cd20483    185 PLvqplldFWKEKLEG--------IPDASKlLPFAKAER----PPVKDYERSTVEATLdkellarmkricaqhavtpfmf 252
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 5415 VRAAWAIVTSRYTSSDDVVFGatVTGRNAPIAGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAHEQ 5490
Cdd:cd20483    253 LLAAFRAFLYRYTEDEDLTIG--MVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSA 326
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
23-184 2.87e-13

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 77.02  E-value: 2.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRWPSSVQT--INGYGPTECCIVCTGYTSEQDFTTGTIGTSIASVS-WVVDpkDHGRLAPLGS 99
Cdd:PRK08974   326 SLKLSVGGGMAVQQAVAERWVKLTGQylLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEiKLVD--DDGNEVPPGE 403
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  100 VGELLVEGPILARGYLSDPEKTAAVFINnpAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVE 179
Cdd:PRK08974   404 PGELWVKGPQVMLGYWQRPEATDEVIKD--GWL---------------ATGDIAVMDEEGFLRIVDRKKDMILVSGFNVY 466

                   ....*
gi 1820002560  180 LGEVE 184
Cdd:PRK08974   467 PNEIE 471
PLN02246 PLN02246
4-coumarate--CoA ligase
1932-2100 2.88e-13

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 76.94  E-value: 2.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1932 HDLFTEQAKARPHAPaiCAWDGE----LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFV 2007
Cdd:PLN02246    26 HDYCFERLSEFSDRP--CLIDGAtgrvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2008 PLDPDHPASRHEDIFRQTGAQVVVTSAQHSARWIGTNH----QVVTVSA---GSLEqFSTLVNP--VDLPA---KPENAA 2075
Cdd:PLN02246   104 TANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEddgvTVVTIDDppeGCLH-FSELTQAdeNELPEveiSPDDVV 182
                          170       180
                   ....*....|....*....|....*
gi 1820002560 2076 YVMFTSGSTGTPKGVVLEHRAVVTS 2100
Cdd:PLN02246   183 ALPYSSGTTGLPKGVMLTHKGLVTS 207
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
854-1241 3.14e-13

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 77.22  E-value: 3.14e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGG--AFV- 930
Cdd:PRK08279    39 LGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLn 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  931 ------PL-------DPGHPASRHE--EIFKQIGAQVvltSSQHAMLFASSE--RHQVTVSKVST--SQLPTVVNFAKSP 991
Cdd:PRK08279   119 tqqrgaVLahslnlvDAKHLIVGEElvEAFEEARADL---ARPPRLWVAGGDtlDDPEGYEDLAAaaAGAPTTNPASRSG 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  992 VDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSclghGEAFGYTDHAR-----------------------VL-------- 1040
Cdd:PRK08279   196 VTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKA----MGGFGGLLRLTpddvlycclplyhntggtvawssVLaagatlal 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1041 --QF-ASYTFDACIAEIITTLLYGGCIC------VPSESDRRNNLAKAIStmdvncALLTPSVarllepsavpslkrlvl 1111
Cdd:PRK08279   272 rrKFsASRFWDDVRRYRATAFQYIGELCryllnqPPKPTDRDHRLRLMIG------NGLRPDI----------------- 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1112 qgeqvsfadWNRWP---GSVQTINGYGPTECSVC-CN--TYSGKQGFKSGIIGTSVASLSWVVDAGNHNR-------LAP 1178
Cdd:PRK08279   329 ---------WDEFQqrfGIPRILEFYAASEGNVGfINvfNFDGTVGRVPLWLAHPYAIVKYDVDTGEPVRdadgrciKVK 399
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 1179 LGSIGELLveGPILAR----GYlNDIDKTEA-----AFIDDPAWllegyeghagrrgrlYKTGDLVRCDADG 1241
Cdd:PRK08279   400 PGEVGLLI--GRITDRgpfdGY-TDPEASEKkilrdVFKKGDAW---------------FNTGDLMRDDGFG 453
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
22-280 3.15e-13

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 76.49  E-value: 3.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   22 PSLRILVMGG----EQVNSADWDRWPSSVQtinGYGPTECCIVCTGYTSE-QDFTTGTIGTSIASVSW-VVDPkdHGRLA 95
Cdd:cd17631    213 SSLRAVIYGGapmpERLLRALQARGVKFVQ---GYGMTETSPGVTFLSPEdHRRKLGSAGRPVFFVEVrIVDP--DGREV 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   96 PLGSVGELLVEGPILARGYLSDPEKTAAVFINnpAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRG 175
Cdd:cd17631    288 PPGEVGEIVVRGPHVMAGYWNRPEATAAAFRD--GWF---------------HTGDLGRLDEDGYLYIVDRKKDMIISGG 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  176 QRVELGEVEH----H--VREC----LPEAKQlaVEVVlplgqknhatlAAFIQLDKGThnallkeKVGGDDSIARvvfla 245
Cdd:cd17631    351 ENVYPAEVEDvlyeHpaVAEVavigVPDEKW--GEAV-----------VAVVVPRPGA-------ELDEDELIAH----- 405
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1820002560  246 gVEEELAK-RLPKHmvptVFF--ALlhfPTTTSGKTDR 280
Cdd:cd17631    406 -CRERLARyKIPKS----VEFvdAL---PRNATGKILK 435
PLN02574 PLN02574
4-coumarate--CoA ligase-like
5633-6036 4.66e-13

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 76.42  E-value: 4.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5633 KARPHAPA-ICAWDGE-LTYGELDALSSKLAGHLTQ-LGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 5709
Cdd:PLN02574    50 HNHNGDTAlIDSSTGFsISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLG 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5710 RHEDTFRHTGAQVVVTSAQHSARWIGTNHQVVTVS------------AGSLGQLSTLVNPVGLPAIPE-NAVYIMFTSGS 5776
Cdd:PLN02574   130 EIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPenydfdskriefPKFYELIKEDFDFVPKPVIKQdDVAAIMYSSGT 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5777 TGIPKGVVLEHRAVVTScwgrgrafgiTNLSRVLQFASYTFDACMDEIITTL----MYG-----------GCICVPSDSD 5841
Cdd:PLN02574   210 TGASKGVVLTHRNLIAM----------VELFVRFEASQYEYPGSDNVYLAALpmfhIYGlslfvvgllslGSTIVVMRRF 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5842 RRNDLVKAISTMDVSCALLTPSVARLLEPSSVPTLQMLVLQGEQVS----------FADWNRWPASVQTINGYGPTEcsi 5911
Cdd:PLN02574   280 DASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVScgaaplsgkfIQDFVQTLPHVDFIQGYGMTE--- 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5912 ccNTYSGKQGFKS---------GIIGTSVASVswVVDPENHDRLAPlGSIGELLVEGPILARGYLNDIQKTAAVFIDDpA 5982
Cdd:PLN02574   357 --STAVGTRGFNTeklskyssvGLLAPNMQAK--VVDWSTGCLLPP-GNCGELWIQGPGVMKGYLNNPKATQSTIDKD-G 430
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 5983 WLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVE 6036
Cdd:PLN02574   431 WL---------------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLE 469
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1933-2444 4.82e-13

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 76.25  E-value: 4.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFtEQAKAR-PHAPAICAWDGELTYGELDALSSKLASHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 2010
Cdd:PRK08974    27 DMF-EQAVARyADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVN 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2011 PDHPASRHEDIFRQTGAQ--VVVTSAQHSARWIGTNHQVVTVSAGSL-EQFS----TLVNPV-----------DLP---- 2068
Cdd:PRK08974   106 PLYTPRELEHQLNDSGAKaiVIVSNFAHTLEKVVFKTPVKHVILTRMgDQLStakgTLVNFVvkyikrlvpkyHLPdais 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2069 -------------AKP----ENAAYVMFTSGSTGTPKGVVLEHRAVVTSC----------LGHGQAFGVTNL----LRAL 2117
Cdd:PRK08974   186 frsalhkgrrmqyVKPelvpEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqakaaygplLHPGKELVVTALplyhIFAL 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2118 QFTAYTFdvcIAEIITTLVhggcICVPSD-----SERRDNLAKAITDmqVNW---GYLTSSVARLLDpclVPSLKVLVLG 2189
Cdd:PRK08974   266 TVNCLLF---IELGGQNLL----ITNPRDipgfvKELKKYPFTAITG--VNTlfnALLNNEEFQELD---FSSLKLSVGG 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2190 GEQVNSTDWGKWPSSVQT--INGYGPTECCVFCTGYTGIQGFQSGNIGTSIASVS-WVVDPEnhGRLAPLGSIGELLVEG 2266
Cdd:PRK08974   334 GMAVQQAVAERWVKLTGQylLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEiKLVDDD--GNEVPPGEPGELWVKG 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2267 PILARGYLNDVDKTqAAFIDDpAWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVE--- 2343
Cdd:PRK08974   412 PQVMLGYWQRPEAT-DEVIKD-GWL---------------ATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEdvv 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2344 -HHmrkclPEANQLAVEVVPP--SGErdhaMLAAFIRLDDETrnspliikyaednstaqivfLTgiEEELSERLPQHM-- 2418
Cdd:PRK08974   475 mLH-----PKVLEVAAVGVPSevSGE----AVKIFVVKKDPS--------------------LT--EEELITHCRRHLtg 523
                          570       580       590
                   ....*....|....*....|....*....|..
gi 1820002560 2419 --VPTvffaLVHF----PTTTSGKTDRKRLRE 2444
Cdd:PRK08974   524 ykVPK----LVEFrdelPKSNVGKILRRELRD 551
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
7633-8021 5.77e-13

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 75.86  E-value: 5.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVasa 7712
Cdd:cd17640      6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7713 qysarwtssschvvtvskalssqlpavVDStntsvRPENAAYIIFTSGSTGVPKGVVLEHRAVAtsclghgraFGITNLS 7792
Cdd:cd17640     83 ---------------------------VEN-----DSDDLATIIYTSGTTGNPKGVMLTHANLL---------HQIRSLS 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7793 ---------RVLQF----------ASYTFDAC-IAEIITTLlcggcICVPSDSDRRN------------SLAKAISTMDV 7840
Cdd:cd17640    122 divppqpgdRFLSIlpiwhsyersAEYFIFACgCSQAYTSI-----RTLKDDLKRVKphyivsvprlweSLYSGIQKQVS 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7841 NWAFLTPSVARLLDPGLIpsLKILAIGGeqsssadwNRWPGSVQK------IHV---YGPTECcifcTGYTTKQGFEPST 7911
Cdd:cd17640    197 KSSPIKQFLFLFFLSGGI--FKFGISGG--------GALPPHVDTffeaigIEVlngYGLTET----SPVVSARRLKCNV 262
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7912 IGTSVA----SVSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTG 7987
Cdd:cd17640    263 RGSVGRplpgTEIKIVDPEGNVVLPP-GEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDGWF---------------NTG 325
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1820002560 7988 DLVQYNADGNLVYLGR-KDSQVKVRGQRVELGEVE 8021
Cdd:cd17640    326 DLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIE 360
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
4141-4409 5.88e-13

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 75.37  E-value: 5.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4141 VLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELGLLQVVVE-----ERIQWTES----ESLEEYPREDKAVSMGVG 4211
Cdd:cd20483     29 VCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDpsfhlIVIDLSEAadpeAALDQLVRNLRRQELDIE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4212 D-RLARYALIKEPYDggkRW-FVWTMHHALYDGWSLPRILHAVKQAYSGVVLER------QPSFNaFIQY-------LSQ 4276
Cdd:cd20483    109 EgEVIRGWLVKLPDE---EFaLVLASHHIAWDRGSSKSIFEQFTALYDALRAGRdlatvpPPPVQ-YIDFtlwhnalLQS 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4277 QDPEAAAAYWQTALVDckaalfptLPPTVT-QPVADTTVeyqcPPPSQSATDITTSTL-----AR--------------- 4335
Cdd:cd20483    185 PLVQPLLDFWKEKLEG--------IPDASKlLPFAKAER----PPVKDYERSTVEATLdkellARmkricaqhavtpfmf 252
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 4336 --AAWAIVTSRYTSSDDVVFGatVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQATDMIAHEQ 4409
Cdd:cd20483    253 llAAFRAFLYRYTEDEDLTIG--MVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSA 326
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
2243-2537 6.47e-13

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 73.63  E-value: 6.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2243 WVVDPENHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPAwlleGYPGHEGRQGRLYKTGDLVRYSSDGNLvc 2322
Cdd:COG3433     23 AIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPF----IPVPYPAQPGRQADDLRLLLRRGLGPG-- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2323 lGRKDSQVKVRGQRVELGEVEHHMRKCLPEANQLAVEVVppsgerdhamlaafiRLDDETRNSPLIIKYAEDNSTAQIvf 2402
Cdd:COG3433     97 -GGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLA---------------ALRGAGVGLLLIVGAVAALDGLAA-- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2403 ltgiEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREIGASFTAQQLAEmrTSSEGPKRQPSTEAErtMQQLWAQ 2482
Cdd:COG3433    159 ----AAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAA--ASPAPALETALTEEE--LRADVAE 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 2483 VLGIELESIGLDDSFFRLGGDSITAMQISSSARALHLSVSTGDILKKKTIALIAR 2537
Cdd:COG3433    231 LLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWA 285
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1532-1799 6.90e-13

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 75.37  E-value: 6.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1532 VLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQVVIEENIQWT--------EP-KSLEEYLSEDKAVSVGLG 1602
Cdd:cd20483     29 VCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIvidlseaaDPeAALDQLVRNLRRQELDIE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1603 D-PLARYAFVKEACGGKRwFVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQW------QPSFNaFIQY-------LGQQD 1668
Cdd:cd20483    109 EgEVIRGWLVKLPDEEFA-LVLASHHIAWDRGSSKSIFEQFTALYDALRAGRdlatvpPPPVQ-YIDFtlwhnalLQSPL 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1669 LEATVAYWQTALADCEAVLfPTLP------PTVTQPvADATVEYQCPP-LSK------ATSDTTTSTLIRAAWAIVTSRY 1735
Cdd:cd20483    187 VQPLLDFWKEKLEGIPDAS-KLLPfakaerPPVKDY-ERSTVEATLDKeLLArmkricAQHAVTPFMFLLAAFRAFLYRY 264
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 1736 TTSDDVVFGttVTGRNTPVTGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAHEQ 1799
Cdd:cd20483    265 TEDEDLTIG--MVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSA 326
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
857-1487 7.12e-13

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 76.22  E-value: 7.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  857 LFAEQARAR--PDASAVCAWDgELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAG-GAFVPLD 933
Cdd:PRK06060     9 LLAEQASEAgwYDRPAFYAAD-VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGvMAFLANP 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 PGHpasRHEEIFKQ--IGAQVVLTSSQHAMLFASSerhQVTVSKVSTSQLPTVVNFAKSPVDPGNTAYIIFTSGTTGIPK 1011
Cdd:PRK06060    88 ELH---RDDHALAArnTEPALVVTSDALRDRFQPS---RVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1012 GVVlqHRavttsclgHGEAFGYTDH--ARVLQFASYTFDACIAEIITTLLYGGCICVP---SESDRRNNLAKAISTMDVN 1086
Cdd:PRK06060   162 AAI--HR--------HADPLTFVDAmcRKALRLTPEDTGLCSARMYFAYGLGNSVWFPlatGGSAVINSAPVTPEAAAIL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1087 CALLTPSV--------ARLLE---PSAVPSLKRLVLQGEQVSFADWNR---WPGSVQTINGYGPTECSvccntysgkQGF 1152
Cdd:PRK06060   232 SARFGPSVlygvpnffARVIDscsPDSFRSLRCVVSAGEALELGLAERlmeFFGGIPILDGIGSTEVG---------QTF 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1153 KSGIIGT-SVASLSWVVDAGNHNRLAPLGSI------GELLVEGPILARGYLNDIDkteaAFIDDPAWLlegyeghagrr 1225
Cdd:PRK06060   303 VSNRVDEwRLGTLGRVLPPYEIRVVAPDGTTagpgveGDLWVRGPAIAKGYWNRPD----SPVANEGWL----------- 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1226 grlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVRECLPEARQLAVEVILPSGQkehALLAAFIQldkgn 1305
Cdd:PRK06060   368 ----DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGA---STLQAFLV----- 435
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1306 hnalfeeKASGEDSMAQVvfLTGVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRLQDIGASFTVQQLAEMRTSSQ 1385
Cdd:PRK06060   436 -------ATSGATIDGSV--MRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSG 506
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1386 GPKR-----------QPSTEVEQTMQQLWAQV------LSIE--------------PNSIGLDDSFFRLGGDSIVAMKLV 1434
Cdd:PRK06060   507 VRAQrddlsasnmtiAGGNDGGATLRERLVALrqerqrLVVDavcaeaakmlgepdPWSVDQDLAFSELGFDSQMTVTLC 586
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 1435 GE-ARRTGLQLSVADIFRHPRLVDLARVQNSQFS----------SAAEEVPAFSLLGEDVNAVQ 1487
Cdd:PRK06060   587 KRlAAVTGLRLPETVGWDYGSISGLAQYLEAELAgghgrlksagPVNSGATGLWAIEEQLNKVE 650
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
6853-7042 7.78e-13

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 75.48  E-value: 7.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6853 GSIGELLVEGPILARGYLNDADKTAAAFVndpawlveghgkhpgrrGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQR 6932
Cdd:cd05959    356 GEPGELYVRGPSSATMYWNNRDKTRDTFQ-----------------GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIW 418
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6933 VELGEIENRLREcMPRATQMAVevispAGAA-EQAKTMVVAFLQLNDEARDallggnvpnddnlsaQVVFPAKVDEKLSN 7011
Cdd:cd05959    419 VSPFEVESALVQ-HPAVLEAAV-----VGVEdEDGLTKPKAFVVLRPGYED---------------SEALEEELKEFVKD 477
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1820002560 7012 LLPSYMMPEVYFAVPQLPMMISGKTDRKRLR 7042
Cdd:cd05959    478 RLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
6842-7055 8.20e-13

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 76.50  E-value: 8.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAfvndpawLVEGHGKhpgrrgRLYKTGDLVYYNKDGNLVYIGR 6921
Cdd:PRK08633   974 VDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEV-------IKDIDGI------GWYVTGDKGHLDEDGFLTITDR 1040
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 KDGQVKVRGQRVELGEIENRLRECMP-RATQMAVEVISPAGAAEQaktMVVAFLQLNDEardallggnvpnddnlsaqvv 7000
Cdd:PRK08633  1041 YSRFAKIGGEMVPLGAVEEELAKALGgEEVVFAVTAVPDEKKGEK---LVVLHTCGAED--------------------- 1096
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 7001 fPAKVDEKLSNL-LPSYMMPEVYFAVPQLPMMISGKTDRKRLREIgasftAQQLAE 7055
Cdd:PRK08633  1097 -VEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL-----ALALLG 1146
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
5649-6137 8.56e-13

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 75.40  E-value: 8.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5649 TYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSAQ 5728
Cdd:PLN02330    57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5729 HSARWIGTNHQVVTVSAGSLGQL--------------STLVNPV----GLPAIPenavyimFTSGSTGIPKGVVLEHRAV 5790
Cdd:PLN02330   137 NYGKVKGLGLPVIVLGEEKIEGAvnwkelleaadragDTSDNEEilqtDLCALP-------FSSGTTGISKGVMLTHRNL 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5791 V----TSCWGRGRAF--GITNLSRVLQFASYTFDA-CmdeiITTLMYGGCICVPSDSDRRNdLVKAISTMDVSCALLTPS 5863
Cdd:PLN02330   210 VanlcSSLFSVGPEMigQVVTLGLIPFFHIYGITGiC----CATLRNKGKVVVMSRFELRT-FLNALITQEVSFAPIVPP 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5864 VARLLEPSSVPT---LQMLVLQGEQVSFADW---------NRWPaSVQTINGYGPTECSiCCNTYSGKQGFKSGIIGTSv 5931
Cdd:PLN02330   285 IILNLVKNPIVEefdLSKLKLQAIMTAAAPLapelltafeAKFP-GVQVQEAYGLTEHS-CITLTHGDPEKGHGIAKKN- 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5932 aSVSWV--------VDPENHDRLaPLGSIGELLVEGPILARGYLNDIQKTAAVfIDDPAWLlegypghpgrqgrlyKTGD 6003
Cdd:PLN02330   362 -SVGFIlpnlevkfIDPDTGRSL-PKNTPGELCVRSQCVMQGYYNNKEETDRT-IDEDGWL---------------HTGD 423
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6004 LVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhHVRECLPEARQLAVeVILPSGQKDHAMLAAFVQLEEGTQnalldke 6083
Cdd:PLN02330   424 IGYIDDDGDIFIVDRIKELIKYKGFQVAPAELE-AILLTHPSVEDAAV-VPLPDEEAGEIPAACVVINPKAKE------- 494
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 6084 aSGEDSMAqvvFLASVEEELAKRLPEHMVPTVffsllhfPTTTSGKTDRKRLRE 6137
Cdd:PLN02330   495 -SEEDILN---FVAANVAHYKKVRVVQFVDSI-------PKSLSGKIMRRLLKE 537
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
2-277 8.57e-13

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 75.33  E-value: 8.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPS-VARLLE-PSH----IPSLRILVMGGEQVNSADWDRWPSSVQT---INGYGPTECCIVCTgYTSEQDFTT 72
Cdd:cd05911    236 KITFLYLVPPiAAALAKsPLLdkydLSSLRVILSGGAPLSKELQELLAKRFPNatiKQGYGMTETGGILT-VNPDGDDKP 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   73 GTIGTSIASVSW-VVDPkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinnpawlleGHGGYagrqgrlYKTGD 151
Cdd:cd05911    315 GSVGRLLPNVEAkIVDD-DGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETF---------DEDGW-------LHTGD 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  152 LVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVeVVLPLGQKNHATlAAFIQLDKGthnALLKEK 231
Cdd:cd05911    378 IGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLE-HPGVADAAV-IGIPDEVSGELP-RAYVVRKPG---EKLTEK 451
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560  232 vggddsiarvvflaGVEEELAKRLP--KHMVPTVFFaLLHFPTTTSGK 277
Cdd:cd05911    452 --------------EVKDYVAKKVAsyKQLRGGVVF-VDEIPKSASGK 484
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
9-284 8.57e-13

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 75.07  E-value: 8.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    9 TPSVARLL---EPSH--IPSLRILVMGGEQVN--SADWDRWPSSVQTINGYGPTECCIVCtGYTSEQDFTTGTIGTSIAS 81
Cdd:cd05972    179 PPTAYRMLikqDLSSykFSHLRLVVSAGEPLNpeVIEWWRAATGLPIRDGYGQTETGLTV-GNFPDMPVKPGSMGRPTPG 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   82 -VSWVVDpkDHGRLAPLGSVGELLVE-GPI-LARGYLSDPEKTAAVFinnpawllegHGGYagrqgrlYKTGDLVRYDAD 158
Cdd:cd05972    258 yDVAIID--DDGRELPPGEEGDIAIKlPPPgLFLGYVGDPEKTEASI----------RGDY-------YLTGDRAYRDED 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  159 GNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAV---------EVVlplgqknhatlAAFIQLDKGthnallk 229
Cdd:cd05972    319 GYFWFVGRADDIIKSSGYRIGPFEVESALLE-HPAVAEAAVvgspdpvrgEVV-----------KAFVVLTSG------- 379
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560  230 ekVGGDDSIArvvflagveEELA----KRLPKHMVPTVFFALLHFPTTTSGKTDRKRLR 284
Cdd:cd05972    380 --YEPSEELA---------EELQghvkKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1397-1457 8.67e-13

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 66.43  E-value: 8.67e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 1397 QTMQQLWAQVLSIEPNSIGLDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADIFRHPRLVD 1457
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1946-2472 8.80e-13

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 75.84  E-value: 8.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1946 PAICAWDgELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDhpASRHEDIF--R 2023
Cdd:PRK06060    23 PAFYAAD-VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPE--LHRDDHALaaR 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2024 QTGAQVVVTSAQHSARWIGTNhqvvTVSAGSLEQFSTLVNPVDL-PAKPENAAYVMFTSGSTGTPKGVVleHRavvtscl 2102
Cdd:PRK06060   100 NTEPALVVTSDALRDRFQPSR----VAEAAELMSEAARVAPGGYePMGGDALAYATYTSGTTGPPKAAI--HR------- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2103 gHGQAFGVTNLL--RALQFTAYTFDVCIAEIITT----------LVHGGCICV---PSDSERRDNLAkAITDMQVNWGyL 2167
Cdd:PRK06060   167 -HADPLTFVDAMcrKALRLTPEDTGLCSARMYFAyglgnsvwfpLATGGSAVInsaPVTPEAAAILS-ARFGPSVLYG-V 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2168 TSSVARLLDPCLVP---SLKVLVLGGEQVN---STDWGKWPSSVQTINGYGPTEccvfcTGYT----GIQGFQSGNIGTS 2237
Cdd:PRK06060   244 PNFFARVIDSCSPDsfrSLRCVVSAGEALElglAERLMEFFGGIPILDGIGSTE-----VGQTfvsnRVDEWRLGTLGRV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2238 IASVSW-VVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDktqaAFIDDPAWLlegypghegrqgrlyKTGDLVRYSS 2316
Cdd:PRK06060   319 LPPYEIrVVAPD--GTTAGPGVEGDLWVRGPAIAKGYWNRPD----SPVANEGWL---------------DTRDRVCIDS 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2317 DGNLVCLGRKDSQVKVRGQRVELGEVEhhmrKCLPEANQLA-VEVVPPSGERDHAMLAAFIrlddetrnSPLIIKYAEDN 2395
Cdd:PRK06060   378 DGWVTYRCRADDTEVIGGVNVDPREVE----RLIIEDEAVAeAAVVAVRESTGASTLQAFL--------VATSGATIDGS 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2396 staqivFLTGIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREIGASFTAQQLAEMRTSSEGPKR---QPSTEA 2472
Cdd:PRK06060   446 ------VMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSGVRAQrddLSASNM 519
PRK07514 PRK07514
malonyl-CoA synthase; Validated
3471-3859 9.11e-13

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 75.30  E-value: 9.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 3549
Cdd:PRK07514    12 AFADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3550 HEEIFEQTGAQVVVAS-----------AQYSARwtssscHVVTV----SKALSSQLPAVVDSTNTSVR-PENAAYIIFTS 3613
Cdd:PRK07514    92 LDYFIGDAEPALVVCDpanfawlskiaAAAGAP------HVETLdadgTGSLLEAAAAAPDDFETVPRgADDLAAILYTS 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3614 GSTGVPKGVVLEHRAVATSCLGHGRAFGITNlSRVLQFASYTFDA---CIAeIITTLLCGG-CICVPS-DSDR-RNSLAK 3687
Cdd:PRK07514   166 GTTGRSKGAMLSHGNLLSNALTLVDYWRFTP-DDVLIHALPIFHThglFVA-TNVALLAGAsMIFLPKfDPDAvLALMPR 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3688 AISTMDVNwAFLTpsvaRLL-DPGLIPSLKI---LAIGGeqssSA--------DWNRWPGsvqkiHV----YGPTEccif 3751
Cdd:PRK07514   244 ATVMMGVP-TFYT----RLLqEPRLTREAAAhmrLFISG----SApllaethrEFQERTG-----HAilerYGMTE---- 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3752 cTGYTTKQGFE----PSTIGTSVASVSW-VVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawlleG 3826
Cdd:PRK07514   306 -TNMNTSNPYDgerrAGTVGFPLPGVSLrVTDPETGAELPP-GEIGMIEVKGPNVFKGYWRMPEKTAEEFRAD------G 377
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1820002560 3827 YpghpgrqgrlYKTGDLVQYNADGNLVYLGR-KD 3859
Cdd:PRK07514   378 F----------FITGDLGKIDERGYVHIVGRgKD 401
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
982-1361 9.25e-13

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 76.16  E-value: 9.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  982 PTVVNFAKSPVDPgntAYIIFTSGTTGIPKGVVLQHRAVTTSC--LGHGEAFGYTDhaRVLQ----FASYTFDAciAEII 1055
Cdd:PRK06814   783 PLVYFCNRDPDDP---AVILFTSGSEGTPKGVVLSHRNLLANRaqVAARIDFSPED--KVFNalpvFHSFGLTG--GLVL 855
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1056 TTL------LYggcicvPSESDRRnnlakAISTM--DVNCALL--TPSV----ARLLEPSAVPSLkRLVLQG-EQVSFAD 1120
Cdd:PRK06814   856 PLLsgvkvfLY------PSPLHYR-----IIPELiyDTNATILfgTDTFlngyARYAHPYDFRSL-RYVFAGaEKVKEET 923
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1121 WNRWPGS--VQTINGYGPTECS--VCCNTysgKQGFKSGiigtSVASLSwvvdAGNHNRLAPLGSI---GELLVEGPILA 1193
Cdd:PRK06814   924 RQTWMEKfgIRILEGYGVTETApvIALNT---PMHNKAG----TVGRLL----PGIEYRLEPVPGIdegGRLFVRGPNVM 992
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1194 RGYLndidKTEAAFIDDPawLLEGYeghagrrgrlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVRECL 1273
Cdd:PRK06814   993 LGYL----RAENPGVLEP--PADGW----------YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELW 1056
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1274 PEARQLAVEVilPSGQKEHALLaafiqldkgnhnaLFEEKASGEdsmaQVVFLTGVEeelAKRLPEHMVPTILFTVKAMP 1353
Cdd:PRK06814  1057 PDALHAAVSI--PDARKGERII-------------LLTTASDAT----RAAFLAHAK---AAGASELMVPAEIITIDEIP 1114

                   ....*...
gi 1820002560 1354 ITTSGKID 1361
Cdd:PRK06814  1115 LLGTGKID 1122
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
23-284 1.04e-12

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 75.10  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRWPS--SVQTINGYGPTECC-IVCTGYTSEQDF-TTGTI--GTSIAsvswVVDpkDHGRLAP 96
Cdd:cd05959    281 SLRLCVSAGEALPAEVGERWKArfGLDILDGIGSTEMLhIFLSNRPGRVRYgTTGKPvpGYEVE----LRD--EDGGDVA 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   97 LGSVGELLVEGPILARGYLSDPEKTAAVFinnpawlleghggyagrQGRLYKTGDLVRYDADGNLVCLGRKDSQVKLRGQ 176
Cdd:cd05959    355 DGEPGELYVRGPSSATMYWNNRDKTRDTF-----------------QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGI 417
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  177 RVELGEVEhhvrECLPEAKQLAVEVVLPLGQKNHAT-LAAFIQLDKG-THNALLKEkvggddsiarvvflaGVEEELAKR 254
Cdd:cd05959    418 WVSPFEVE----SALVQHPAVLEAAVVGVEDEDGLTkPKAFVVLRPGyEDSEALEE---------------ELKEFVKDR 478
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1820002560  255 LPKHMVP--TVFFALLhfPTTTSGKTDRKRLR 284
Cdd:cd05959    479 LAPYKYPrwIVFVDEL--PKTATGKIQRFKLR 508
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
21-285 1.08e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 75.22  E-value: 1.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   21 IPSLRILVMGGEQVNSADWDRWPS--SVQTINGYGPTECC-IVCTGYTSEQDFTTGTI----GTSIASVSW-VVDPkDHG 92
Cdd:PRK06187   280 FSSLRLVIYGGAALPPALLREFKEkfGIDLVQGYGMTETSpVVSVLPPEDQLPGQWTKrrsaGRPLPGVEArIVDD-DGD 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   93 RLAPLG-SVGELLVEGPILARGYLSDPEKTAAVFINNpaWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQV 171
Cdd:PRK06187   359 ELPPDGgEVGEIIVRGPWLMQGYWNRPEATAETIDGG--WL---------------HTGDVGYIDEDGYLYITDRIKDVI 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  172 KLRGQRVELGEVE----HH--VREClpeakqlAV---------EVVLplgqknhatlaAFIQLDKGthnallkEKVGGDD 236
Cdd:PRK06187   422 ISGGENIYPRELEdalyGHpaVAEV-------AVigvpdekwgERPV-----------AVVVLKPG-------ATLDAKE 476
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560  237 SIArvvFLAGVeeeLAK-RLPKHM--VPTVffallhfPTTTSGKTDRKRLRE 285
Cdd:PRK06187   477 LRA---FLRGR---LAKfKLPKRIafVDEL-------PRTSVGKILKRVLRE 515
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
7611-8129 1.11e-12

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 75.03  E-value: 1.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARarPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPED--VVPLCFEKSMWtvVAMLAVLKAGgaFVPLD 7688
Cdd:PRK10946    29 DILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDtaLVQLGNVAEFY--ITFFALLKLG--VAPVN 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7689 PDHPASRHE--EIFEQTGAQVVVASAQYS-----------ARWTSSSCHVVTVSKALSSQLPAVV-----DSTNTSVRPE 7750
Cdd:PRK10946   103 ALFSHQRSElnAYASQIEPALLIADRQHAlfsdddflntlVAEHSSLRVVLLLNDDGEHSLDDAInhpaeDFTATPSPAD 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7751 NAAYIIFTSGSTGVPKGVVLEH-------RAVATSClghgrafGITNLSRVLQF--ASYTFDACIAEIITTLLCGGCICV 7821
Cdd:PRK10946   183 EVAFFQLSGGSTGTPKLIPRTHndyyysvRRSVEIC-------GFTPQTRYLCAlpAAHNYPMSSPGALGVFLAGGTVVL 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7822 PSDSDRRNSLAkAISTMDVNWAFLTPSVARL-----LDPG---LIPSLKILAIGGEQSSSADWNRWPGSV--QKIHVYGP 7891
Cdd:PRK10946   256 APDPSATLCFP-LIEKHQVNVTALVPPAVSLwlqaiAEGGsraQLASLKLLQVGGARLSETLARRIPAELgcQLQQVFGM 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7892 TECCIfctGYTTKQGFEPSTIGTSVASVS-----WVVDpENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFiDDp 7966
Cdd:PRK10946   335 AEGLV---NYTRLDDSDERIFTTQGRPMSpddevWVAD-ADGNPLPQ-GEVGRLMTRGPYTFRGYYKSPQHNASAF-DA- 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7967 awllEGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVreclpearqLAVEVILpsgqkn 8046
Cdd:PRK10946   408 ----NGF----------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLL---------LRHPAVI------ 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8047 HAMLAVfvqlgkgthiahLEEKAGGEDSMAqvvFLTGTEEELAKRLPKHM---------VPTVFFALLHFPMTTSGKADR 8117
Cdd:PRK10946   459 HAALVS------------MEDELMGEKSCA---FLVVKEPLKAVQLRRFLreqgiaefkLPDRVECVDSLPLTAVGKVDK 523
                          570
                   ....*....|..
gi 1820002560 8118 KRLREIGASFTA 8129
Cdd:PRK10946   524 KQLRQWLASRAS 535
PRK07788 PRK07788
acyl-CoA synthetase; Validated
862-1013 1.19e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 74.96  E-value: 1.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  862 ARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRH 941
Cdd:PRK07788    59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  942 EEIFKQIGAQVVLTSSQHAMLFASSE----RHQVTVSKV-----STSQLPTVVNF------AKSPVDPGNTAYIIFTSGT 1006
Cdd:PRK07788   139 AEVAAREGVKALVYDDEFTDLLSALPpdlgRLRAWGGNPdddepSGSTDETLDDLiagsstAPLPKPPKPGGIVILTSGT 218

                   ....*..
gi 1820002560 1007 TGIPKGV 1013
Cdd:PRK07788   219 TGTPKGA 225
PLN02574 PLN02574
4-coumarate--CoA ligase-like
1940-2343 1.26e-12

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 74.88  E-value: 1.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1940 KARPHAPA-ICAWDGE-LTYGELDALSSKLASHLVQ-LGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 2016
Cdd:PLN02574    50 HNHNGDTAlIDSSTGFsISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLG 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2017 RHEDIFRQTGAQVVVTSAQHSARWIGTNHQVVTVS-AGS---------------LEQFSTLVNPvdlPAKPENAAYVMFT 2080
Cdd:PLN02574   130 EIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPeNYDfdskriefpkfyeliKEDFDFVPKP---VIKQDDVAAIMYS 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2081 SGSTGTPKGVVLEHRAVVTSC-------LGHGQAFGVTNL-LRAL-QFTAYTFDVCIAEIITTlvhGGCICVPSDSERRD 2151
Cdd:PLN02574   207 SGTTGASKGVVLTHRNLIAMVelfvrfeASQYEYPGSDNVyLAALpMFHIYGLSLFVVGLLSL---GSTIVVMRRFDASD 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2152 nLAKAI-----TDMQVNWGYLTSSVARLLDPCLVP--SLKVLVLGGEQVNST---DWGKWPSSVQTINGYGPTEccvfcT 2221
Cdd:PLN02574   284 -MVKVIdrfkvTHFPVVPPILMALTKKAKGVCGEVlkSLKQVSCGAAPLSGKfiqDFVQTLPHVDFIQGYGMTE-----S 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2222 GYTGIQGFQSGNIgTSIASV--------SWVVDPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpAWLle 2293
Cdd:PLN02574   358 TAVGTRGFNTEKL-SKYSSVgllapnmqAKVVDWST-GCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKD-GWL-- 432
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2294 gypghegrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVE 2343
Cdd:PLN02574   433 -------------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLE 469
PRK07638 PRK07638
acyl-CoA synthetase; Validated
5628-6138 1.28e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 74.82  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5628 FTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDmVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHP 5707
Cdd:PRK07638     7 YKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5708 ASRHEDTFRHTGAQVVVTSAQHSARWIGTNHQVVTVSagSLGQLSTLVNPVGLPAI-PENAVYIM-FTSGSTGIPKGVVL 5785
Cdd:PRK07638    86 QDELKERLAISNADMIVTERYKLNDLPDEEGRVIEID--EWKRMIEKYLPTYAPIEnVQNAPFYMgFTSGSTGKPKAFLR 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5786 EHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICV-----PsdsdrrNDLVKAISTMDVSCALL 5860
Cdd:PRK07638   164 AQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLmrkfiP------NQVLDKLETENISVMYT 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5861 TPSVAR-LLEPSSVPTLQMLVLqgeqVSFADW---------NRWPaSVQTINGYGPTECSICCNTYSGKQGFKSGIIGTS 5930
Cdd:PRK07638   238 VPTMLEsLYKENRVIENKMKII----SSGAKWeaeakekikNIFP-YAKLYEFYGASELSFVTALVDEESERRPNSVGRP 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5931 VASVSWVVDPENHDRLAPlGSIGELLVEGPILARGYLNDIQKTAAvfIDDPAWLLEGYPGHPGRQGRLYktgdlvrydan 6010
Cdd:PRK07638   313 FHNVQVRICNEAGEEVQK-GEIGTVYVKSPQFFMGYIIGGVLARE--LNADGWMTVRDVGYEDEEGFIY----------- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6011 gnlvCLGRKDSQVKLRGQRVELGEVEHHVREClPEARQLAVevilpSGQKDHAMLAAFVQLEEGTQNAlldkeasgedsm 6090
Cdd:PRK07638   379 ----IVGREKNMILFGGINIFPEEIESVLHEH-PAVDEIVV-----IGVPDSYWGEKPVAIIKGSATK------------ 436
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 6091 aqvvflASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREI 6138
Cdd:PRK07638   437 ------QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSW 478
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
862-1367 1.30e-12

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 74.97  E-value: 1.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  862 ARARPDASAVcAWDGE-----LTYGELDELSSKLAAHLVQLGVKREDVVPLCfeksMWT----VVAMLAVLKAGGAFVPL 932
Cdd:cd12119      6 ARLHGDREIV-SRTHEgevhrYTYAEVAERARRLANALRRLGVKPGDRVATL----AWNthrhLELYYAVPGMGAVLHTI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  933 DPGHPASRHEEIFKQIGAQVVLTSSQHAMLFASSERHQVTVSKVST---------SQLPTVVNF-----AKSPVDP---- 994
Cdd:cd12119     81 NPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVmtddaampePAGVGVLAYeellaAESPEYDwpdf 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  995 -GNTAYII-FTSGTTGIPKGVVLQHR--------AVTTSCLG--------------HGEAFGytdharvLQFAsytfdac 1050
Cdd:cd12119    161 dENTAAAIcYTSGTTGNPKGVVYSHRslvlhamaALLTDGLGlsesdvvlpvvpmfHVNAWG-------LPYA------- 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1051 iaeiitTLLYGGCICVPSESDRRNNLAKAISTMDVNCALLTPSVARLL------EPSAVPSLKRLVLQGEQV--SFADWN 1122
Cdd:cd12119    227 ------AAMVGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLldhleaNGRDLSSLRRVVIGGSAVprSLIEAF 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1123 RWPGsVQTINGYGPTECS--VCCNTYSGKQGFKSGI--------IGTSVASLSW-VVDAGNhNRLAPLG-SIGELLVEGP 1190
Cdd:cd12119    301 EERG-VRVIHAWGMTETSplGTVARPPSEHSNLSEDeqlalrakQGRPVPGVELrIVDDDG-RELPWDGkAVGELQVRGP 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1191 ILARGYLNDIDKTEAAFIDDpaWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGR-KDSqVKVRGQ---RVEL-GEI 1265
Cdd:cd12119    379 WVTKSYYKNDEESEALTEDG--WL---------------RTGDVATIDEDGYLTITDRsKDV-IKSGGEwisSVELeNAI 440
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1266 EHHvreclPEARQLAVeVILPSgQK--EHALlaAFIQLDKGnhnalfeEKASGEDsmaqvvfltgVEEELAKRLPEHMVP 1343
Cdd:cd12119    441 MAH-----PAVAEAAV-IGVPH-PKwgERPL--AVVVLKEG-------ATVTAEE----------LLEFLADKVAKWWLP 494
                          570       580
                   ....*....|....*....|....*
gi 1820002560 1344 -TILFtVKAMPITTSGKIDRKRLQD 1367
Cdd:cd12119    495 dDVVF-VDEIPKTSTGKIDKKALRE 518
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
4545-4993 1.47e-12

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 74.91  E-value: 1.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4545 DQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGG--AFV--- 4619
Cdd:PRK08279    41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLntq 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4620 ----PL-------DPDHPASRHE--HIFRQTGAQVVLASAQY-ATLWTSLGRSVVIVSEASTSQLPVVTKTADPSVNPGN 4685
Cdd:PRK08279   121 qrgaVLahslnlvDAKHLIVGEElvEAFEEARADLARPPRLWvAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKD 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4686 AAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVL-----------------------------QF-ASYT 4735
Cdd:PRK08279   201 TAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYcclplyhntggtvawssvlaagatlalrrKFsASRF 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4736 FDACIAEIITTLLCCGCIC------VPSDSDRRNNLAKAI-NAmdvnwalLTPSVarmldpcvvqslkilvlggeqvnsa 4808
Cdd:PRK08279   281 WDDVRRYRATAFQYIGELCryllnqPPKPTDRDHRLRLMIgNG-------LRPDI------------------------- 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4809 dWDRWPK--SIQTI-NAYGPTECSIccttysgkqGF-----KSGTIGTS---------IV-----SVSWVVDPENHNRLA 4866
Cdd:PRK08279   329 -WDEFQQrfGIPRIlEFYAASEGNV---------GFinvfnFDGTVGRVplwlahpyaIVkydvdTGEPVRDADGRCIKV 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4867 PLGSIGELLveGPILAR----GYlNDMEKTEA-----AFIDDPAWllegygghsgrqgrlYKTGDLVRYDADGNLVYLGR 4937
Cdd:PRK08279   399 KPGEVGLLI--GRITDRgpfdGY-TDPEASEKkilrdVFKKGDAW---------------FNTGDLMRDDGFGHAQFVDR 460
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 4938 KDSQVKLRGQRVELGEVEHHVREC--LTEAKQLAVEVivpEGEGGYAMLAAfVQLGDD 4993
Cdd:PRK08279   461 LGDTFRWKGENVATTEVENALSGFpgVEEAVVYGVEV---PGTDGRAGMAA-IVLADG 514
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
3488-3976 1.55e-12

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 74.63  E-value: 1.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3488 TYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQ 3567
Cdd:PLN02330    57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3568 YSARWTSSSCHVVTVSKALSSQ-------LPAVVDSTNTSVRPE----NAAYIIFTSGSTGVPKGVVLEHR-AVATSC-- 3633
Cdd:PLN02330   137 NYGKVKGLGLPVIVLGEEKIEGavnwkelLEAADRAGDTSDNEEilqtDLCALPFSSGTTGISKGVMLTHRnLVANLCss 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3634 ---LGHGRAFGITNLSRVLQFASYTFDA-CIAeiitTLLCGGCICVPSDSDRRNSLaKAISTMDVNWAFLTPSVARLL-- 3707
Cdd:PLN02330   217 lfsVGPEMIGQVVTLGLIPFFHIYGITGiCCA----TLRNKGKVVVMSRFELRTFL-NALITQEVSFAPIVPPIILNLvk 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3708 DPGL----IPSLKILAIGGEQSS------SADWNRWPGsVQKIHVYGPTE-CCIfctgyTTKQGfEPSTiGTSVA---SV 3773
Cdd:PLN02330   292 NPIVeefdLSKLKLQAIMTAAAPlapellTAFEAKFPG-VQVQEAYGLTEhSCI-----TLTHG-DPEK-GHGIAkknSV 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3774 SWV--------VDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTGDLVQ 3845
Cdd:PLN02330   364 GFIlpnlevkfIDPDTGRSL-PKNTPGELCVRSQCVMQGYYNNKEETDRT-IDEDGWL---------------HTGDIGY 426
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3846 YNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVeVILPSGQKDHAMLAAFVQLEEGTQNAlldkeagg 3925
Cdd:PLN02330   427 IDDDGDIFIVDRIKELIKYKGFQVAPAELE-AILLTHPSVEDAAV-VPLPDEEAGEIPAACVVINPKAKESE-------- 496
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 3926 EDSMAqvvFLASVEEELAKRLPEHMVPTVffsllhfPTTTSGKTDRKRLRE 3976
Cdd:PLN02330   497 EDILN---FVAANVAHYKKVRVVQFVDSI-------PKSLSGKIMRRLLKE 537
PRK08316 PRK08316
acyl-CoA synthetase; Validated
5626-6137 1.58e-12

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 74.58  E-value: 1.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVP---- 5701
Cdd:PRK08316    15 DILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPvnfm 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5702 LDPDHPASrhedTFRHTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLGQLSTLVNPVGL-----------PAIPENAVY- 5769
Cdd:PRK08316    95 LTGEELAY----ILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWldfadwaeagsVAEPDVELAd 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 -----IMFTSGSTGIPKGVVLEHRAVV---TSCwgrgrafgITNLsrvlqfaSYTFD------------ACMDEIITTLM 5829
Cdd:PRK08316   171 ddlaqILYTSGTESLPKGAMLTHRALIaeyVSC--------IVAG-------DMSADdiplhalplyhcAQLDVFLGPYL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5830 YGGCICVPSDSDRRNDLVKAISTMDVSCALLTPSV----AR--LLEPSSVPTLQ----------MLVLQGEQvsfadwNR 5893
Cdd:PRK08316   236 YVGATNVILDAPDPELILRTIEAERITSFFAPPTVwislLRhpDFDTRDLSSLRkgyygasimpVEVLKELR------ER 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5894 WPAsVQTINGYGPTECSICCNTYSGK-QGFKSGIIGTSVASV-SWVVDPENHDrlAPLGSIGELLVEGPILARGYLNDIQ 5971
Cdd:PRK08316   310 LPG-LRFYNCYGQTEIAPLATVLGPEeHLRRPGSAGRPVLNVeTRVVDDDGND--VAPGEVGEIVHRSPQLMLGYWDDPE 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5972 KTAAVFIDDpaWllegypghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECLPEARQLA- 6050
Cdd:PRK08316   387 KTAEAFRGG--W---------------FHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVE----EALYTHPAVAe 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6051 VEVI-LPSGQKDHAmLAAFVQLEEGtqnalldKEASGEDSMAQVvflasveeelAKRLPEHMVP-TVFF--SLlhfPTTT 6126
Cdd:PRK08316   446 VAVIgLPDPKWIEA-VTAVVVPKAG-------ATVTEDELIAHC----------RARLAGFKVPkRVIFvdEL---PRNP 504
                          570
                   ....*....|.
gi 1820002560 6127 SGKTDRKRLRE 6137
Cdd:PRK08316   505 SGKILKRELRE 515
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
7610-8120 1.59e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 74.65  E-value: 1.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7610 HDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 7689
Cdd:PRK13383    38 YTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7690 DHPASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSkalssqlPAVVDSTNTSVRPENAA---YIIFTSGSTGVPK 7766
Cdd:PRK13383   118 EFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVID-------PATAGAEESGGRPAVAApgrIVLLTSGTTGKPK 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7767 GVVLEHRavatscLGHGRAFGITNLSRV-------LQFASYTFDAC-IAEIITTLLCGGCICVPSDSDRRNSLAKAiSTM 7838
Cdd:PRK13383   191 GVPRAPQ------LRSAVGVWVTILDRTrlrtgsrISVAMPMFHGLgLGMLMLTIALGGTVLTHRHFDAEAALAQA-SLH 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7839 DVNWAFLTPSV-ARLLD-PGLI------PSLKILAIGGEQSSSADWNRWPGSVQKI--HVYGPTECCIFCTGYTTKQGFE 7908
Cdd:PRK13383   264 RADAFTAVPVVlARILElPPRVrarnplPQLRVVMSSGDRLDPTLGQRFMDTYGDIlyNGYGSTEVGIGALATPADLRDA 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7909 PSTIGTSVASVSWVVDPENHNRLAPLGSmGELLMEGPILARGYLNDVDKteaAFIDDPAwllegypghpgrqgrlyKTGD 7988
Cdd:PRK13383   344 PETVGKPVAGCPVRILDRNNRPVGPRVT-GRIFVGGELAGTRYTDGGGK---AVVDGMT-----------------STGD 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7989 LVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVrECLPEARQLAVeVILPSGQKNHaMLAVFVQLGKGTHIahleek 8068
Cdd:PRK13383   403 MGYLDNAGRLFIVGREDDMIISGGENVYPRAVENAL-AAHPAVADNAV-IGVPDERFGH-RLAAFVVLHPGSGV------ 473
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 8069 aggeDSMAQVVFLTGTEEELAKRLPKHMVPTVffallhfPMTTSGKADRKRL 8120
Cdd:PRK13383   474 ----DAAQLRDYLKDRVSRFEQPRDINIVSSI-------PRNPTGKVLRKEL 514
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
1954-2326 1.70e-12

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 74.43  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1954 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVV-VT 2032
Cdd:cd05932      6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALfVG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2033 SAQHsarWIGTNHQV----VTVSAGSL------EQFSTLVN---PVD--LPAKPENAAYVMFTSGSTGTPKGVVLEHRAV 2097
Cdd:cd05932     86 KLDD---WKAMAPGVpeglISISLPPPsaancqYQWDDLIAqhpPLEerPTRFPEQLATLIYTSGTTGQPKGVMLTFGSF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2098 VTSCLGHGQAFGVTNLLRALQFTAYTFdvcIAEiiTTLVHGGCICVPSDSERRDNLAKAITDMQVNWGYLTSSVARL--- 2174
Cdd:cd05932    163 AWAAQAGIEHIGTEENDRMLSYLPLAH---VTE--RVFVEGGSLYGGVLVAFAESLDTFVEDVQRARPTLFFSVPRLwtk 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2175 -------------LDPCL-VPSLKVLV-------LGGEQVNSTDWGKWPSSVQTIN-----------GYGPTECCVFCT- 2221
Cdd:cd05932    238 fqqgvqdkipqqkLNLLLkIPVVNSLVkrkvlkgLGLDQCRLAGCGSAPVPPALLEwyrslglnileAYGMTENFAYSHl 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2222 GYTGIQgfQSGNIGTSIASVSWVVDPEnhgrlaplgsiGELLVEGPILARGYLNDVDKTQAAFIDDpAWLlegypghegr 2301
Cdd:cd05932    318 NYPGRD--KIGTVGNAGPGVEVRISED-----------GEILVRSPALMMGYYKDPEATAEAFTAD-GFL---------- 373
                          410       420
                   ....*....|....*....|....*
gi 1820002560 2302 qgrlyKTGDLVRYSSDGNLVCLGRK 2326
Cdd:cd05932    374 -----RTGDKGELDADGNLTITGRV 393
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
7208-7475 2.02e-12

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 73.83  E-value: 2.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7208 VLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLLQVVVE-----EKIQWTES----EALEEYLKEDKAVSMGLG 7278
Cdd:cd20483     29 VCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDpsfhlIVIDLSEAadpeAALDQLVRNLRRQELDIE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7279 D-PLAHYALVKEAwgGKRW-FVWTIHHALYDGGSLPLILHAVKQVYSGAVLER------QPSFNaFIQY-------LGQQ 7343
Cdd:cd20483    109 EgEVIRGWLVKLP--DEEFaLVLASHHIAWDRGSSKSIFEQFTALYDALRAGRdlatvpPPPVQ-YIDFtlwhnalLQSP 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7344 DLEATAAYWQTALSDC-EAVLFPPLPSTVTQPVADTTVEyqcppLSKATLDTTTSTLIR---------------AAWAIV 7407
Cdd:cd20483    186 LVQPLLDFWKEKLEGIpDASKLLPFAKAERPPVKDYERS-----TVEATLDKELLARMKricaqhavtpfmfllAAFRAF 260
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 7408 TSCYTSSDDVVYGttVTGRNAPIAGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAHEQ 7475
Cdd:cd20483    261 LYRYTEDEDLTIG--MVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSA 326
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
3607-3909 2.03e-12

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 72.75  E-value: 2.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3607 AYIIFTSGSTGVPKGVVLEHRAVATS---------CLGHGRAFGITNLSRVlqfasytfdACIAEIITTLLCGGCICVPs 3677
Cdd:cd17630      3 ATVILTSGSTGTPKAVVHTAANLLASaaglhsrlgFGGGDSWLLSLPLYHV---------GGLAILVRSLLAGAELVLL- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3678 dsDRRNSLAKAISTMDVNWAFLTPS-VARLLDPGLIP----SLKILAIGG--------EQSSSADWNRWPGsvqkihvYG 3744
Cdd:cd17630     73 --ERNQALAEDLAPPGVTHVSLVPTqLQRLLDSGQGPaalkSLRAVLLGGapippellERAADRGIPLYTT-------YG 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3745 PTEcciFCTGYTTKQ--GFEPSTIGtsvasvswVVDPENHNRLAPlgsMGELLMEGPILARGYLNDVDKTEAafiDDPAW 3822
Cdd:cd17630    144 MTE---TASQVATKRpdGFGRGGVG--------VLLPGRELRIVE---DGEIWVGGASLAMGYLRGQLVPEF---NEDGW 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3823 llegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE------HHVREC----LPEAR--QLAV 3890
Cdd:cd17630    207 ---------------FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEaalaahPAVRDAfvvgVPDEElgQRPV 271
                          330
                   ....*....|....*....
gi 1820002560 3891 EVILPSGQKDHAMLAAFVQ 3909
Cdd:cd17630    272 AVIVGRGPADPAELRAWLK 290
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
2-285 2.04e-12

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 74.40  E-value: 2.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWAL-LTPSVARLL-----EPSHIPSLRILVMGGEQVNS-ADWDRWPSSVQTINGYGPTECC---IVCTGYTSEQDFt 71
Cdd:PRK06087   276 RCTCMLgATPFIYDLLnllekQPADLSALRFFLCGGTTIPKkVARECQQRGIKLLSVYGSTESSphaVVNLDDPLSRFM- 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   72 tGTIGTSIASVSW-VVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVfINNPAWlleghggyagrqgrlYKTG 150
Cdd:PRK06087   355 -HTDGYAAAGVEIkVVD--EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA-LDEEGW---------------YYSG 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  151 DLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAVeVVLP---LGQKnhatLAAFIQLdKGTHNAL 227
Cdd:PRK06087   416 DLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQH-PKIHDACV-VAMPderLGER----SCAYVVL-KAPHHSL 488
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560  228 LKEKVggddsiarVVFLAgvEEELAKRL-PKHMVptvffALLHFPTTTSGKTDRKRLRE 285
Cdd:PRK06087   489 TLEEV--------VAFFS--RKRVAKYKyPEHIV-----VIDKLPRTASGKIQKFLLRK 532
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
3026-3213 2.18e-12

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 70.84  E-value: 2.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3026 TPMQEGILTSQGkDPDAYWVCFIYEVipnqETSISLARLQQAWKGVVHQHSLLRTLLV--DNVPgstgttnVVLKDPQPS 3103
Cdd:COG4908      2 SPAQKRFLFLEP-GSNAYNIPAVLRL----EGPLDVEALERALRELVRRHPALRTRFVeeDGEP-------VQRIDPDAD 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3104 ISVfssegtaTIELFRSRYNPAAQRSIGQLQHH---------------LSICQLNNGKVYLCLDINHAIIDAHSRGILMH 3168
Cdd:COG4908     70 LPL-------EVVDLSALPEPEREAELEELVAEeasrpfdlargpllrAALIRLGEDEHVLLLTIHHIISDGWSLGILLR 142
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 3169 DLQEAYDA-------NLNPQSTSFRDFASYIKQQSQ----EEAGRYWAEYLDGVEP 3213
Cdd:COG4908    143 ELAALYAAllegeppPLPELPIQYADYAAWQRAWLQsealEKQLEYWRQQLAGAPP 198
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
1939-2121 2.40e-12

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 73.75  E-value: 2.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 2018
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2019 EDIFRQTGAQVVVTSaQHSARWIGTNHQVVTVSAGSleqfstlvnpVDLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVV 2098
Cdd:PRK09029    93 EELLPSLTLDFALVL-EGENTFSALTSLHLQLVEGA----------HAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHL 161
                          170       180
                   ....*....|....*....|...
gi 1820002560 2099 TSCLGhgqafgvtnLLRALQFTA 2121
Cdd:PRK09029   162 ASAEG---------VLSLMPFTA 175
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
7073-7133 2.80e-12

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 65.28  E-value: 2.80e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 7073 RTMQQLWARMLKVKADSIGLDDSFFRLGGDSIVAMKLVGEARRT-GLQLSVADVFRHPRLVD 7133
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
PRK07638 PRK07638
acyl-CoA synthetase; Validated
3467-3977 2.97e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 73.66  E-value: 2.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3467 FTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLcFEKSMWTVVAMLAVLKAGGAFVPLDPDHP 3546
Cdd:PRK07638     7 YKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAIL-LENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3547 ASRHEEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSK---ALSSQLPAVVDSTNTSVRPenaAYIIFTSGSTGVPKGVV 3623
Cdd:PRK07638    86 QDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDEwkrMIEKYLPTYAPIENVQNAP---FYMGFTSGSTGKPKAFL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3624 LEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICV-----PsdsdrrNSLAKAISTMDVNWAF 3698
Cdd:PRK07638   163 RAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLmrkfiP------NQVLDKLETENISVMY 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3699 LTPSVARLL---DPGLIPSLKILaiggeqSSSADW---------NRWPgSVQKIHVYGPTECCiFCTgYTTKQGFE--PS 3764
Cdd:PRK07638   237 TVPTMLESLykeNRVIENKMKII------SSGAKWeaeakekikNIFP-YAKLYEFYGASELS-FVT-ALVDEESErrPN 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3765 TIGTSVASVSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAafIDDPAWLLEGYPGHPGRQGRLYKTGdlv 3844
Cdd:PRK07638   308 SVGRPFHNVQVRICNEAGEEVQK-GEIGTVYVKSPQFFMGYIIGGVLARE--LNADGWMTVRDVGYEDEEGFIYIVG--- 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3845 qynADGNLVYLGrkdsqvkvrGQRVELGEVEHHVREClPEARQLAVevilpSGQKDHAMLAAFVQLEEGTQNAlldkeag 3924
Cdd:PRK07638   382 ---REKNMILFG---------GINIFPEEIESVLHEH-PAVDEIVV-----IGVPDSYWGEKPVAIIKGSATK------- 436
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 3925 gedsmaqvvflASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREI 3977
Cdd:PRK07638   437 -----------QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSW 478
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
445-717 3.46e-12

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 72.77  E-value: 3.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  445 YIMQDVLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSElGLLQVVVEE-----------KMQWTESES-LEEYLNED 512
Cdd:cd19531     24 YNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDG-EPVQVILPPlplplpvvdlsGLPEAEREAeAQRLAREE 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  513 KAASMGLG-DRLARYALIKesCGGKRW-FVWTIHHALYDGWSLPLVLDAVKQVYSgAALERQPSfnTF----IQY----V 582
Cdd:cd19531    103 ARRPFDLArGPLLRATLLR--LGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYA-AFLAGRPS--PLpplpIQYadyaV 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  583 SQQD------VKAAAAYWQTALADCEAVLfpPLPSTVTQPVADT----TVKYQCPPspEVTSS--------NITTSTLIR 644
Cdd:cd19531    178 WQREwlqgevLERQLAYWREQLAGAPPVL--ELPTDRPRPAVQSfrgaRVRFTLPA--ELTAAlralarreGATLFMTLL 253
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560  645 AAWAIIASRYTSSEDIVFGTTVTGRNAPitGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEmiAYE 717
Cdd:cd19531    254 AAFQVLLHRYSGQDDIVVGTPVAGRNRA--ELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALE--AYA 322
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
46-293 3.72e-12

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 73.64  E-value: 3.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   46 VQTINGYGPTECCIVCTGYTSEQdfTTGTIGtSIAS--VSWVVDpkDHGRLAPLGSVGELLV---EGPILARGYLSDPEK 120
Cdd:PRK06155   318 VDLLDGYGSTETNFVIAVTHGSQ--RPGSMG-RLAPgfEARVVD--EHDQELPDGEPGELLLradEPFAFATGYFGMPEK 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  121 TAAvfinnpAWlleghggyagrQGRLYKTGDLVRYDADGNLVCLGR-KDSqVKLRGQRVELGEVEHHVREclpeakQLAV 199
Cdd:PRK06155   393 TVE------AW-----------RNLWFHTGDRVVRDADGWFRFVDRiKDA-IRRRGENISSFEVEQVLLS------HPAV 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  200 EVVlplgqknhatlAAFIqldkgthnalLKEKVGGDDSIARVVFLAGVE---EELAK----RLPKHMVPTVFFALLHFPT 272
Cdd:PRK06155   449 AAA-----------AVFP----------VPSELGEDEVMAAVVLRDGTAlepVALVRhcepRLAYFAVPRYVEFVAALPK 507
                          250       260
                   ....*....|....*....|.
gi 1820002560  273 TTSGKTDRKRLREIGasFTAQ 293
Cdd:PRK06155   508 TENGKVQKFVLREQG--VTAD 526
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
8146-8214 4.01e-12

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 65.26  E-value: 4.01e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 8146 PLTEAEQTMQQLWARVLGIDADIIGLDDSFFR-LGGDSIAAMKLVGEAR-RTGLQLSVADIFRHPRLIDLA 8214
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEeEFGIELPDTELFEYPTVADLA 72
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
10-285 4.05e-12

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 73.30  E-value: 4.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   10 PSVARLL-----EPSHIPSLRILVMGGEQVNSADWDRWP--SSVQTINGYGPTECcIVCTGYTSEQDFTTGTIGTSiaSV 82
Cdd:cd05970    284 PTIYRFLiredlSRYDLSSLRYCTTAGEALNPEVFNTFKekTGIKLMEGFGQTET-TLTIATFPWMEPKPGSMGKP--AP 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   83 SWVVDPKDH-GRLAPLGSVGELLV---EG-PI-LARGYLSDPEKTAAVFinnpawllegHGGYagrqgrlYKTGDLVRYD 156
Cdd:cd05970    361 GYEIDLIDReGRSCEAGEEGEIVIrtsKGkPVgLFGGYYKDAEKTAEVW----------HDGY-------YHTGDAAWMD 423
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  157 ADGNLVCLGRKDSQVKLRGQRVELGEVEhhvreclpeakqlavevvlplgqknhatlAAFIQldkgtHNALLKEKVGG-D 235
Cdd:cd05970    424 EDGYLWFVGRTDDLIKSSGYRIGPFEVE-----------------------------SALIQ-----HPAVLECAVTGvP 469
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560  236 DSI------ARVVFLAGVE--EELAKRLPKHM--------VPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:cd05970    470 DPIrgqvvkATIVLAKGYEpsEELKKELQDHVkkvtapykYPRIVEFVDELPKTISGKIRRVEIRE 535
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
51-220 4.42e-12

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 73.60  E-value: 4.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   51 GYGPTECCIVCTGYTsEQDFTTGTIGTSIASVSWVVDPKdhgrlaplgsvGELLVEGPILARGYLSDPEKTAAVFInnpa 130
Cdd:COG1022    377 GYGLTETSPVITVNR-PGDNRIGTVGPPLPGVEVKIAED-----------GEILVRGPNVMKGYYKNPEATAEAFD---- 440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  131 wllegHGGYagrqgrlYKTGDLVRYDADGNLVCLGRKDSQVKLR-GQRVELGEVEHHVREClPEAKQLAVevvlpLGQkN 209
Cdd:COG1022    441 -----ADGW-------LHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKAS-PLIEQAVV-----VGD-G 501
                          170
                   ....*....|.
gi 1820002560  210 HATLAAFIQLD 220
Cdd:COG1022    502 RPFLAALIVPD 512
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
7611-7793 4.63e-12

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 73.37  E-value: 4.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGG--AFV--- 7685
Cdd:PRK08279    41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLntq 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7686 ----PL-------DPDHPASRHE--EIFEQTGAQVVVASAQYSArWTSSSCHVVTVS--KALSSQLPAVVDSTNTSVRPE 7750
Cdd:PRK08279   121 qrgaVLahslnlvDAKHLIVGEElvEAFEEARADLARPPRLWVA-GGDTLDDPEGYEdlAAAAAGAPTTNPASRSGVTAK 199
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 7751 NAAYIIFTSGSTGVPKGVVLEHRAVATSclghGRAFG-ITNLSR 7793
Cdd:PRK08279   200 DTAFYIYTSGTTGLPKAAVMSHMRWLKA----MGGFGgLLRLTP 239
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
849-1368 4.66e-12

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 73.50  E-value: 4.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  849 AVDRCIHDLFAEQARARPDaSAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVV----PLCFEksmwTVVAMLAVLK 924
Cdd:cd05967     55 ALDRHVEAGRGDQIALIYD-SPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRViiymPMIPE----AAIAMLACAR 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  925 AG-------GAFVPLDPghpASRHEEIfkqiGAQVVLTSS---------------QHAMLFASSERHQVTV-----SKVS 977
Cdd:cd05967    130 IGaihsvvfGGFAAKEL---ASRIDDA----KPKLIVTAScgiepgkvvpykpllDKALELSGHKPHHVLVlnrpqVPAD 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  978 TSQLPTVVNFAK----------SPVDPGNTAYIIFTSGTTGIPKGVVlqhR-------AVTTSC-----LGHGEAF-GYT 1034
Cdd:cd05967    203 LTKPGRDLDWSEllakaepvdcVPVAATDPLYILYTSGTTGKPKGVV---RdngghavALNWSMrniygIKPGDVWwAAS 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1035 DHARVLQFaSYTFDACIAEIITTLLYGGcicVPSESDRRNNLAKAISTMDVNCALLTPSVARLL---EPSA-------VP 1104
Cdd:cd05967    280 DVGWVVGH-SYIVYGPLLHGATTVLYEG---KPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIrkeDPDGkyikkydLS 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1105 SLKRLVLQGEQ--VSFADWNRWPGSVQTINGYGPTEC--SVCCNtYSGKQGF--KSGIIGTSVASLSW-VVDAgNHNRLA 1177
Cdd:cd05967    356 SLRTLFLAGERldPPTLEWAENTLGVPVIDHWWQTETgwPITAN-PVGLEPLpiKAGSPGKPVPGYQVqVLDE-DGEPVG 433
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1178 PlGSIGELLVEGPiLARGYLNDIDKTEAAFIddpawllEGYEGHAgrRGrLYKTGDLVRCDADGNLVCLGRKDSQVKVRG 1257
Cdd:cd05967    434 P-NELGNIVIKLP-LPPGCLLTLWKNDERFK-------KLYLSKF--PG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAG 501
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1258 QRVELGEIEhhvreclpearqlavEVILpsgqkEHALLA--AFIqldkGNHNALfeekaSGEDSMAQVVFLTGV---EEE 1332
Cdd:cd05967    502 HRLSTGEME---------------ESVL-----SHPAVAecAVV----GVRDEL-----KGQVPLGLVVLKEGVkitAEE 552
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 1333 LAKRLPEHMVPTI--------LFTVKAMPITTSGKIDRKRLQDI 1368
Cdd:cd05967    553 LEKELVALVREQIgpvaafrlVIFVKRLPKTRSGKILRRTLRKI 596
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
877-1253 4.67e-12

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 72.88  E-value: 4.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVvlts 956
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDA---- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  957 sqhamlfasserhqvtvskvstsqlptvvnFAKSPVdPGNTAYIIFTSGTTGIPKGVVLQHR-------AVTTSclgHGE 1029
Cdd:cd05910     78 ------------------------------FIGIPK-ADEPAAILFTSGSTGTPKGVVYRHGtfaaqidALRQL---YGI 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1030 AFGYTDHARVLQFAsyTFDACIAeiITTLLYGGCICVPSESDRRNnLAKAISTMDVNCALLTPSVARLL------EPSAV 1103
Cdd:cd05910    124 RPGEVDLATFPLFA--LFGPALG--LTSVIPDMDPTRPARADPQK-LVGAIRQYGVSIVFGSPALLERVarycaqHGITL 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1104 PSLKRLVLQGEQVSFADWNRW----PGSVQTINGYGPTEC---------SVCCNTYSGKQGFKSGIIGTSVASLSWVV-- 1168
Cdd:cd05910    199 PSLRRVLSAGAPVPIALAARLrkmlSDEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTCVGRPIPGVRVRIie 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1169 --DAGNH---NRLA-PLGSIGELLVEGPILARGYLNDIDKTEAAFIDDPawllegyeghagRRGRLYKTGDLVRCDADGN 1242
Cdd:cd05910    279 idDEPIAewdDTLElPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN------------SEGFWHRMGDLGYLDDEGR 346
                          410
                   ....*....|.
gi 1820002560 1243 LVCLGRKDSQV 1253
Cdd:cd05910    347 LWFCGRKAHRV 357
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
1391-1460 4.69e-12

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 65.26  E-value: 4.69e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 1391 PSTEVEQTMQQLWAQVLSIEPNSIGLDDSFFR-LGGDSIVAMKLVGEAR-RTGLQLSVADIFRHPRLVDLAR 1460
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEeEFGIELPDTELFEYPTVADLAD 73
PRK06164 PRK06164
acyl-CoA synthetase; Validated
6844-7054 4.72e-12

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 73.24  E-value: 4.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6844 PSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDpAWlveghgkhpgrrgrlYKTGDLVYYNKDGNLVYIGRKD 6923
Cdd:PRK06164   366 PQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDD-GY---------------FRTGDLGYTRGDGQFVYQTRMG 429
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6924 GQVKVRGQRVELGEIENRLRECMP-RATQMavevispAGAAEQAKTMVVAFLQLNDEARdallggnvPNDDNLSAQvvfp 7002
Cdd:PRK06164   430 DSLRLGGFLVNPAEIEHALEALPGvAAAQV-------VGATRDGKTVPVAFVIPTDGAS--------PDEAGLMAA---- 490
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 7003 akvdekLSNLLPSYMMPEVYFAVPQLPMMISG---KTDRKRLREIGASFTAQQLA 7054
Cdd:PRK06164   491 ------CREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQARLAAERA 539
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3602-3939 5.30e-12

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 71.64  E-value: 5.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3602 RPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGhGRAFG--------ITNLSRVLQFASYTFDAC-------IAEIITT 3666
Cdd:cd05924      1 RSADDLYILYTGGTTGMPKGVMWRQEDIFRMLMG-GADFGtgeftpseDAHKAAAAAAGTVMFPAPplmhgtgSWTAFGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3667 LLCGGCICVPSDS-DRRNSLA-----KAISTMDVNWAFLTPSVARLLDPGL--IPSLKILAIGGEQSSSADWNRWPGSVQ 3738
Cdd:cd05924     80 LLGGQTVVLPDDRfDPEEVWRtiekhKVTSMTIVGDAMARPLIDALRDAGPydLSSLFAISSGGALLSPEVKQGLLELVP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3739 KIHV---YGPTECCIFCTGYTTKQGFEPSTIgTSVASVSWVVDPENHNRLAPLGSMGELLMEGPIlARGYLNDVDKTEAA 3815
Cdd:cd05924    160 NITLvdaFGSSETGFTGSGHSAGSGPETGPF-TRANPDTVVLDDDGRVVPPGSGGVGWIARRGHI-PLGYYGDEAKTAET 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3816 F--IDDPAWLLegypghpgrqgrlykTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVReclpeaRQLAVEVI 3893
Cdd:cd05924    238 FpeVDGVRYAV---------------PGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALK------SHPAVYDV 296
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 3894 LPSGQKDH---AMLAAFVQLEEGTQNALLDKEAGGEDSMA------QVVFLASVE 3939
Cdd:cd05924    297 LVVGRPDErwgQEVVAVVQLREGAGVDLEELREHCRTRIAryklpkQVVFVDEIE 351
PRK07529 PRK07529
AMP-binding domain protein; Validated
5598-6137 5.87e-12

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 73.07  E-value: 5.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5598 IETTTLEDRQqlwawnqnVPpaieRCVHDLFTEQAKARPHAPAIC------AWDG--ELTYGELDALSSKLAGHLTQLGV 5669
Cdd:PRK07529    13 IEAVPLAARD--------LP----ASTYELLSRAAARHPDAPALSflldadPLDRpeTWTYAELLADVTRTANLLHSLGV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5670 KPEDMV----PLCFEksmwTVVAMLAVLKAGGAFvP----LDPDHPASrhedTFRHTGAQVVVTSA--------QHSARW 5733
Cdd:PRK07529    81 GPGDVVafllPNLPE----THFALWGGEAAGIAN-PinplLEPEQIAE----LLRAAGAKVLVTLGpfpgtdiwQKVAEV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5734 IGTNHQVVTV-SAGSLGQLSTLVNPVGLPAIPENAVYI----------------------------MF-TSGSTGIPKGV 5783
Cdd:PRK07529   152 LAALPELRTVvEVDLARYLPGPKRLAVPLIRRKAHARIldfdaelarqpgdrlfsgrpigpddvaaYFhTGGTTGMPKLA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5784 VLEHRAVVTSCWGRGRAFGITnLSRVLQFASYTF--DACMDEIITTLMYGGCICVPSDSDRRNDLV-----KAISTMDVS 5856
Cdd:PRK07529   232 QHTHGNEVANAWLGALLLGLG-PGDTVFCGLPLFhvNALLVTGLAPLARGAHVVLATPQGYRGPGVianfwKIVERYRIN 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5857 CAlltpsvarllepSSVPTLQMLVLQ----GEQVS---FADWNRWPASV------------QTINGYGPTE--CSICCNT 5915
Cdd:PRK07529   311 FL------------SGVPTVYAALLQvpvdGHDISslrYALCGAAPLPVevfrrfeaatgvRIVEGYGLTEatCVSSVNP 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5916 YSGKQgfKSGIIG-----TSVASVswVVDPENHD-RLAPLGSIGELLVEGPILARGYLNDiQKTAAVFIDDpAWLlegyp 5989
Cdd:PRK07529   379 PDGER--RIGSVGlrlpyQRVRVV--ILDDAGRYlRDCAVDEVGVLCIAGPNVFSGYLEA-AHNKGLWLED-GWL----- 447
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5990 ghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVE----HHvreclpEARQLAVEVilpsGQKD-HA- 6063
Cdd:PRK07529   448 ----------NTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEeallRH------PAVALAAAV----GRPDaHAg 507
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6064 -MLAAFVQLEEGTQnalldkeasgedsmaqvVFLASVEEELAKRLPEH-MVPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:PRK07529   508 eLPVAYVQLKPGAS-----------------ATEAELLAFARDHIAERaAVPKHVRILDALPKTAVGKIFKPALRR 566
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
5632-6135 5.96e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 72.72  E-value: 5.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKAR-PHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 5710
Cdd:PRK13383    44 TAARwPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5711 HEDTFRHTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLGQLSTlvnpVGLPAIPENAVYIMFTSGSTGIPKGVvlEHRAV 5790
Cdd:PRK13383   124 LAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEES----GGRPAVAAPGRIVLLTSGTTGKPKGV--PRAPQ 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5791 VTScwGRGRAFGITNLSRV-----LQFASYTFDAC-MDEIITTLMYGGCICVPSDSDRRNDLVKAISTMDVSCALLTPSV 5864
Cdd:PRK13383   198 LRS--AVGVWVTILDRTRLrtgsrISVAMPMFHGLgLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVL 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5865 ARLLE-PSSV------PTLQMLVLQGEQVSFADWNRWPASVQTI--NGYGPTECSICCNTYSGKQGFKSGIIGTSVASVS 5935
Cdd:PRK13383   276 ARILElPPRVrarnplPQLRVVMSSGDRLDPTLGQRFMDTYGDIlyNGYGSTEVGIGALATPADLRDAPETVGKPVAGCP 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5936 WVVDPENHDRLAPlgsigelLVEGPILARGYLNDiqktaavfiddpawllEGYPGHPGRQ--GRLYKTGDLVRYDANGNL 6013
Cdd:PRK13383   356 VRILDRNNRPVGP-------RVTGRIFVGGELAG----------------TRYTDGGGKAvvDGMTSTGDMGYLDNAGRL 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6014 VCLGRKDSQVKLRGQRVELGEVEHHVrECLPEARQLAVeVILPSGQKDHaMLAAFVQLEEGtqnalldkeaSGEDSmaqv 6093
Cdd:PRK13383   413 FIVGREDDMIISGGENVYPRAVENAL-AAHPAVADNAV-IGVPDERFGH-RLAAFVVLHPG----------SGVDA---- 475
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 6094 vflASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 6135
Cdd:PRK13383   476 ---AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
5086-5146 6.67e-12

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 64.12  E-value: 6.67e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 5086 RTMQQLWTRVLGIELNGIGLDDSFFRLGGDSIAAMKLVGEARRT-GLQLSVADVFRHPRLVD 5146
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
5647-6036 6.70e-12

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 72.47  E-value: 6.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5647 ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTS 5726
Cdd:cd05914      7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5727 AqhsarwigtnhqvvtvsagslgqlstlvnpvglpaiPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNL 5806
Cdd:cd05914     87 D------------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKG 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5807 SRVLQFA--SYTFdACMDEIITTLMYGGCICVPSD--SDRRNDLVKAISTMDV-SCALLT----------PSVA------ 5865
Cdd:cd05914    131 DKILSILplHHIY-PLTFTLLLPLLNGAHVVFLDKipSAKIIALAFAQVTPTLgVPVPLViekifkmdiiPKLTlkkfkf 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5866 RLLEPSSVPTLQMLVLQGEQVSFADWNRW--------PASVQ----TIN-----GYGPTECS--ICcntYSGKQGFKSGI 5926
Cdd:cd05914    210 KLAKKINNRKIRKLAFKKVHEAFGGNIKEfviggakiNPDVEeflrTIGfpytiGYGMTETApiIS---YSPPNRIRLGS 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5927 IGTSVASVSWVVDPENhdrlaPLGSIGELLVEGPILARGYLNDIQKTAAVFIDDpAWLlegypghpgrqgrlyKTGDLVR 6006
Cdd:cd05914    287 AGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKD-GWF---------------HTGDLGK 345
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1820002560 6007 YDANGNLVCLGRKDSQVKL-RGQRVELGEVE 6036
Cdd:cd05914    346 IDAEGYLYIRGRKKEMIVLsSGKNIYPEEIE 376
PRK07514 PRK07514
malonyl-CoA synthase; Validated
7610-8005 7.17e-12

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 72.60  E-value: 7.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7610 HDLFA--EQARARPGAPAICAWDGE-LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP 7686
Cdd:PRK07514     3 NNLFDalRAAFADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7687 LDPDHPASRHEEIFEQTGAQVVVAS-----------AQYSARwtssscHVVTV----SKALSSQLPAVVDSTNTSVR-PE 7750
Cdd:PRK07514    83 LNTAYTLAELDYFIGDAEPALVVCDpanfawlskiaAAAGAP------HVETLdadgTGSLLEAAAAAPDDFETVPRgAD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7751 NAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNlSRVLQFASYTFDA---CIAeIITTLLCGG-CICVPS-DS 7825
Cdd:PRK07514   157 DLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTP-DDVLIHALPIFHThglFVA-TNVALLAGAsMIFLPKfDP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7826 DR-RNSLAKAISTMDVNwAFLTpsvaRLL-DPGLIPSLKI---LAIGGeqssSA--------DWNRWPGsvqkiHV---- 7888
Cdd:PRK07514   235 DAvLALMPRATVMMGVP-TFYT----RLLqEPRLTREAAAhmrLFISG----SApllaethrEFQERTG-----HAiler 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7889 YGPTEccifcTGYTTKQGFE----PSTIGTSVASVSW-VVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFI 7963
Cdd:PRK07514   301 YGMTE-----TNMNTSNPYDgerrAGTVGFPLPGVSLrVTDPETGAELPP-GEIGMIEVKGPNVFKGYWRMPEKTAEEFR 374
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 7964 DDpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLGR-KD 8005
Cdd:PRK07514   375 AD------GF----------FITGDLGKIDERGYVHIVGRgKD 401
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
45-186 7.24e-12

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 72.27  E-value: 7.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   45 SVQTINGYGPTE-CCIVCTGYTSEQDFT-TGTIGTSIASV-SWVVDPKDhGRLAPLGSVGELLVEGPILARGYLSDPEKT 121
Cdd:cd05904    301 NVDLGQGYGMTEsTGVVAMCFAPEKDRAkYGSVGRLVPNVeAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLNNPEAT 379
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  122 AAVfINNPAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHH 186
Cdd:cd05904    380 AAT-IDKEGWL---------------HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEAL 428
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
5717-6042 7.65e-12

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 72.25  E-value: 7.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5717 HTGAQVVVTSAQHSARWIGTNHQ-------VVTVSAgSLGQ--LSTLVNPVGLPAI-----PENAVYIMFTSGSTGIPKG 5782
Cdd:cd17639     27 LKPGDKVAIFAETRAEWLITALGcwsqnipIVTVYA-TLGEdaLIHSLNETECSAIftdgkPDDLACIMYTSGSTGNPKG 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5783 VVLEHRAVVTSCWGRGRAFGITN-----------LSRVLQFasyTFDACMdeiittLMYGGCICVPS-----DSDRRN-- 5844
Cdd:cd17639    106 VMLTHGNLVAGIAGLGDRVPELLgpddrylaylpLAHIFEL---AAENVC------LYRGGTIGYGSprtltDKSKRGck 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5845 -DLV------------------KAISTMDVSCALLTPSV---------ARLLEPSSVPTLQMLV------LQGEQVSFAD 5890
Cdd:cd17639    177 gDLTefkptlmvgvpaiwdtirKGVLAKLNPMGGLKRTLfwtayqsklKALKEGPGTPLLDELVfkkvraALGGRLRYML 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5891 WNRWPASVQT-----------INGYGPTEcSICCNTYSGKQGFKSGIIGTSVAS-----VSWvvdPE-NHDRLAPLGSiG 5953
Cdd:cd17639    257 SGGAPLSADTqeflnivlcpvIQGYGLTE-TCAGGTVQDPGDLETGRVGPPLPCceiklVDW---EEgGYSTDKPPPR-G 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5954 ELLVEGPILARGYLNDIQKTAAVFIDDpawllegypghpgrqgRLYKTGDLVRYDANGNLVCLGRKDSQVKLR-GQRVEL 6032
Cdd:cd17639    332 EILIRGPNVFKGYYKNPEKTKEAFDGD----------------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIAL 395
                          410
                   ....*....|
gi 1820002560 6033 GEVEHHVREC 6042
Cdd:cd17639    396 EKLESIYRSN 405
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
3456-3949 8.13e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 72.77  E-value: 8.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3456 PPAIERCVHDLFTEQAKARPHAPAIC-------AWDGeLTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAM 3528
Cdd:PRK12582    44 LGPYPRSIPHLLAKWAAEAPDRPWLAqrepghgQWRK-VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMT 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3529 LAVLKAGGAFVPLDP-------DHPASRH-------EEIFEQTGAQVvvASAQYSARWTSSSCHVVTVSKALSSQLP--- 3591
Cdd:PRK12582   123 LAAMQAGVPAAPVSPayslmshDHAKLKHlfdlvkpRVVFAQSGAPF--ARALAALDLLDVTVVHVTGPGEGIASIAfad 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3592 -------AVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHG--RAFG-ITNLSRVLQFA--SYTFDAC 3659
Cdd:PRK12582   201 laatpptAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEqlRPREpDPPPPVSLDWMpwNHTMGGN 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3660 IAeIITTLLCGGCICVpsDSDR-------------RNSLAKAISTMDVNWAFLTPSVARllDPGLIPS----LKILAIGG 3722
Cdd:PRK12582   281 AN-FNGLLWGGGTLYI--DDGKplpgmfeetirnlREISPTVYGNVPAGYAMLAEAMEK--DDALRRSffknLRLMAYGG 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3723 EQSSSADWNRwpgsVQKIHVYGPTECCIFCTGYTTKQgfepsTIGTSVaSVSWVVD---------PENHNRLAPLGSMGE 3793
Cdd:PRK12582   356 ATLSDDLYER----MQALAVRTTGHRIPFYTGYGATE-----TAPTTT-GTHWDTErvgliglplPGVELKLAPVGDKYE 425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3794 LLMEGPILARGYLNDVDKTEAAFiDDpawllEGYpghpgrqgrlYKTGDLVQY----NADGNLVYLGRKDSQVKV-RGQR 3868
Cdd:PRK12582   426 VRVKGPNVTPGYHKDPELTAAAF-DE-----EGF----------YRLGDAARFvdpdDPEKGLIFDGRVAEDFKLsTGTW 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3869 VELGEVEHH-VRECLPEARQLAVevilpSGQ-KDHAMLAAFVQLeEGTQNALLDKEAGGEDsmaqVVFLASVEEELAKRL 3946
Cdd:PRK12582   490 VSVGTLRPDaVAACSPVIHDAVV-----AGQdRAFIGLLAWPNP-AACRQLAGDPDAAPED----VVKHPAVLAILREGL 559

                   ...
gi 1820002560 3947 PEH 3949
Cdd:PRK12582   560 SAH 562
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
7753-8122 8.25e-12

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 70.82  E-value: 8.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7753 AYIIFTSGSTGVPKGVVLEHRAVATS---------CLGHGRAFGITNLSRVlqfasytfdACIAEIITTLLCGGCICVPs 7823
Cdd:cd17630      3 ATVILTSGSTGTPKAVVHTAANLLASaaglhsrlgFGGGDSWLLSLPLYHV---------GGLAILVRSLLAGAELVLL- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7824 dsDRRNSLAKAISTMDVNWAFLTPS-VARLLDPGLIP----SLKILAIGG--------EQSSSADWNRWPGsvqkihvYG 7890
Cdd:cd17630     73 --ERNQALAEDLAPPGVTHVSLVPTqLQRLLDSGQGPaalkSLRAVLLGGapippellERAADRGIPLYTT-------YG 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7891 PTEcciFCTGYTTKQ--GFEPSTIGtsvasvswVVDPENHNRLAPlgsMGELLMEGPILARGYLNDVDKTEAafiDDPAW 7968
Cdd:cd17630    144 MTE---TASQVATKRpdGFGRGGVG--------VLLPGRELRIVE---DGEIWVGGASLAMGYLRGQLVPEF---NEDGW 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7969 llegypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE------HHVREC----LPEAR--QLAV 8036
Cdd:cd17630    207 ---------------FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEaalaahPAVRDAfvvgVPDEElgQRPV 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8037 EVILPSGQKNHAMLAVFVQlgkgthiahleekaggedsmaqvvfltgteeelaKRLPKHMVPTVFFALLHFPMTTSGKAD 8116
Cdd:cd17630    272 AVIVGRGPADPAELRAWLK----------------------------------DKLARFKLPKRIYPVPELPRTGGGKVD 317

                   ....*.
gi 1820002560 8117 RKRLRE 8122
Cdd:cd17630    318 RRALRA 323
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
3447-3881 8.50e-12

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 72.36  E-value: 8.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3447 KIW------GWNADVPPAIERCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEK 3520
Cdd:PRK07059     3 KIWlksyppGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3521 SMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVV-----ASAQYSARWTSSSCHVVTVS------------ 3583
Cdd:PRK07059    83 VLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVvlenfATTVQQVLAKTAVKHVVVASmgdllgfkghiv 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3584 -------KAL--SSQLPAVVdSTNTSVR-------------PENAAYIIFTSGSTGVPKGVVLEHR----AVATSCLGHG 3637
Cdd:PRK07059   163 nfvvrrvKKMvpAWSLPGHV-RFNDALAegarqtfkpvklgPDDVAFLQYTGGTTGVSKGATLLHRnivaNVLQMEAWLQ 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3638 RAF----GITNLSRVLQFASYTFDACIAEIITTLLCGGC-ICVPSDSDRRnSLAKAISTMDVNwafLTPSV-----ARLL 3707
Cdd:PRK07059   242 PAFekkpRPDQLNFVCALPLYHIFALTVCGLLGMRTGGRnILIPNPRDIP-GFIKELKKYQVH---IFPAVntlynALLN 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3708 DPGL----IPSLKILAIGGEQSSSADWNRWpgsVQKIHV-----YGPTEC--CIFCTGYTTKQgFEpSTIGTSVASVSWV 3776
Cdd:PRK07059   318 NPDFdkldFSKLIVANGGGMAVQRPVAERW---LEMTGCpitegYGLSETspVATCNPVDATE-FS-GTIGLPLPSTEVS 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3777 VDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLG 3856
Cdd:PRK07059   393 IRDDDGNDL-PLGEPGEICIRGPQVMAGYWNRPDETAKVMTAD------GF----------FRTGDVGVMDERGYTKIVD 455
                          490       500
                   ....*....|....*....|....*
gi 1820002560 3857 RKDSQVKVRGQRVELGEVEHHVREC 3881
Cdd:PRK07059   456 RKKDMILVSGFNVYPNEIEEVVASH 480
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
6850-7042 8.67e-12

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 71.72  E-value: 8.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6850 APLGSIGELLVEGPILARGYLNDADKTAAAFvndpawlveghgkhpgrRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVR 6929
Cdd:cd05919    281 IPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-----------------NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6930 GQRVELGEIENRLRECMPRATQMAVEVISPAGAaeqakTMVVAFLQLNDEArdallggnvPNDDNLSAQvvfpakVDEKL 7009
Cdd:cd05919    344 GQWVSPVEVESLIIQHPAVAEAAVVAVPESTGL-----SRLTAFVVLKSPA---------APQESLARD------IHRHL 403
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1820002560 7010 SNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLR 7042
Cdd:cd05919    404 LERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
PRK06164 PRK06164
acyl-CoA synthetase; Validated
85-296 8.77e-12

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 72.47  E-value: 8.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   85 VVDPKDhGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNpawlleghgGYagrqgrlYKTGDLVRYDADGNLVCL 164
Cdd:PRK06164   363 ARDPQD-GALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDD---------GY-------FRTGDLGYTRGDGQFVYQ 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  165 GRKDSQVKLRGQRVELGEVEHHVREClpEAKQLAVEVVLPLGQKNHAtlAAFIQLDKGTHNAllkekvggddsiarvvfL 244
Cdd:PRK06164   426 TRMGDSLRLGGFLVNPAEIEHALEAL--PGVAAAQVVGATRDGKTVP--VAFVIPTDGASPD-----------------E 484
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  245 AGVEEELAKRLPKHMVPTVFFALLHFPTTTSG---KTDRKRLREIGASFTAQQLA 296
Cdd:PRK06164   485 AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQARLAAERA 539
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
2066-2444 1.03e-11

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 71.89  E-value: 1.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2066 DLPAKPENAAYVM-FTSGSTGTPKGVVLEHRAVVTSCLGhGQAFGVTNLlralqftaYTFDVCIaeIITTLVH------- 2137
Cdd:cd12119    156 DWPDFDENTAAAIcYTSGTTGNPKGVVYSHRSLVLHAMA-ALLTDGLGL--------SESDVVL--PVVPMFHvnawglp 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2138 ------GGCICVPSDSERRDNLAKAITDMQVNWGYLTSSVARLLDPCL------VPSLKVLVLGGEQVnstdwgkwPSS- 2204
Cdd:cd12119    225 yaaamvGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLeangrdLSSLRRVVIGGSAV--------PRSl 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2205 --------VQTINGYGPTECCVFCT--GYTGIQGFQSG--------NIGTSIASVSW-VVDPEnhGRLAPL--GSIGELL 2263
Cdd:cd12119    297 ieafeergVRVIHAWGMTETSPLGTvaRPPSEHSNLSEdeqlalraKQGRPVPGVELrIVDDD--GRELPWdgKAVGELQ 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2264 VEGPILARGYLNDVDKTQAAFIDDpaWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLGR-KDSqVKVRGQ---RVEL 2339
Cdd:cd12119    375 VRGPWVTKSYYKNDEESEALTEDG--WL---------------RTGDVATIDEDGYLTITDRsKDV-IKSGGEwisSVEL 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2340 gE---VEHhmrkclPEANQLAVEVVPPS--GERDhamlAAFIRLDDETRNSPliikyaednstaqivflTGIEEELSERL 2414
Cdd:cd12119    437 -EnaiMAH------PAVAEAAVIGVPHPkwGERP----LAVVVLKEGATVTA-----------------EELLEFLADKV 488
                          410       420       430
                   ....*....|....*....|....*....|
gi 1820002560 2415 PQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:cd12119    489 AKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2559-2695 1.10e-11

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 71.37  E-value: 1.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2559 FDLTPIQHLYLtldpSGRSSfDQ------C-FFLELRNR-VQPQLLVTALTALVQRHSMLRARFQRQtgGRwQQYISEHD 2630
Cdd:cd19535      2 FPLTDVQYAYW----IGRQD-DQelggvgChAYLEFDGEdLDPDRLERAWNKLIARHPMLRAVFLDD--GT-QQILPEVP 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 2631 SSSLIVNHIHTRDTTEIVEALRQSRGS-----LDIERGPV--LAAVLCDAGeRQSLFVAIHHLVVDLVSWRI 2695
Cdd:cd19535     74 WYGITVHDLRGLSEEEAEAALEELRERlshrvLDVERGPLfdIRLSLLPEG-RTRLHLSIDLLVADALSLQI 144
PRK08316 PRK08316
acyl-CoA synthetase; Validated
1933-2444 1.26e-11

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 71.89  E-value: 1.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP---- 2008
Cdd:PRK08316    15 DILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPvnfm 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2009 LDPDHPASrhedIFRQTGAQVVVTSAQ-----HSARWIGTNHQVV-------TVSAGSLEQFSTL-----VNPVDLPAKP 2071
Cdd:PRK08316    95 LTGEELAY----ILDHSGARAFLVDPAlaptaEAALALLPVDTLIlslvlggREAPGGWLDFADWaeagsVAEPDVELAD 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2072 ENAAYVMFTSGSTGTPKGVVLEHRAVV---TSC---------------------------LGHGQAFGVTNLLRALQFTA 2121
Cdd:PRK08316   171 DDLAQILYTSGTESLPKGAMLTHRALIaeyVSCivagdmsaddiplhalplyhcaqldvfLGPYLYVGATNVILDAPDPE 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2122 YTFDVCIAEIITTLvhggcICVPS---------DSERRD--NLAKaitdmqvnwGYLTSSVArlldPclVPSLKVLvlgg 2190
Cdd:PRK08316   251 LILRTIEAERITSF-----FAPPTvwisllrhpDFDTRDlsSLRK---------GYYGASIM----P--VEVLKEL---- 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2191 eQVNSTDWGKWpssvqtiNGYGPTECCVFCT--------GYTGIQGFQSGNIGTSIasvswvVDPEnhGRLAPLGSIGEL 2262
Cdd:PRK08316   307 -RERLPGLRFY-------NCYGQTEIAPLATvlgpeehlRRPGSAGRPVLNVETRV------VDDD--GNDVAPGEVGEI 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2263 LVEGPILARGYLNDVDKTQAAFIDDpaWllegypghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEV 2342
Cdd:PRK08316   371 VHRSPQLMLGYWDDPEKTAEAFRGG--W---------------FHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREV 433
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2343 EhhmrkclpeanqlavEVV---PPSGErdhamlAAFIRLDDEtrnspliiKYAEdNSTAQIVFLTGI---EEEL----SE 2412
Cdd:PRK08316   434 E---------------EALythPAVAE------VAVIGLPDP--------KWIE-AVTAVVVPKAGAtvtEDELiahcRA 483
                          570       580       590
                   ....*....|....*....|....*....|...
gi 1820002560 2413 RLPQHMVP-TVFFALVhFPTTTSGKTDRKRLRE 2444
Cdd:PRK08316   484 RLAGFKVPkRVIFVDE-LPRNPSGKILKRELRE 515
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
4551-5054 1.45e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 71.57  E-value: 1.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARAR-PDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 4629
Cdd:PRK13383    44 TAARwPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4630 HEHIFRQTGAQVVLASAQYATLWTSLGRSVVIVSEASTSqlpVVTKTADPSVNPgNAAYAIFTSGSTGIPKGVvlEHKAV 4709
Cdd:PRK13383   124 LAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAG---AEESGGRPAVAA-PGRIVLLTSGTTGKPKGV--PRAPQ 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4710 VTSclGHGQAFGITDHTRV-----LQFASYTFDAC-IAEIITTLLCCGCICVPSDSDRRNNLAKAINAMDVNWALLTPSV 4783
Cdd:PRK13383   198 LRS--AVGVWVTILDRTRLrtgsrISVAMPMFHGLgLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVL 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4784 ARMLD-PCVVQS------LKILVLGGEQVNSADWDRWPKSIQTI--NAYGPTECSICCTTYSGKQGFKSGTIGTSIVSVS 4854
Cdd:PRK13383   276 ARILElPPRVRArnplpqLRVVMSSGDRLDPTLGQRFMDTYGDIlyNGYGSTEVGIGALATPADLRDAPETVGKPVAGCP 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4855 WVVDPENHNRLAPLGSiGELLVEGPILARGYlndmekteaafiddpawllEGYGGHSGRQGrLYKTGDLVRYDADGNLVY 4934
Cdd:PRK13383   356 VRILDRNNRPVGPRVT-GRIFVGGELAGTRY-------------------TDGGGKAVVDG-MTSTGDMGYLDNAGRLFI 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4935 LGRKDSQVKLRGQRVELGEVEHHVRECLTEAKQLAVEviVPEGEGGYaMLAAFVQLgddtyntlvkeKAGGDsltvqvVF 5014
Cdd:PRK13383   415 VGREDDMIISGGENVYPRAVENALAAHPAVADNAVIG--VPDERFGH-RLAAFVVL-----------HPGSG------VD 474
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1820002560 5015 LDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRL 5054
Cdd:PRK13383   475 AAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
7602-7992 1.48e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 71.62  E-value: 1.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7602 PPAIERCVHDLFAEQARARPGAPAIC-------AWDGeLTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAM 7674
Cdd:PRK12582    44 LGPYPRSIPHLLAKWAAEAPDRPWLAqrepghgQWRK-VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMT 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7675 LAVLKAGGAFVPLDP-------DHPASRH-------EEIFEQTGAQVvvASAQYSARWTSSSCHVVTVSKALSSQLP--- 7737
Cdd:PRK12582   123 LAAMQAGVPAAPVSPayslmshDHAKLKHlfdlvkpRVVFAQSGAPF--ARALAALDLLDVTVVHVTGPGEGIASIAfad 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7738 -------AVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHG--RAFG-ITNLSRVLQFA--SYTFDAC 7805
Cdd:PRK12582   201 laatpptAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEqlRPREpDPPPPVSLDWMpwNHTMGGN 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7806 IAeIITTLLCGGCICVpsDSDR-------------RNSLAKAISTMDVNWAFLTPSVARllDPGLIPS----LKILAIGG 7868
Cdd:PRK12582   281 AN-FNGLLWGGGTLYI--DDGKplpgmfeetirnlREISPTVYGNVPAGYAMLAEAMEK--DDALRRSffknLRLMAYGG 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7869 EQSSSADWNRwpgsVQKIHVYGPTECCIFCTGYTTKQgfepsTIGTSVaSVSWVVD---------PENHNRLAPLGSMGE 7939
Cdd:PRK12582   356 ATLSDDLYER----MQALAVRTTGHRIPFYTGYGATE-----TAPTTT-GTHWDTErvgliglplPGVELKLAPVGDKYE 425
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 7940 LLMEGPILARGYLNDVDKTEAAFiDDpawllEGYpghpgrqgrlYKTGDLVQY 7992
Cdd:PRK12582   426 VRVKGPNVTPGYHKDPELTAAAF-DE-----EGF----------YRLGDAARF 462
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
6167-6227 1.50e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 62.97  E-value: 1.50e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 6167 QTMQKLWAQVLGIELNGIGLDDSFFRLGGDSIAAMKLVGEARR-IGLQLSVADIFRYARLVD 6227
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEeFGVEIPPSDLFEHPTLAE 62
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
878-1272 1.69e-11

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 71.09  E-value: 1.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKREDVVPL--------------CFEKSMwTVVAMLAVLkaggafvpldpGHPASRHEe 943
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIfaetraewlitalgCWSQNI-PIVTVYATL-----------GEDALIHS- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  944 iFKQIGAQVVLTSSqhamlfasserhqvtvskvstsqlptvvnfakSPVDPgntAYIIFTSGTTGIPKGVVLQHRAVTTS 1023
Cdd:cd17639     73 -LNETECSAIFTDG--------------------------------KPDDL---ACIMYTSGSTGNPKGVMLTHGNLVAG 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1024 CLGHGEA-----------FGYTDHARVLQFAsytfdaciAEIIttLLYGGC----------------------------- 1063
Cdd:cd17639    117 IAGLGDRvpellgpddryLAYLPLAHIFELA--------AENV--CLYRGGtigygsprtltdkskrgckgdltefkptl 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1064 -ICVPS--ESDRRNNLAKaistmdVNCA-LLTPSV---------ARLLEPSAVPSLKRLV------LQGEQVSF------ 1118
Cdd:cd17639    187 mVGVPAiwDTIRKGVLAK------LNPMgGLKRTLfwtayqsklKALKEGPGTPLLDELVfkkvraALGGRLRYmlsgga 260
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1119 ---ADWNRWPGSV--QTINGYGPTEcSVCCNTYSGKQGFKSGIIGTSVAS-----LSWvvDAGNHNRLAPLGSiGELLVE 1188
Cdd:cd17639    261 plsADTQEFLNIVlcPVIQGYGLTE-TCAGGTVQDPGDLETGRVGPPLPCceiklVDW--EEGGYSTDKPPPR-GEILIR 336
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1189 GPILARGYLNDIDKTEAAFIDDpawllegyeghagrrgRLYKTGDLVRCDADGNLVCLGRKDSQVKVR-GQRVELGEIEH 1267
Cdd:cd17639    337 GPNVFKGYYKNPEKTKEAFDGD----------------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLES 400

                   ....*
gi 1820002560 1268 HVREC 1272
Cdd:cd17639    401 IYRSN 405
PRK07529 PRK07529
AMP-binding domain protein; Validated
4514-5056 1.72e-11

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 71.52  E-value: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4514 VAGIETTTTGDRqqlwawnqDVPpaieRCVHDQFAEQARARPDTPAIC------AWDG--ELTYGELDTLSSKLASHLVQ 4585
Cdd:PRK07529    10 IEAIEAVPLAAR--------DLP----ASTYELLSRAAARHPDAPALSflldadPLDRpeTWTYAELLADVTRTANLLHS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4586 LGVKPEDMV----PLCFEksmwTVVAMLAVLKAGGAFvP----LDPDHPAsrheHIFRQTGAQVVLASAQY--ATLWTSL 4655
Cdd:PRK07529    78 LGVGPGDVVafllPNLPE----THFALWGGEAAGIAN-PinplLEPEQIA----ELLRAAGAKVLVTLGPFpgTDIWQKV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4656 ---------GRSVVIVS---------------------------EASTSQLPVVTKTADPSVNPGNAAyAIF-TSGSTGI 4698
Cdd:PRK07529   149 aevlaalpeLRTVVEVDlarylpgpkrlavplirrkaharildfDAELARQPGDRLFSGRPIGPDDVA-AYFhTGGTTGM 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4699 PKGVVLEHKAVVTSCLGHGQAFGItDHTRVLQFASYTF--DACIAEIITTLLCCGCICVPSDSDRRN-----NLAKAINA 4771
Cdd:PRK07529   228 PKLAQHTHGNEVANAWLGALLLGL-GPGDTVFCGLPLFhvNALLVTGLAPLARGAHVVLATPQGYRGpgviaNFWKIVER 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4772 MDVNWALLTPSVARML-----DPCVVQSLKILVLGGEQVNSADWDRWPKS--IQTINAYGPTE--CSICCTTYSGKQgfK 4842
Cdd:PRK07529   307 YRINFLSGVPTVYAALlqvpvDGHDISSLRYALCGAAPLPVEVFRRFEAAtgVRIVEGYGLTEatCVSSVNPPDGER--R 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4843 SGTIG-------TSIVsvswVVDPENHN-RLAPLGSIGELLVEGPILARGYLNDmEKTEAAFIDDpAWLlegygghsgrq 4914
Cdd:PRK07529   385 IGSVGlrlpyqrVRVV----ILDDAGRYlRDCAVDEVGVLCIAGPNVFSGYLEA-AHNKGLWLED-GWL----------- 447
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4915 grlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE----HHvrecltEAKQLAVEVIVPEGEGGyAMLAAFVQL 4990
Cdd:PRK07529   448 ----NTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEeallRH------PAVALAAAVGRPDAHAG-ELPVAYVQL 516
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 4991 gddtyntlvkeKAGGdSLTVQVVfLDRVEEELAKR--VPEHMMLttfftLEAMPTTTSGKIDRKRLRE 5056
Cdd:PRK07529   517 -----------KPGA-SATEAEL-LAFARDHIAERaaVPKHVRI-----LDALPKTAVGKIFKPALRR 566
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
3446-3976 1.72e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 71.60  E-value: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3446 KKIW--GWNADVPPAIERCVHDL--FTEQAKAR-PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEK 3520
Cdd:PRK06710     4 EKPWlkSYPEEIPSTISYDIQPLhkYVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3521 SMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVV---------VASAQYSAR-------------------- 3571
Cdd:PRK06710    84 CPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlcldlvfprVTNVQSATKiehvivtriadflpfpknll 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3572 ----WTSSSCHVVTVSKALSSQL-PAVVDSTNTSVR----PEN-AAYIIFTSGSTGVPKGVVLEHRAVATSCLghgraFG 3641
Cdd:PRK06710   164 ypfvQKKQSNLVVKVSESETIHLwNSVEKEVNTGVEvpcdPENdLALLQYTGGTTGFPKGVMLTHKNLVSNTL-----MG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3642 ITNLSRVLQ-----------FASYTFDACIAeiiTTLLCGGCICVPSDSDRRnSLAKAISTMDVNWAFLTPSV-ARLLDP 3709
Cdd:PRK06710   239 VQWLYNCKEgeevvlgvlpfFHVYGMTAVMN---LSIMQGYKMVLIPKFDMK-MVFEAIKKHKVTLFPGAPTIyIALLNS 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3710 GLIPSLKILAIGGEQSSSADWnrwPGSVQK----------IHVYGPTECCIFCTGYTTKQGFEPSTIGtsvasVSW---- 3775
Cdd:PRK06710   315 PLLKEYDISSIRACISGSAPL---PVEVQEkfetvtggklVEGYGLTESSPVTHSNFLWEKRVPGSIG-----VPWpdte 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3776 --VVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDdpAWLlegypghpgrqgrlyKTGDLVQYNADGNLV 3853
Cdd:PRK06710   387 amIMSLETGEALPP-GEIGEIVVKGPQIMKGYWNKPEETAAVLQD--GWL---------------HTGDVGYMDEDGFFY 448
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3854 YLGRKDSQVKVRGQRVELGEVEHHVREclPEARQLAVEVILPSGQKDHAmLAAFVQLEEGTQNAlldkeaggedsmaqvv 3933
Cdd:PRK06710   449 VKDRKKDMIVASGFNVYPREVEEVLYE--HEKVQEVVTIGVPDPYRGET-VKAFVVLKEGTECS---------------- 509
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 3934 flasvEEEL----AKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:PRK06710   510 -----EEELnqfaRKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
4559-5056 1.81e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 71.09  E-value: 1.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4559 AICAWDGE-LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQT 4637
Cdd:PRK08276     3 VIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4638 GAQVVLASAQYATLWTSLgrsvvivseASTSQLPVVTKTADPSVNPGNAAYA--------------------IFTSGSTG 4697
Cdd:PRK08276    83 GAKVLIVSAALADTAAEL---------AAELPAGVPLLLVVAGPVPGFRSYEealaaqpdtpiadetagadmLYSSGTTG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4698 IPKGVV--LEHKAVVTSCLGH----GQAFGITD-----------HTRVLQFASYT------------FDA--CIAEI--- 4743
Cdd:PRK08276   154 RPKGIKrpLPGLDPDEAPGMMlallGFGMYGGPdsvylspaplyHTAPLRFGMSAlalggtvvvmekFDAeeALALIery 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4744 -ITTLLccgciCVPSDSDRRNNLAKAI-NAMDVN---WALLT-----PSV-ARMLD---PCVVQSLKILVLGGEQV-NSA 4808
Cdd:PRK08276   234 rVTHSQ-----LVPTMFVRMLKLPEEVrARYDVSslrVAIHAaapcpVEVkRAMIDwwgPIIHEYYASSEGGGVTViTSE 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4809 DWDRWPksiqtinaygptecsiccttysgkqgfksGTIGTSIVSVSWVVDpENHNRLAPlGSIGELLVEGPILARGYLND 4888
Cdd:PRK08276   309 DWLAHP-----------------------------GSVGKAVLGEVRILD-EDGNELPP-GEIGTVYFEMDGYPFEYHND 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4889 MEKTEAAFIDDpawllegygghsgrqgRLYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHhvrECLTEAKQL 4968
Cdd:PRK08276   358 PEKTAAARNPH----------------GWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIEN---LLVTHPKVA 418
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4969 AVEVI-VPEGEGGYAMLAAfVQLGDDTyntlvkekAGGDSLTVQVvfLDRVEEELAK-RVPEhmmltTFFTLEAMPTTTS 5046
Cdd:PRK08276   419 DVAVFgVPDEEMGERVKAV-VQPADGA--------DAGDALAAEL--IAWLRGRLAHyKCPR-----SIDFEDELPRTPT 482
                          570
                   ....*....|
gi 1820002560 5047 GKIDRKRLRE 5056
Cdd:PRK08276   483 GKLYKRRLRD 492
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
6841-7042 1.91e-11

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 70.93  E-value: 1.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6841 FVRPSNAALAPLGSIGELLVEGPILARGYLNDadktaaafvndpawlvEGHGKHPGRRGRLYKTGDLVYYNKDGNLVYIG 6920
Cdd:cd05922    298 EILDDDGTPTPPGEPGEIVHRGPNVMKGYWND----------------PPYRRKEGRGGGVLHTGDLARRDEDGFLFIVG 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6921 RKDGQVKVRGQRVELGEIENRLRECMPRATQMAVEVISPAGAAeqaktmVVAFLQLNDEardallggnvpnddnlsaqvV 7000
Cdd:cd05922    362 RRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEK------LALFVTAPDK--------------------I 415
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 7001 FPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLR 7042
Cdd:cd05922    416 DPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
5626-6139 1.95e-11

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 71.44  E-value: 1.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGG--AFV--- 5700
Cdd:PRK08279    41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLntq 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5701 ----PL-------DPDHPASRHE--DTFRHTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLGQLSTLVNPVGLPAIP--E 5765
Cdd:PRK08279   121 qrgaVLahslnlvDAKHLIVGEElvEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTakD 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5766 NAVYImFTSGSTGIPKGVVLEHRAVVtsCWGRGRAfGITNLSR----------------------VL----------QFA 5813
Cdd:PRK08279   201 TAFYI-YTSGTTGLPKAAVMSHMRWL--KAMGGFG-GLLRLTPddvlycclplyhntggtvawssVLaagatlalrrKFS 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5814 SYTFdacMDEII----TTLMYGGCIC------VPSDSDRRNDLVKAIStmdvscALLTPSVarllepssvptlqmlvlqg 5883
Cdd:PRK08279   277 ASRF---WDDVRryraTAFQYIGELCryllnqPPKPTDRDHRLRLMIG------NGLRPDI------------------- 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5884 eqvsfadWNRWPA--SVQTI-NGYGPTECSIC-CN--TYSGKQGFKSGIIGTSVASVSWVVDPENHDR-------LAPLG 5950
Cdd:PRK08279   329 -------WDEFQQrfGIPRIlEFYAASEGNVGfINvfNFDGTVGRVPLWLAHPYAIVKYDVDTGEPVRdadgrciKVKPG 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5951 SIGELLveGPILAR----GYlNDIQKTAA-----VFIDDPAWllegypghpgrqgrlYKTGDLVRYDANGNLVCLGRKDS 6021
Cdd:PRK08279   402 EVGLLI--GRITDRgpfdGY-TDPEASEKkilrdVFKKGDAW---------------FNTGDLMRDDGFGHAQFVDRLGD 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6022 QVKLRGQRVELGEVEhhvreclpearqlavevilpsgqkdhAMLAAFVQLEEGTQNALLDKEASGEDSMAQVVF------ 6095
Cdd:PRK08279   464 TFRWKGENVATTEVE--------------------------NALSGFPGVEEAVVYGVEVPGTDGRAGMAAIVLadgaef 517
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 6096 -LASVEEELAKRLPEHMVPtVFFSLL-HFPTTTSGKTDRKRLREIG 6139
Cdd:PRK08279   518 dLAALAAHLYERLPAYAVP-LFVRLVpELETTGTFKYRKVDLRKEG 562
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
878-1274 2.09e-11

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 71.23  E-value: 2.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKR-EDVVPLCFEKSMWTVVAMLAVLkAGGAFVPLDPGHPASRHEEIFKQIGAQVVLTS 956
Cdd:cd05933      9 LTYKEYYEACRQAAKAFLKLGLERfHGVGILGFNSPEWFIAAVGAIF-AGGIAVGIYTTNSPEACQYVAETSEANILVVE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  957 SQHAM-----------------------------LFASSERHQVTVSkVSTSQLPTVVnfakSPVDPGNTAYIIFTSGTT 1007
Cdd:cd05933     88 NQKQLqkilqiqdklphlkaiiqykeplkekepnLYSWDEFMELGRS-IPDEQLDAII----SSQKPNQCCTLIYTSGTT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1008 GIPKGVVLQHRAVTTSCLGHGEAFGYtDHARVLQ--FASYT----FDACIAEIITTLLYGGCICVPSESDRRNNLAKAIS 1081
Cdd:cd05933    163 GMPKGVMLSHDNITWTAKAASQHMDL-RPATVGQesVVSYLplshIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKTLR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1082 TMDVNCALLTPSV-----ARLLEPSAVPS-LKRLVLQ-----GEQVSFADWN---------RW----------------- 1124
Cdd:cd05933    242 EVRPTAFMGVPRVwekiqEKMKAVGAKSGtLKRKIASwakgvGLETNLKLMGgespsplfyRLakklvfkkvrkalgldr 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1125 ---------PGSVQTIN-----------GYGPTECSvCCNTYSGKQGFKSGIIGTSVASLSWVVDAGNHNrlaplgSIGE 1184
Cdd:cd05933    322 cqkfftgaaPISRETLEfflslnipimeLYGMSETS-GPHTISNPQAYRLLSCGKALPGCKTKIHNPDAD------GIGE 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1185 LLVEGPILARGYLNDIDKTEAAfIDDPAWLlegyegHagrrgrlykTGDLVRCDADGNLVCLGR-KDSQVKVRGQRVELG 1263
Cdd:cd05933    395 ICFWGRHVFMGYLNMEDKTEEA-IDEDGWL------H---------SGDLGKLDEDGFLYITGRiKELIITAGGENVPPV 458
                          490
                   ....*....|.
gi 1820002560 1264 EIEHHVRECLP 1274
Cdd:cd05933    459 PIEDAVKKELP 469
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
450-718 2.20e-11

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 70.37  E-value: 2.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  450 VLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLlQVVVEEK------MQW-TESESLEEYLNEDKAASMGLGDR 522
Cdd:cd19538     29 VIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPY-QLILEEDeatpklEIKeVDEEELESEINEAVRYPFDLSEE 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  523 LARYALIKESCGGKRWFVWTIHHALYDGWSL-PLVLDaVKQVYSGAALERQPSFNTF-IQY----VSQQ----------- 585
Cdd:cd19538    108 PPFRATLFELGENEHVLLLLLHHIAADGWSLaPLTRD-LSKAYRARCKGEAPELAPLpVQYadyaLWQQellgdesdpds 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  586 DVKAAAAYWQTALADCEAVLfpPLPSTVTQPVADT----TVKYQCPP------SPEVTSSNITTSTLIRAAWAIIASRYT 655
Cdd:cd19538    187 LIARQLAYWKKQLAGLPDEI--ELPTDYPRPAESSyeggTLTFEIDSelhqqlLQLAKDNNVTLFMVLQAGFAALLTRLG 264
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  656 SSEDIVFGTTVTGRNApiTGVEAMVGPTIATVPLRVrprkgqTVS---AFLENLQQ-QATEMIAYEQ 718
Cdd:cd19538    265 AGTDIPIGSPVAGRND--DSLEDLVGFFVNTLVLRT------DTSgnpSFRELLERvKETNLEAYEH 323
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
3484-3859 2.22e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 71.30  E-value: 2.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3484 DG---ELTYGELDALSSKLASHLVQLGvNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL-DPDHPAsrHEEIFeqtga 3559
Cdd:PRK07769    50 DGvarDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPG--HVGRL----- 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3560 QVVVASAQYSARWTSSSChVVTVSKALSSqLPA-------VVDSTNTSV-----RPE----NAAYIIFTSGSTGVPKGVV 3623
Cdd:PRK07769   122 HAVLDDCTPSAILTTTDS-AEGVRKFFRA-RPAkerprviAVDAVPDEVgatwvPPEanedTIAYLQYTSGSTRIPAGVQ 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3624 LEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICV--PSDSDRR-----NSLAK----AISTM 3692
Cdd:PRK07769   200 ITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFmsPAAFVRRpgrwiRELARkpggTGGTF 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3693 DV--NWAFlTPSVARLLDPGLIPSL-----KILAIGGEQSSSADWNRW-----PGSVQKIHV---YGPTECCIFCTgyTT 3757
Cdd:PRK07769   280 SAapNFAF-EHAAARGLPKDGEPPLdlsnvKGLLNGSEPVSPASMRKFneafaPYGLPPTAIkpsYGMAEATLFVS--TT 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3758 KQGFEPSTI-------------------GTSVASVS--------W--VVDPENHNRLaPLGSMGELLMEGPILARGYLND 3808
Cdd:PRK07769   357 PMDEEPTVIyvdrdelnagrfvevpadaPNAVAQVSagkvgvseWavIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGK 435
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 3809 VDKTEAAF----------------IDDPAWLlegypghpgrqgrlyKTGDLVQYnADGNLVYLGR-KD 3859
Cdd:PRK07769   436 PEETAATFqnilksrlseshaegaPDDALWV---------------RTGDYGVY-FDGELYITGRvKD 487
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4566-4942 2.35e-11

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 70.57  E-value: 2.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4566 ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPdhpasrhehifrqtgaqvvlas 4645
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP---------------------- 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4646 aqyatlwtSLGRSVVI--VSEASTSQLPVVTKTADPsvnpgnaAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGIT 4723
Cdd:cd05910     60 --------GMGRKNLKqcLQEAEPDAFIGIPKADEP-------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIR 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4724 DHTRVLQ----FAsyTFDACIAeiITTLLCCGCICVPSDSDRRNnLAKAINAMDVNWALLTPSV-ARMLDPCVVQ----- 4793
Cdd:cd05910    125 PGEVDLAtfplFA--LFGPALG--LTSVIPDMDPTRPARADPQK-LVGAIRQYGVSIVFGSPALlERVARYCAQHgitlp 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4794 SLKILVLGGEQVNSADWDRWPKSI----QTINAYGPTEC----SI------CCTTYSGKQGfkSGT-IGTSIVSVSWVV- 4857
Cdd:cd05910    200 SLRRVLSAGAPVPIALAARLRKMLsdeaEILTPYGATEAlpvsSIgsrellATTTAATSGG--AGTcVGRPIPGVRVRIi 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4858 ------DPENHNRLA-PLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPawllegygghsgRQGRLYKTGDLVRYDADG 4930
Cdd:cd05910    278 eiddepIAEWDDTLElPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN------------SEGFWHRMGDLGYLDDEG 345
                          410
                   ....*....|..
gi 1820002560 4931 NLVYLGRKDSQV 4942
Cdd:cd05910    346 RLWFCGRKAHRV 357
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1933-2451 2.57e-11

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 70.79  E-value: 2.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAkaRPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPED--VVPLCFEKSMWtvVAMLAVLKAGgaFVPLD 2010
Cdd:PRK10946    29 DILTRHA--ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDtaLVQLGNVAEFY--ITFFALLKLG--VAPVN 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2011 PDHPASRHE--DIFRQTGAQVVVTSAQHS------------ARWIGTNHqVVTVSAGSLEQFSTLVN--PVDLPAKPENA 2074
Cdd:PRK10946   103 ALFSHQRSElnAYASQIEPALLIADRQHAlfsdddflntlvAEHSSLRV-VLLLNDDGEHSLDDAINhpAEDFTATPSPA 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2075 AYVMF---TSGSTGTPKGVVLEH-------RAVVTSClghgqAFGV-TNLLRALQfTAYTFDVCIAEIITTLVHGGCICV 2143
Cdd:PRK10946   182 DEVAFfqlSGGSTGTPKLIPRTHndyyysvRRSVEIC-----GFTPqTRYLCALP-AAHNYPMSSPGALGVFLAGGTVVL 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2144 PSDSErRDNLAKAITDMQVNWGYLT-SSVARLLDPCLVP-------SLKVLVLGGEQVNSTDWGKWPSSV--QTINGYGP 2213
Cdd:PRK10946   256 APDPS-ATLCFPLIEKHQVNVTALVpPAVSLWLQAIAEGgsraqlaSLKLLQVGGARLSETLARRIPAELgcQLQQVFGM 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2214 TECCVfctGYTGIQGFQSGNIGTSIASVS-----WVVDpeNHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFiDDp 2288
Cdd:PRK10946   335 AEGLV---NYTRLDDSDERIFTTQGRPMSpddevWVAD--ADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAF-DA- 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2289 awllEGYpghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEH----HmrkclPEANQLAVEVVPPS 2364
Cdd:PRK10946   408 ----NGF----------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENlllrH-----PAVIHAALVSMEDE 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2365 --GERDhamlAAFIRLDDETRnSPLIIKYAEDNSTAQIvfltgieeelseRLPQHmvptvFFALVHFPTTTSGKTDRKRL 2442
Cdd:PRK10946   469 lmGEKS----CAFLVVKEPLK-AVQLRRFLREQGIAEF------------KLPDR-----VECVDSLPLTAVGKVDKKQL 526

                   ....*....
gi 1820002560 2443 REIGASFTA 2451
Cdd:PRK10946   527 RQWLASRAS 535
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
3471-3974 2.58e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 70.80  E-value: 2.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKAR-PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 3549
Cdd:PRK13383    44 TAARwPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3550 HEEIFEQTGAQVVVASAQYSARWTSSSCHVVTVSkalssqlPAVVDSTNTSVRPENAA---YIIFTSGSTGVPKGVVLEH 3626
Cdd:PRK13383   124 LAAALRAHHISTVVADNEFAERIAGADDAVAVID-------PATAGAEESGGRPAVAApgrIVLLTSGTTGKPKGVPRAP 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3627 RavatscLGHGRAFGITNLSRV-------LQFASYTFDAC-IAEIITTLLCGGCICVPSDSDRRNSLAKAiSTMDVNWAF 3698
Cdd:PRK13383   197 Q------LRSAVGVWVTILDRTrlrtgsrISVAMPMFHGLgLGMLMLTIALGGTVLTHRHFDAEAALAQA-SLHRADAFT 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3699 LTPSV-ARLLD-PGLI------PSLKILAIGGEQSSSADWNRWPGSVQKI--HVYGPTECCIFCTGYTTKQGFEPSTIGT 3768
Cdd:PRK13383   270 AVPVVlARILElPPRVrarnplPQLRVVMSSGDRLDPTLGQRFMDTYGDIlyNGYGSTEVGIGALATPADLRDAPETVGK 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3769 SVASVSWVVDPENHNRLAPLGSmGELLMEGPILARGYLNDVDKteaAFIDDPAwllegypghpgrqgrlyKTGDLVQYNA 3848
Cdd:PRK13383   350 PVAGCPVRILDRNNRPVGPRVT-GRIFVGGELAGTRYTDGGGK---AVVDGMT-----------------STGDMGYLDN 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3849 DGNLVYLGRKDSQVKVRGQRVELGEVEHHVrECLPEARQLAVeVILPSGQKDHaMLAAFVQLEEGTqnalldkeagGEDS 3928
Cdd:PRK13383   409 AGRLFIVGREDDMIISGGENVYPRAVENAL-AAHPAVADNAV-IGVPDERFGH-RLAAFVVLHPGS----------GVDA 475
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 3929 maqvvflASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:PRK13383   476 -------AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2474-2533 2.70e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 62.20  E-value: 2.70e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 2474 RTMQQLWAQVLGIELESIGLDDSFFRLGGDSITAMQISSS-ARALHLSVSTGDILKKKTIA 2533
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARlEEEFGVEIPPSDLFEHPTLA 61
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
4551-4920 2.94e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 70.49  E-value: 2.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPA-ICAWDGE-LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 4628
Cdd:PRK13391     7 AQTTPDKPAvIMASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4629 RHEHIFRQTGAQVVLASAQYATLWTSL--------GRSVVIVSEASTSQLPVVTKTADPSVNPGN----AAYAIFTSGST 4696
Cdd:PRK13391    87 EAAYIVDDSGARALITSAAKLDVARALlkqcpgvrHRLVLDGDGELEGFVGYAEAVAGLPATPIAdeslGTDMLYSSGTT 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4697 GIPKGVV--LEHKAVVT--SCLGHGQ-AFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLAkAINA 4771
Cdd:PRK13391   167 GRPKGIKrpLPEQPPDTplPLTAFLQrLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLA-LIEE 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4772 MDVNWALLTPSV-ARML-------DPCVVQSLKILVLGGE----QVNSADWDRWPKSIQtiNAYGPTECSICCTTYSGKQ 4839
Cdd:PRK13391   246 YGVTHTQLVPTMfSRMLklpeevrDKYDLSSLEVAIHAAApcppQVKEQMIDWWGPIIH--EYYAATEGLGFTACDSEEW 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4840 GFKSGTIGTSIVSVSWVVDPenHNRLAPLGSIGELLVEGPILARgYLNDMEKTEAAFIDDPAWLLEGYGGHSGRQGRLYK 4919
Cdd:PRK13391   324 LAHPGTVGRAMFGDLHILDD--DGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGTWSTVGDIGYVDEDGYLYL 400

                   .
gi 1820002560 4920 T 4920
Cdd:PRK13391   401 T 401
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
842-1368 3.28e-11

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 70.62  E-value: 3.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  842 WNADMPPAVD--------RCIHDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQ-LGVKREDVVPLCFEKS 912
Cdd:PRK12492     6 WNDKRPAGVPstidlaayKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  913 MWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGA-------------QVVL--TSSQHA-------MLFASSERHQ 970
Cdd:PRK12492    86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGAralvylnmfgklvQEVLpdTGIEYLieakmgdLLPAAKGWLV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  971 VTVSK-----VSTSQLPTVVNFAKS------------PVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTT------SCLGH 1027
Cdd:PRK12492   166 NTVVDkvkkmVPAYHLPQAVPFKQAlrqgrglslkpvPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAnmlqvrACLSQ 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1028 GEAFGYT--DHARVLQFAS------YTFDA-CIAEIIT----TLL-----YGGCIcvpSESDR-RNNLAKAISTMDVncA 1088
Cdd:PRK12492   246 LGPDGQPlmKEGQEVMIAPlplyhiYAFTAnCMCMMVSgnhnVLItnprdIPGFI---KELGKwRFSALLGLNTLFV--A 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1089 LLTPSVARLLEPSAvpsLKRLVLQGEQVSFADWNRWPG--SVQTINGYGPTECS--VCCNTYsGKQGfKSGIIGTSVASL 1164
Cdd:PRK12492   321 LMDHPGFKDLDFSA---LKLTNSGGTALVKATAERWEQltGCTIVEGYGLTETSpvASTNPY-GELA-RLGTVGIPVPGT 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1165 SWVV--DAGNHnrlAPLGSIGELLVEGPILARGYLNDIDKTEAAfIDDPAWLlegyeghagrrgrlyKTGDLVRCDADGN 1242
Cdd:PRK12492   396 ALKVidDDGNE---LPLGERGELCIKGPQVMKGYWQQPEATAEA-LDAEGWF---------------KTGDIAVIDPDGF 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1243 LVCLGRKDSQVKVRGQRVELGEIEhHVRECLPEARQLAVeVILPSGQKEHALLAAFIQLDKGnhNALFEEKASGEDSmaq 1322
Cdd:PRK12492   457 VRIVDRKKDLIIVSGFNVYPNEIE-DVVMAHPKVANCAA-IGVPDERSGEAVKLFVVARDPG--LSVEELKAYCKEN--- 529
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 1323 vvfLTGVeeelakRLPEHMVptilfTVKAMPITTSGKIDRKRLQDI 1368
Cdd:PRK12492   530 ---FTGY------KVPKHIV-----LRDSLPMTPVGKILRRELRDI 561
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
4006-4066 3.38e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 62.20  E-value: 3.38e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 4006 QTMQQLWAQVLSLGADIIGLDDSFFRLGGDSIAAMKLVGEARR-MGLHLSVADIFRHPKLAD 4066
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEeFGVEIPPSDLFEHPTLAE 62
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
4547-4716 3.44e-11

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 69.90  E-value: 3.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQaraRPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHP 4626
Cdd:PRK09029    12 WAQV---RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4627 ASRHEHIFRQTGAQVVLASAQYATlwtslgrsvviVSEASTSQLPVVTKTADPSVNPGNAAYAIFTSGSTGIPkgvvleh 4706
Cdd:PRK09029    89 QPLLEELLPSLTLDFALVLEGENT-----------FSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLP------- 150
                          170
                   ....*....|
gi 1820002560 4707 KAVVTSCLGH 4716
Cdd:PRK09029   151 KAAVHTAQAH 160
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
858-1360 3.61e-11

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 70.38  E-value: 3.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  858 FAEQA--RARPDASAVC--AWDG---ELTYGELDELSSKLAAHLVQLGVKRED----VVPLCFEksmwTVVAMLAVLKAG 926
Cdd:cd05943     72 YAENLlrHADADDPAAIyaAEDGertEVTWAELRRRVARLAAALRALGVKPGDrvagYLPNIPE----AVVAMLATASIG 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  927 GAFVPLDP--GHPA--SRheeiFKQIGAQVVLTSSQH-------------AMLFAS--SERHQVTVSKVSTSQLPTVVNF 987
Cdd:cd05943    148 AIWSSCSPdfGVPGvlDR----FGQIEPKVLFAVDAYtyngkrhdvrekvAELVKGlpSLLAVVVVPYTVAAGQPDLSKI 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  988 AKS------------------PVDPGNTAYIIFTSGTTGIPK-------GVVLQH-RAVTTSC-LGHGEA-FGYTD---- 1035
Cdd:cd05943    224 AKAltledflatgaagelefePLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHlKEHILHCdLRPGDRlFYYTTcgwm 303
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1036 --HARVLQFASYTfdaciaeiiTTLLYGGCICVPSEsDRRNNLAKA--ISTMDVNCALLTPSVARLLEPSAVPSLKRLVL 1111
Cdd:cd05943    304 mwNWLVSGLAVGA---------TIVLYDGSPFYPDT-NALWDLADEegITVFGTSAKYLDALEKAGLKPAETHDLSSLRT 373
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1112 QGEQVS------FaDW--NRWPGSVQTINGYGPTE---CSVCCN----TYSGK-QGfksGIIGTSVASLSwvvDAGNHNR 1175
Cdd:cd05943    374 ILSTGSplkpesF-DYvyDHIKPDVLLASISGGTDiisCFVGGNpllpVYRGEiQC---RGLGMAVEAFD---EEGKPVW 446
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1176 laplGSIGELLVEGPILAR--GYLNDID--KTEAAFIDDpawlLEGYEGHagrrgrlyktGDLVRCDADGNLVCLGRKDS 1251
Cdd:cd05943    447 ----GEKGELVCTKPFPSMpvGFWNDPDgsRYRAAYFAK----YPGVWAH----------GDWIEITPRGGVVILGRSDG 508
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1252 QVKVRGQRVELGEIeHHVRECLPEarqlaVEVILPSGQKehallaafiQLDKGNHNALFeekasgedsmaqVVFLTGVE- 1330
Cdd:cd05943    509 TLNPGGVRIGTAEI-YRVVEKIPE-----VEDSLVVGQE---------WKDGDERVILF------------VKLREGVEl 561
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 1820002560 1331 -EELAKRL---------PEHmVPTILFTVKAMPITTSGKI 1360
Cdd:cd05943    562 dDELRKRIrstirsalsPRH-VPAKIIAVPDIPRTLSGKK 600
PRK08315 PRK08315
AMP-binding domain protein; Validated
4536-5060 3.70e-11

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 70.22  E-value: 3.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4536 PPAIERCVHDQFAEQARARPDTPAICAWDGEL--TYGELDTLSSKLASHLVQLGVKPEDMV----PLCFEksmWTVVaML 4609
Cdd:PRK08315    11 VPLLEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVgiwaPNVPE---WVLT-QF 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4610 AVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLASAQYAT-------------LWTSLG-----------RSVVIVSEA 4665
Cdd:PRK08315    87 ATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFKDsdyvamlyelapeLATCEPgqlqsarlpelRRVIFLGDE 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4666 STSQLPVVTKTADPSVNPGNAAYAI--------------FTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVlqf 4731
Cdd:PRK08315   167 KHPGMLNFDELLALGRAVDDAELAArqatldpddpiniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRL--- 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4732 asytfdaCI--------AEIITTLLCC---GCICVPSDS-DRRNNLAkAINA-----------MDVnwALLT-PSVArML 4787
Cdd:PRK08315   244 -------CIpvplyhcfGMVLGNLACVthgATMVYPGEGfDPLATLA-AVEEerctalygvptMFI--AELDhPDFA-RF 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4788 D------------PCVVQSLKILVlggEQVNSADwdrwpksIqTInAYGPTECS--ICCTTYSGKQGFKSGTIGTSI--V 4851
Cdd:PRK08315   313 DlsslrtgimagsPCPIEVMKRVI---DKMHMSE-------V-TI-AYGMTETSpvSTQTRTDDPLEKRVTTVGRALphL 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4852 SVSwVVDPENhNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAfIDDPAWLlegyggHsgrqgrlykTGDLVRYDADGN 4931
Cdd:PRK08315   381 EVK-IVDPET-GETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDADGWM------H---------TGDLAVMDEEGY 442
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4932 LVYLGR-KDsqVKLRGqrvelG------EVEhhvrECL-TEAKQLAVEVI-VPE---GEggyaMLAAFVQLgddtyntlv 4999
Cdd:PRK08315   443 VNIVGRiKD--MIIRG-----GeniyprEIE----EFLyTHPKIQDVQVVgVPDekyGE----EVCAWIIL--------- 498
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 5000 KEkagGDSLTVQVV--FLDrveEELAK-RVPEHmmlttFFTLEAMPTTTSGKIDRKRLREIGAS 5060
Cdd:PRK08315   499 RP---GATLTEEDVrdFCR---GKIAHyKIPRY-----IRFVDEFPMTVTGKIQKFKMREMMIE 551
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
51-284 3.92e-11

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 68.84  E-value: 3.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   51 GYGPTECCIVCTgytseQDFTTGTIGTSIASV--------SWVVDPKDhGRLAPLGSVGELLVEGPILARGYLSDPEKTA 122
Cdd:cd05917    150 AYGMTETSPVST-----QTRTDDSIEKRVNTVgrimphteAKIVDPEG-GIVPPVGVPGELCIRGYSVMKGYWNDPEKTA 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  123 AVfINNPAWlleghggyagrqgrlYKTGDLVRYDADGNLVCLGR-KDSQVKlRGQRVELGEVEhhvrECLpeAKQLAVEV 201
Cdd:cd05917    224 EA-IDGDGW---------------LHTGDLAVMDEDGYCRIVGRiKDMIIR-GGENIYPREIE----EFL--HTHPKVSD 280
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  202 VLPLGQKNH---ATLAAFIQLDKGthnallkEKVGGDDSIArvvFLAGveeelakRLPKHMVPTVFFALLHFPTTTSGKT 278
Cdd:cd05917    281 VQVVGVPDErygEEVCAWIRLKEG-------AELTEEDIKA---YCKG-------KIAHYKVPRYVFFVDEFPLTVSGKI 343

                   ....*.
gi 1820002560  279 DRKRLR 284
Cdd:cd05917    344 QKFKLR 349
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
7597-7990 3.97e-11

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 70.29  E-value: 3.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7597 WNADVPPAIERCVHDLFAEQARARPGAPAIC---AWDG--ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTV 7671
Cdd:PRK08180    29 RSAEPLGDYPRRLTDRLVHWAQEAPDRVFLAergADGGwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHA 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7672 VAMLAVLKAGGAFVPLDP-------DHPASRHeeIFEQ-TGAQVVVASAQYSARWTSSSC----HVVTVSKA-------- 7731
Cdd:PRK08180   109 LLALAAMYAGVPYAPVSPayslvsqDFGKLRH--VLELlTPGLVFADDGAAFARALAAVVpadvEVVAVRGAvpgraatp 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7732 ----LSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAF--------------------- 7786
Cdd:PRK08180   187 faalLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFpflaeeppvlvdwlpwnhtfg 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7787 GITNLSRVLQF-ASYTFD------ACIAEiitTLlcggcicvpsdsdrRNslAKAIS-TMDVN----WAFLTPSVARllD 7854
Cdd:PRK08180   267 GNHNLGIVLYNgGTLYIDdgkptpGGFDE---TL--------------RN--LREISpTVYFNvpkgWEMLVPALER--D 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7855 PGLIPS----LKILAIGGEQSSSADWNRwpgsVQKIHV------------YGPTE---CCIFCTGYTTKQGFepstIGTS 7915
Cdd:PRK08180   326 AALRRRffsrLKLLFYAGAALSQDVWDR----LDRVAEatcgerirmmtgLGMTEtapSATFTTGPLSRAGN----IGLP 397
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 7916 VasvswvvdPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFiDDpawllEGYpghpgrqgrlYKTGDLV 7990
Cdd:PRK08180   398 A--------PGCEVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAF-DE-----EGY----------YRSGDAV 448
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
3464-3875 4.00e-11

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 70.22  E-value: 4.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3464 HDLFTEQAKARPHAPAI--CAWDGE---LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAF 3538
Cdd:cd05970     20 YDVVDAMAKEYPDKLALvwCDDAGEeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3539 VPldPDHPASRHEEIF--EQTGAQVVVASA----QYSARWTSSSCHVVTVSKALSSQLP-------AVVDSTNTSVRP-- 3603
Cdd:cd05970    100 IP--ATHQLTAKDIVYriESADIKMIVAIAedniPEEIEKAAPECPSKPKLVWVGDPVPegwidfrKLIKNASPDFERpt 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3604 -------ENAAYIIFTSGSTGVPKGVvlEHraVATSCLGH-GRAFGITNL---SRVLQFASYTFDACI-AEIITTLLCGG 3671
Cdd:cd05970    178 ansypcgEDILLVYFSSGTTGMPKMV--EH--DFTYPLGHiVTAKYWQNVregGLHLTVADTGWGKAVwGKIYGQWIAGA 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3672 CICVpSDSDR---RNSLAKaISTMDVNWAFLTPSVARLL--------DpglIPSLKILAIGGEQSSSADWNRWPG--SVQ 3738
Cdd:cd05970    254 AVFV-YDYDKfdpKALLEK-LSKYGVTTFCAPPTIYRFLiredlsryD---LSSLRYCTTAGEALNPEVFNTFKEktGIK 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3739 KIHVYGPTECCIfCTGytTKQGFEPSTIGTSVASVSWVVDPENHN-RLAPLGSMGEL---LMEG-PI-LARGYLNDVDKT 3812
Cdd:cd05970    329 LMEGFGQTETTL-TIA--TFPWMEPKPGSMGKPAPGYEIDLIDREgRSCEAGEEGEIvirTSKGkPVgLFGGYYKDAEKT 405
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 3813 EAAFIDdpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 3875
Cdd:cd05970    406 AEVWHD-------GY----------YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVE 451
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
8261-8515 4.01e-11

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 69.65  E-value: 4.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8261 VVPASYIQQFYIATGVRAPREA--FNYPFIDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQ-GKLYQVIPRHQDLPFS 8337
Cdd:cd19547      1 VYPLAPMQEGMLFRGLFWPDSDayFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8338 IFEVNGALAEESQAIHIRDL--DQTSPLGLPT----SFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQ---- 8407
Cdd:cd19547     81 LLDWSGEDPDRRAELLERLLadDRAAGLSLADcplyRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEelah 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8408 -QEPLLSTT-GFHSYLAYVHN---QRSASINYWSRLLKGSHITNITSKLRPKLGK-DTTIRSV--KVERVIRTPQLPTGL 8479
Cdd:cd19547    161 gREPQLSPCrPYRDYVRWIRArtaQSEESERFWREYLRDLTPSPFSTAPADREGEfDTVVHEFpeQLTRLVNEAARGYGV 240
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1820002560 8480 TMASLVSSAWAVVLSHISGEEDVVYGLVVAGRNSDL 8515
Cdd:cd19547    241 TTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPEL 276
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
4690-5056 4.27e-11

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 68.51  E-value: 4.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4690 IFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPsdsDRRNNLAKAI 4769
Cdd:cd17630      6 ILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLL---ERNQALAEDL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4770 NAMDVNWALLTPS-VARMLD----PCVVQSLKILVLGGEQVNSADWDRWPK-SIQTINAYGPTECS--ICCTTYSGkqgF 4841
Cdd:cd17630     83 APPGVTHVSLVPTqLQRLLDsgqgPAALKSLRAVLLGGAPIPPELLERAADrGIPLYTTYGMTETAsqVATKRPDG---F 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4842 KSGTIGtsivsvswVVDPENHNRLAPlgsIGELLVEGPILARGYLNDMEKTEAafiDDPAWllegygghsgrqgrlYKTG 4921
Cdd:cd17630    160 GRGGVG--------VLLPGRELRIVE---DGEIWVGGASLAMGYLRGQLVPEF---NEDGW---------------FTTK 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4922 DLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE------HHVREclteakqlAVEVIVPEGEGGYAMLAAFVqlgddty 4995
Cdd:cd17630    211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEaalaahPAVRD--------AFVVGVPDEELGQRPVAVIV------- 275
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 4996 ntlvkekaGGDSLTVQVvFLDRVEEELAK-RVPEHmmlttFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:cd17630    276 --------GRGPADPAE-LRAWLKDKLARfKLPKR-----IYPVPELPRTGGGKVDRRALRA 323
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
3451-3844 4.33e-11

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 70.29  E-value: 4.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3451 WNADVPPAIERCVHDLFTEQAKARPHAPAIC---AWDG--ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTV 3525
Cdd:PRK08180    29 RSAEPLGDYPRRLTDRLVHWAQEAPDRVFLAergADGGwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHA 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3526 VAMLAVLKAGGAFVPLDP-------DHPASRHeeIFEQ-TGAQVVVASAQYSARWTSSSC----HVVTVSKA-------- 3585
Cdd:PRK08180   109 LLALAAMYAGVPYAPVSPayslvsqDFGKLRH--VLELlTPGLVFADDGAAFARALAAVVpadvEVVAVRGAvpgraatp 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3586 ----LSSQLPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAF--------------------- 3640
Cdd:PRK08180   187 faalLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFpflaeeppvlvdwlpwnhtfg 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3641 GITNLSRVLQF-ASYTFD------ACIAEiitTLlcggcicvpsdsdrRNslAKAIS-TMDVN----WAFLTPSVARllD 3708
Cdd:PRK08180   267 GNHNLGIVLYNgGTLYIDdgkptpGGFDE---TL--------------RN--LREISpTVYFNvpkgWEMLVPALER--D 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3709 PGLIPS----LKILAIGGEQSSSADWNRwpgsVQKIHV------------YGPTE---CCIFCTGYTTKQGFepstIGTS 3769
Cdd:PRK08180   326 AALRRRffsrLKLLFYAGAALSQDVWDR----LDRVAEatcgerirmmtgLGMTEtapSATFTTGPLSRAGN----IGLP 397
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 3770 VasvswvvdPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFiDDpawllEGYpghpgrqgrlYKTGDLV 3844
Cdd:PRK08180   398 A--------PGCEVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAF-DE-----EGY----------YRSGDAV 448
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
1929-2445 4.73e-11

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 70.08  E-value: 4.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1929 RCVHDLFTEQAKARPHAPAICAWDGE------LTYGELDALSSKLASHLVQLGVNPEDVVPlCFEKSMWTVVAM-LAVLK 2001
Cdd:PRK13295    24 RTINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVS-CQLPNWWEFTVLyLACSR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2002 AGGAFVPLDPdhpasrhedIFRQ---------TGAQVVVTsaqhSARWIGTNH---------------QVVTVSAGSLEQ 2057
Cdd:PRK13295   103 IGAVLNPLMP---------IFRErelsfmlkhAESKVLVV----PKTFRGFDHaamarrlrpelpalrHVVVVGGDGADS 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2058 FSTLV------NPVDLPA-------KPENAAYVMFTSGSTGTPKGVVLEHRAVVTsclghgqafGVTNLLRALQFTAYtf 2124
Cdd:PRK13295   170 FEALLitpaweQEPDAPAilarlrpGPDDVTQLIYTSGTTGEPKGVMHTANTLMA---------NIVPYAERLGLGAD-- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2125 DVC-IAEII---TTLVHG-------GCICVPSDSERRDNLAKAITDMQVNWGY--------LTSSVArlLDPCLVPSLKV 2185
Cdd:PRK13295   239 DVIlMASPMahqTGFMYGlmmpvmlGATAVLQDIWDPARAAELIRTEGVTFTMastpfltdLTRAVK--ESGRPVSSLRT 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2186 LVLGGEQVNstdwgkwPSSVQT---------INGYGPTECCVFCTGYTGIQGFQSGNigTSIASVSW----VVDPEnhGR 2252
Cdd:PRK13295   317 FLCAGAPIP-------GALVERaraalgakiVSAWGMTENGAVTLTKLDDPDERAST--TDGCPLPGvevrVVDAD--GA 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2253 LAPLGSIGELLVEGPILARGYLNDVDKTQaafIDDPAWllegypghegrqgrlYKTGDLVRYSSDGNLVCLGR-KDsqVK 2331
Cdd:PRK13295   386 PLPAGQIGRLQVRGCSNFGGYLKRPQLNG---TDADGW---------------FDTGDLARIDADGYIRISGRsKD--VI 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2332 VRG-QRVELGEVEHHMRKcLPEANQLAVEVVPPS--GERDHAMlaafirlddetrnspLIIKYAEDNSTAQIV-FLTgie 2407
Cdd:PRK13295   446 IRGgENIPVVEIEALLYR-HPAIAQVAIVAYPDErlGERACAF---------------VVPRPGQSLDFEEMVeFLK--- 506
                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1820002560 2408 eelSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREI 2445
Cdd:PRK13295   507 ---AQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREM 541
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
7630-8005 6.08e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 69.76  E-value: 6.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7630 DG---ELTYGELDVLSSNLAGHLVQLGvNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL-DPDHPAsrHEEIFeqtga 7705
Cdd:PRK07769    50 DGvarDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPG--HVGRL----- 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7706 QVVVASAQYSARWTSSSChVVTVSKALSSqLPA-------VVDSTNTSV-----RPE----NAAYIIFTSGSTGVPKGVV 7769
Cdd:PRK07769   122 HAVLDDCTPSAILTTTDS-AEGVRKFFRA-RPAkerprviAVDAVPDEVgatwvPPEanedTIAYLQYTSGSTRIPAGVQ 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7770 LEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICV--PSDSDRR-----NSLAK----AISTM 7838
Cdd:PRK07769   200 ITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFmsPAAFVRRpgrwiRELARkpggTGGTF 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7839 DV--NWAFlTPSVARLLDPGLIPSL-----KILAIGGEQSSSADWNRW-----PGSVQKIHV---YGPTECCIFCTgyTT 7903
Cdd:PRK07769   280 SAapNFAF-EHAAARGLPKDGEPPLdlsnvKGLLNGSEPVSPASMRKFneafaPYGLPPTAIkpsYGMAEATLFVS--TT 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7904 KQGFEPSTI-------------------GTSVASVS--------W--VVDPENHNRLaPLGSMGELLMEGPILARGYLND 7954
Cdd:PRK07769   357 PMDEEPTVIyvdrdelnagrfvevpadaPNAVAQVSagkvgvseWavIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGK 435
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 7955 VDKTEAAF----------------IDDPAWLlegypghpgrqgrlyKTGDLVQYnADGNLVYLGR-KD 8005
Cdd:PRK07769   436 PEETAATFqnilksrlseshaegaPDDALWV---------------RTGDYGVY-FDGELYITGRvKD 487
PRK09088 PRK09088
acyl-CoA synthetase; Validated
10-289 6.34e-11

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 69.45  E-value: 6.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   10 PSVARLL------EPSHIPSLRILVMGGEQVNSADWDRW-PSSVQTINGYGPTECCIVcTGYTSEQDFT---TGTIGTSI 79
Cdd:PRK09088   234 PQMAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWlDDGIPMVDGFGMSEAGTV-FGMSVDCDVIrakAGAAGIPT 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   80 ASV-SWVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFiNNPAWlleghggyagrqgrlYKTGDLVRYDAD 158
Cdd:PRK09088   313 PTVqTRVVD--DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF-TGDGW---------------FRTGDIARRDAD 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  159 GNLVCLGRKDSQVKLRGQRVELGEVE-----H-HVREClpeakqlAVeVVLPLGQKNHATLAAFIQLDkgthnallkekv 232
Cdd:PRK09088   375 GFFWVVDRKKDMFISGGENVYPAEIEavladHpGIREC-------AV-VGMADAQWGEVGYLAIVPAD------------ 434
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  233 ggddsiARVVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGAS 289
Cdd:PRK09088   435 ------GAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
6856-6980 7.38e-11

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 68.78  E-value: 7.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6856 GELLVEGPILARGYLNDADKTAAAFVNDPaWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGR-KDGQVKVRGQRVE 6934
Cdd:cd05907    279 GEILVRGPNVMLGYYKNPEATAEALDADG-WL---------------HTGDLGEIDEDGFLHITGRkKDLIITSGGKNIS 342
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 6935 LGEIENRLRECmpratqmavEVISPAGAAEQAKTMVVAFLQLNDEA 6980
Cdd:cd05907    343 PEPIENALKAS---------PLISQAVVIGDGRPFLVALIVPDPEA 379
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
23-285 7.64e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 69.41  E-value: 7.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRWP--SSVQTINGYGPTECCIVCTGyTSEQDFTTGTIGTSIASVSW-VVDpkDHGRLAPLGS 99
Cdd:PRK05677   327 ALKLTLSGGMALQLATAERWKevTGCAICEGYGMTETSPVVSV-NPSQAIQVGTIGIPVPSTLCkVID--DDGNELPLGE 403
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  100 VGELLVEGPILARGYLSDPEKTAAVFiNNPAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVE 179
Cdd:PRK05677   404 VGELCVKGPQVMKGYWQRPEATDEIL-DSDGWL---------------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVY 467
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  180 LGEVEhHVRECLPEAKQLAVeVVLPlGQKNHATLAAFIQLDKGThnALLKEKvggddsiarvvflagVEEELAKRLPKHM 259
Cdd:PRK05677   468 PNELE-DVLAALPGVLQCAA-IGVP-DEKSGEAIKVFVVVKPGE--TLTKEQ---------------VMEHMRANLTGYK 527
                          250       260
                   ....*....|....*....|....*.
gi 1820002560  260 VPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:PRK05677   528 VPKAVEFRDELPTTNVGKILRRELRD 553
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7748-8116 8.11e-11

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 68.18  E-value: 8.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7748 RPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGhGRAFG--------ITNLSRVLQFASYTFDAC-------IAEIITT 7812
Cdd:cd05924      1 RSADDLYILYTGGTTGMPKGVMWRQEDIFRMLMG-GADFGtgeftpseDAHKAAAAAAGTVMFPAPplmhgtgSWTAFGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7813 LLCGGCICVPSDS-DRRNSLA-----KAISTMDVNWAFLTPSVARLLDPGL--IPSLKILAIGGEQSSSADWNRWPGSVQ 7884
Cdd:cd05924     80 LLGGQTVVLPDDRfDPEEVWRtiekhKVTSMTIVGDAMARPLIDALRDAGPydLSSLFAISSGGALLSPEVKQGLLELVP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7885 KIHV---YGPTECCIFCTGYTTKQGFEPSTIgTSVASVSWVVDPENHNRLAPLGSMGELLMEGPIlARGYLNDVDKTEAA 7961
Cdd:cd05924    160 NITLvdaFGSSETGFTGSGHSAGSGPETGPF-TRANPDTVVLDDDGRVVPPGSGGVGWIARRGHI-PLGYYGDEAKTAET 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7962 F--IDDPAWLLegypghpgrqgrlykTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQlAVEVI 8039
Cdd:cd05924    238 FpeVDGVRYAV---------------PGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKS-HPAVYD-VLVVG 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8040 LPS---GQKnhamLAVFVQLgkgthiahleeKAGGEDSMAQVVflTGTEEELAK-RLPKHM--VPTVffallhfPMTTSG 8113
Cdd:cd05924    301 RPDerwGQE----VVAVVQL-----------REGAGVDLEELR--EHCRTRIARyKLPKQVvfVDEI-------ERSPAG 356

                   ...
gi 1820002560 8114 KAD 8116
Cdd:cd05924    357 KAD 359
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
6842-7043 8.28e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 69.06  E-value: 8.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPLG-SIGELLVEGPILARGYLNDADKTAAAFVNDpaWLveghgkhpgrrgrlyKTGDLVYYNKDGNLvYI- 6919
Cdd:PRK06187   353 VDDDGDELPPDGgEVGEIIVRGPWLMQGYWNRPEATAETIDGG--WL---------------HTGDVGYIDEDGYL-YIt 414
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6920 GRKDGQVKVRGQRVELGEIENRLRECmPratqmAVE---VIspaGAA-EQAKTMVVAFLQLNDEARdallggnvpnddnl 6995
Cdd:PRK06187   415 DRIKDVIISGGENIYPRELEDALYGH-P-----AVAevaVI---GVPdEKWGERPVAVVVLKPGAT-------------- 471
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 6996 saqvVFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:PRK06187   472 ----LDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
450-717 8.67e-11

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 68.44  E-value: 8.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  450 VLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQVVVE-----EKMQWTES----ESLEEYLNEDKAASMGLG 520
Cdd:cd20483     29 VCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDpsfhlIVIDLSEAadpeAALDQLVRNLRRQELDIE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  521 D-RLARYALIKESCGGKRwFVWTIHHALYDGWSLPLVLDAVKQVYSGAALER------QPSFnTFIQY-------VSQQD 586
Cdd:cd20483    109 EgEVIRGWLVKLPDEEFA-LVLASHHIAWDRGSSKSIFEQFTALYDALRAGRdlatvpPPPV-QYIDFtlwhnalLQSPL 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  587 VKAAAAYWQTALADC-EAVLFPPLPSTVTQPVAD---TTVKYQCPPS-----PEVTSSNITTS-TLIRAAWAIIASRYTS 656
Cdd:cd20483    187 VQPLLDFWKEKLEGIpDASKLLPFAKAERPPVKDyerSTVEATLDKEllarmKRICAQHAVTPfMFLLAAFRAFLYRYTE 266
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  657 SEDIVFGttVTGRNAPITGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEmiAYE 717
Cdd:cd20483    267 DEDLTIG--MVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLE--AYE 323
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
309-377 9.03e-11

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 61.88  E-value: 9.03e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560   309 PSTEAERTMQQL----WARVLGIE-PDSIGLDDSFFRLGGDSIAAIKLVGE-ARRTGLQPSVADIFRHPTLAALA 377
Cdd:smart00823    5 PPAERRRLLLDLvreqVAAVLGHAaAEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALA 79
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
7203-7473 9.08e-11

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 68.54  E-value: 9.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7203 YIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSElGLLQVVVEE-----------KIQWTESEA-LEEYLKED 7270
Cdd:cd19531     24 YNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDG-EPVQVILPPlplplpvvdlsGLPEAEREAeAQRLAREE 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7271 KAVSMGLG-DPLAHYALVKEAwGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAF-IQY--------- 7339
Cdd:cd19531    103 ARRPFDLArGPLLRATLLRLG-EDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPPLpIQYadyavwqre 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7340 -LGQQDLEATAAYWQTALSDCEAVLfpPLPSTVTQPVADT----TVEYQCPP--------LSKATlDTTTSTLIRAAWAI 7406
Cdd:cd19531    182 wLQGEVLERQLAYWREQLAGAPPVL--ELPTDRPRPAVQSfrgaRVRFTLPAeltaalraLARRE-GATLFMTLLAAFQV 258
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 7407 VTSCYTSSDDVVYGTTVTGRNAPiaGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQSTDMIAH 7473
Cdd:cd19531    259 LLHRYSGQDDIVVGTPVAGRNRA--ELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAYAH 323
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1538-1893 9.10e-11

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 68.50  E-value: 9.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1538 DVDEDVFRAAWEHIVRSTAVLRTRIVQHSELGLLQV-------VIEENIQWTEPKSLEEYLSEDKAVSVGL-GDPLARYA 1609
Cdd:cd20484     35 KLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIepskplsFQEEDISSLKESEIIAYLREKAKEPFVLeNGPLMRVH 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1610 FVKeaCGGKRWFVW-TIHHAVYDGWS-LPLI---LHAVKQVYSGGVLQWQPS---FNAFIQ----YLGQQDLEATVAYWQ 1677
Cdd:cd20484    115 LFS--RSEQEHFVLiTIHHIIFDGSSsLTLIhslLDAYQALLQGKQPTLASSpasYYDFVAweqdMLAGAEGEEHRAYWK 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1678 TALADCEAVL--FPTLPPTVTQPVADATVEYQCPP-LSK------ATSDTTTSTLIRAAWAIVTSRYTTSDDVVFGTTVT 1748
Cdd:cd20484    193 QQLSGTLPILelPADRPRSSAPSFEGQTYTRRLPSeLSNqiksfaRSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTM 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1749 GRntPVTGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAHEQ---TGLQRIAKMGQGPQHACSFQTLL--- 1822
Cdd:cd20484    273 GR--PEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAypfPAMVRDLNIPRSQANSPVFQVAFfyq 350
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 1823 -VVQPVDdvLDNTLGEWRD--HSEL-----QEfTTYTLMLQCMLAAEGVQITASFDTRVIEKWVVEKMLRQFSFIMQQL 1893
Cdd:cd20484    351 nFLQSTS--LQQFLAEYQDvlSIEFvegihQE-GEYELVLEVYEQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEEL 426
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
1939-2308 9.18e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 68.95  E-value: 9.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPA-ICAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 2016
Cdd:PRK13391     7 AQTTPDKPAvIMASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2017 RHEDIFRQTGAQVVVTSAQH-------SARWIGTNHQVVTVSAGSLEQFSTLVNPV-DLPAKP---ENAAYVMF-TSGST 2084
Cdd:PRK13391    87 EAAYIVDDSGARALITSAAKldvaralLKQCPGVRHRLVLDGDGELEGFVGYAEAVaGLPATPiadESLGTDMLySSGTT 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2085 GTPKGVV--LEHRAVVtsclghgQAFGVTNLL-RALQFTAYTFDVCIAEI---------ITTLVHGGCICVPS--DSERR 2150
Cdd:PRK13391   167 GRPKGIKrpLPEQPPD-------TPLPLTAFLqRLWGFRSDMVYLSPAPLyhsapqravMLVIRLGGTVIVMEhfDAEQY 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2151 DNLAK--AITDMQvnwgyltssvarlldpcLVPSL--KVLVLGGEQVNSTDW--------GKWPSSVQT----INGYGP- 2213
Cdd:PRK13391   240 LALIEeyGVTHTQ-----------------LVPTMfsRMLKLPEEVRDKYDLsslevaihAAAPCPPQVkeqmIDWWGPi 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2214 -------TEccvfCTGYTGIQGFQ----SGNIGTSIASVSWVVDPenHGRLAPLGSIGELLVEGPILARgYLNDVDKTQA 2282
Cdd:PRK13391   303 iheyyaaTE----GLGFTACDSEEwlahPGTVGRAMFGDLHILDD--DGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAE 375
                          410       420
                   ....*....|....*....|....*.
gi 1820002560 2283 AFIDDPAWLLEGYPGHEGRQGRLYKT 2308
Cdd:PRK13391   376 ARHPDGTWSTVGDIGYVDEDGYLYLT 401
PRK12316 PRK12316
peptide synthase; Provisional
8253-8562 9.18e-11

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 69.99  E-value: 9.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8253 LRIDDITDVVPASYIQQ--FYIATGVRAPREAFNYPFIDLsDAVDIQVLQASCSALLEHFPILRTHFVYfQGKL---YQV 8327
Cdd:PRK12316  4094 LPLGEIEDIYPLSPMQQgmLFHSLYEQEAGDYINQMRVDV-QGLDVERFRAAWQAALDRHDVLRSGFVW-QGELgrpLQV 4171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8328 IPRHQDLPFSIFEVNG------ALAEESQAIHIRDLD-QTSPLglpTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWA 8400
Cdd:PRK12316  4172 VHKQVSLPFAELDWRGradlqaALDALAAAERERGFDlQRAPL---LRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLG 4248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8401 SLASIYQQEPLLSTTG-FHSYLAYVHNQ-RSASINYW-SRLLKGSHITNIT-----SKLRPKLGKDTTIRSVKVERVIRT 8472
Cdd:PRK12316  4249 EVLERYSGRPPAQPGGrYRDYIAWLQRQdAAASEAFWrEQLAALDEPTRLAqaiarADLRSANGYGEHVRELDATATARL 4328
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8473 PQLP--TGLTMASLVSSAWAVVLSHISGEEDVVYGLVVAGRNSDLPSITEV-------------------------SVQD 8525
Cdd:PRK12316  4329 REFArtQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQiglfintlpviatpraqqsvvewlqQVQR 4408
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1820002560 8526 QYISLGESDSIGLDDIvQHCTDWPAKSEFDSIIQHQN 8562
Cdd:PRK12316  4409 QNLALREHEHTPLYEI-QRWAGQGGEALFDSLLVFEN 4444
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
46-285 1.01e-10

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 68.88  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   46 VQTINGYGPTEccivctgyTSEQDFTT---------GTIGtsIASVSWVVDPKDHGRLAPLGSVGELLVEGPILARGYLS 116
Cdd:cd05926    291 APVLEAYGMTE--------AAHQMTSNplppgprkpGSVG--KPVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLN 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  117 DPEKTAAVFINNPaWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQ 196
Cdd:cd05926    361 NPEANAEAAFKDG-WF---------------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH-PAVLE 423
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  197 lAVEVVLP---LGQKnhatLAAFIQLDKGTHnaLLKEKvggddsiarvvflagVEEELAKRLPKHMVPTVFFALLHFPTT 273
Cdd:cd05926    424 -AVAFGVPdekYGEE----VAAAVVLREGAS--VTEEE---------------LRAFCRKHLAAFKVPKKVYFVDELPKT 481
                          250
                   ....*....|..
gi 1820002560  274 TSGKTDRKRLRE 285
Cdd:cd05926    482 ATGKIQRRKVAE 493
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
5617-6007 1.02e-10

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 69.14  E-value: 1.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5617 PPAIERCVHDLFTEQAKARPHAPAIC---AWDG--ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLA 5691
Cdd:PRK08180    34 LGDYPRRLTDRLVHWAQEAPDRVFLAergADGGwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALA 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5692 VLKAGGAFVPLDPDHP-ASRHEDTFRH-----TGAQVVVTSAQHSARWI---GTNH-QVVTVSAGSLGQ----LSTLVNP 5757
Cdd:PRK08180   114 AMYAGVPYAPVSPAYSlVSQDFGKLRHvlellTPGLVFADDGAAFARALaavVPADvEVVAVRGAVPGRaatpFAALLAT 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5758 VGLPAI--------PENAVYIMFTSGSTGIPKGVVLEHR------AVVTSCWGRGRA--------------FG-ITNLSR 5808
Cdd:PRK08180   194 PPTAAVdaahaavgPDTIAKFLFTSGSTGLPKAVINTHRmlcanqQMLAQTFPFLAEeppvlvdwlpwnhtFGgNHNLGI 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5809 VLQF-ASYTFD------ACMD-------EIITTLMYGgcicVPS-----------DSDRRNDLVKAISTMDVSCALLTPS 5863
Cdd:PRK08180   274 VLYNgGTLYIDdgkptpGGFDetlrnlrEISPTVYFN----VPKgwemlvpalerDAALRRRFFSRLKLLFYAGAALSQD 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5864 VARLLEPSSVPTLqmlvlqGEQVSFAdwnrwpasvqtiNGYGPTECSICCnTYSGKQGFKSGIIGTSVasvswvvdPENH 5943
Cdd:PRK08180   350 VWDRLDRVAEATC------GERIRMM------------TGLGMTETAPSA-TFTTGPLSRAGNIGLPA--------PGCE 402
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 5944 DRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFiDDpawllEGYpghpgrqgrlYKTGDLVRY 6007
Cdd:PRK08180   403 VKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAF-DE-----EGY----------YRSGDAVRF 450
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
7599-8027 1.03e-10

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 68.89  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7599 ADVPPAIERCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVL 7678
Cdd:PRK07059    15 AEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7679 KAGGAFVPLDPDHPASRHEEIFEQTGAQVVV-----ASAQYSARWTSSSCHVVTVS-------------------KAL-- 7732
Cdd:PRK07059    95 RAGYVVVNVNPLYTPRELEHQLKDSGAEAIVvlenfATTVQQVLAKTAVKHVVVASmgdllgfkghivnfvvrrvKKMvp 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7733 SSQLPAVVdSTNTSVR-------------PENAAYIIFTSGSTGVPKGVVLEHR----AVATSCLGHGRAF----GITNL 7791
Cdd:PRK07059   175 AWSLPGHV-RFNDALAegarqtfkpvklgPDDVAFLQYTGGTTGVSKGATLLHRnivaNVLQMEAWLQPAFekkpRPDQL 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7792 SRVLQFASYTFDACIAEIITTLLCGGC-ICVPSDSDRRnSLAKAISTMDVNwafLTPSV-----ARLLDPGL----IPSL 7861
Cdd:PRK07059   254 NFVCALPLYHIFALTVCGLLGMRTGGRnILIPNPRDIP-GFIKELKKYQVH---IFPAVntlynALLNNPDFdkldFSKL 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7862 KILAIGGEQSSSADWNRWpgsVQKIHV-----YGPTEC--CIFCTGYTTKQgFEpSTIGTSVASVSWVVDPENHNRLaPL 7934
Cdd:PRK07059   330 IVANGGGMAVQRPVAERW---LEMTGCpitegYGLSETspVATCNPVDATE-FS-GTIGLPLPSTEVSIRDDDGNDL-PL 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7935 GSMGELLMEGPILARGYLNDVDKTEAAFIDDpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQR 8014
Cdd:PRK07059   404 GEPGEICIRGPQVMAGYWNRPDETAKVMTAD------GF----------FRTGDVGVMDERGYTKIVDRKKDMILVSGFN 467
                          490
                   ....*....|...
gi 1820002560 8015 VELGEVEHHVREC 8027
Cdd:PRK07059   468 VYPNEIEEVVASH 480
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
4-285 1.05e-10

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 68.75  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    4 NWALLTPSVARLlepsHIPSLRILVMGGEQVNSADWDRWP--SSVQTINGYGPTECC-IVCTGYTSEQDFTtGTIGTSIA 80
Cdd:PRK08751   315 NGLLNTPGFDQI----DFSSLKMTLGGGMAVQRSVAERWKqvTGLTLVEAYGLTETSpAACINPLTLKEYN-GSIGLPIP 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   81 SVSWVVDpKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVfINNPAWLleghggyagrqgrlyKTGDLVRYDADGN 160
Cdd:PRK08751   390 STDACIK-DDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKV-MDADGWL---------------HTGDIARMDEQGF 452
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  161 LVCLGRKDSQVKLRGQRVELGEVEhHVRECLPEAKQLAVeVVLPLGQKNHATLAAFIQLDKgthnALLKEKvggddsiar 240
Cdd:PRK08751   453 VYIVDRKKDMILVSGFNVYPNEIE-DVIAMMPGVLEVAA-VGVPDEKSGEIVKVVIVKKDP----ALTAED--------- 517
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560  241 vvflagVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:PRK08751   518 ------VKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
7633-8027 1.08e-10

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 68.78  E-value: 1.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVVplcfeksmwtvvamlavlkaggafvpldpdhpasrheEIFEQTgaqvvvasa 7712
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKV-------------------------------------AIFAET--------- 39
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7713 qySARW--TSSSCH-----VVTVSKALSSqlPAVVDSTN--------TSVRPENAAYIIFTSGSTGVPKGVVLEHRAVAT 7777
Cdd:cd17639     40 --RAEWliTALGCWsqnipIVTVYATLGE--DALIHSLNetecsaifTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVA 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7778 SCLGHGRAFG--ITNLSRVLqfaSYTFDACIAEIITTLLC---GGCIC-----------------------------VPS 7823
Cdd:cd17639    116 GIAGLGDRVPelLGPDDRYL---AYLPLAHIFELAAENVClyrGGTIGygsprtltdkskrgckgdltefkptlmvgVPA 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7824 --DSDRRNSLAKaISTM--------DVNWAFLTPSVARLLDPGLIPSL---KILAI-GGEQSS--------SADWNRWPG 7881
Cdd:cd17639    193 iwDTIRKGVLAK-LNPMgglkrtlfWTAYQSKLKALKEGPGTPLLDELvfkKVRAAlGGRLRYmlsggaplSADTQEFLN 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7882 SV--QKIHVYGPTECCifCTGYTTKQG-FEPSTIGTSVAS-----VSWvvdPE-NHNRLAPLgSMGELLMEGPILARGYL 7952
Cdd:cd17639    272 IVlcPVIQGYGLTETC--AGGTVQDPGdLETGRVGPPLPCceiklVDW---EEgGYSTDKPP-PRGEILIRGPNVFKGYY 345
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 7953 NDVDKTEAAFIDDpawllegypghpgrqgRLYKTGDLVQYNADGNLVYLGRKDSQVKVR-GQRVELGEVEHHVREC 8027
Cdd:cd17639    346 KNPEKTKEAFDGD----------------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSN 405
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
5612-6036 1.11e-10

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 68.70  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5612 WNQNVPPAIE--------RCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLAGHLTQ-LGVKPEDMVPLCFEKS 5682
Cdd:PRK12492     6 WNDKRPAGVPstidlaayKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5683 MWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVV---------------TSAQH-----------SARWIGT 5736
Cdd:PRK12492    86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVylnmfgklvqevlpdTGIEYlieakmgdllpAAKGWLV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5737 NHQVVTV----------------SAGSLGQ-LSTLVNPVGLPAIpenAVyIMFTSGSTGIPKGVVLEHRAVVT------S 5793
Cdd:PRK12492   166 NTVVDKVkkmvpayhlpqavpfkQALRQGRgLSLKPVPVGLDDI---AV-LQYTGGTTGLAKGAMLTHGNLVAnmlqvrA 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5794 CWGRGRAFG---ITNLSRVL-----QFASYTFDA-CMdeiitTLMYGG----CICVPSDSdrrNDLVKAISTMDVScALL 5860
Cdd:PRK12492   242 CLSQLGPDGqplMKEGQEVMiaplpLYHIYAFTAnCM-----CMMVSGnhnvLITNPRDI---PGFIKELGKWRFS-ALL 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5861 ---TPSVARLLEPS----SVPTLQMLVLQGEQVSFADWNRWPA--SVQTINGYGPTECS--ICCNTYsGKQGfKSGIIGT 5929
Cdd:PRK12492   313 glnTLFVALMDHPGfkdlDFSALKLTNSGGTALVKATAERWEQltGCTIVEGYGLTETSpvASTNPY-GELA-RLGTVGI 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5930 SVASVSWVVDPENHDRLaPLGSIGELLVEGPILARGYLNDIQKTAAVfIDDPAWLlegypghpgrqgrlyKTGDLVRYDA 6009
Cdd:PRK12492   391 PVPGTALKVIDDDGNEL-PLGERGELCIKGPQVMKGYWQQPEATAEA-LDAEGWF---------------KTGDIAVIDP 453
                          490       500
                   ....*....|....*....|....*..
gi 1820002560 6010 NGNLVCLGRKDSQVKLRGQRVELGEVE 6036
Cdd:PRK12492   454 DGFVRIVDRKKDLIIVSGFNVYPNEIE 480
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
7634-8021 1.31e-10

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 68.47  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7634 TYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQ 7713
Cdd:PLN02330    57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7714 YSARWTSSSCHVVTVSKALSSQ-------LPAVVDSTNTSVRPE----NAAYIIFTSGSTGVPKGVVLEHR-AVATSC-- 7779
Cdd:PLN02330   137 NYGKVKGLGLPVIVLGEEKIEGavnwkelLEAADRAGDTSDNEEilqtDLCALPFSSGTTGISKGVMLTHRnLVANLCss 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7780 ---LGHGRAFGITNLSRVLQFASYTFDA-CIAeiitTLLCGGCICVPSDSDRRNSLaKAISTMDVNWAFLTPSVARLL-- 7853
Cdd:PLN02330   217 lfsVGPEMIGQVVTLGLIPFFHIYGITGiCCA----TLRNKGKVVVMSRFELRTFL-NALITQEVSFAPIVPPIILNLvk 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7854 DPGL----IPSLKILAIGGEQSS------SADWNRWPGsVQKIHVYGPTE-CCIfctgyTTKQGfEPSTiGTSVA---SV 7919
Cdd:PLN02330   292 NPIVeefdLSKLKLQAIMTAAAPlapellTAFEAKFPG-VQVQEAYGLTEhSCI-----TLTHG-DPEK-GHGIAkknSV 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7920 SWV--------VDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTGDLVQ 7991
Cdd:PLN02330   364 GFIlpnlevkfIDPDTGRSL-PKNTPGELCVRSQCVMQGYYNNKEETDRT-IDEDGWL---------------HTGDIGY 426
                          410       420       430
                   ....*....|....*....|....*....|
gi 1820002560 7992 YNADGNLVYLGRKDSQVKVRGQRVELGEVE 8021
Cdd:PLN02330   427 IDDDGDIFIVDRIKELIKYKGFQVAPAELE 456
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
6842-7043 1.35e-10

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 68.09  E-value: 1.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDpAWlveghgkhpgrrgrlYKTGDLVYYNKDGNLVYIGR 6921
Cdd:cd05941    278 VDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDD-GW---------------FKTGDLGVVDEDGYYWILGR 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 -KDGQVKVRGQRVELGEIENRLREcMPRATQMAVevispAGAAE----QAktmVVAFLQLNDEardallggnvpnddnls 6996
Cdd:cd05941    342 sSVDIIKSGGYKVSALEIERVLLA-HPGVSECAV-----IGVPDpdwgER---VVAVVVLRAG----------------- 395
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 6997 AQVVFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:cd05941    396 AAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
4536-4937 1.43e-10

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 68.37  E-value: 1.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4536 PPAIERCVHDQFAEQARARPDTPAIC---AWDG--ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLA 4610
Cdd:PRK08180    34 LGDYPRRLTDRLVHWAQEAPDRVFLAergADGGwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALA 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4611 VLKAGGAFVPLDP-------DHpaSRHEHIFRQTGAQVVLAS--AQYAT---LWTSLGRSVVIV--SEASTSQLPVVTKT 4676
Cdd:PRK08180   114 AMYAGVPYAPVSPayslvsqDF--GKLRHVLELLTPGLVFADdgAAFARalaAVVPADVEVVAVrgAVPGRAATPFAALL 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4677 ADPSVNPGNAAYA----------IFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFG--------ITD-----HT------- 4726
Cdd:PRK08180   192 ATPPTAAVDAAHAavgpdtiakfLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPflaeeppvLVDwlpwnHTfggnhnl 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4727 -RVLQF-ASYTFD------ACIA-------EIITTLLccgcicvpsdsdrrNNLAKAinamdvnWALLTPSVARmlDPCV 4791
Cdd:PRK08180   272 gIVLYNgGTLYIDdgkptpGGFDetlrnlrEISPTVY--------------FNVPKG-------WEMLVPALER--DAAL 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4792 VQS----LKILVLGGEQVNSADWDRWPK-SIQTI-------NAYGPTECSICCTTYSGKQGfKSGTIGTSIvsvswvvdP 4859
Cdd:PRK08180   329 RRRffsrLKLLFYAGAALSQDVWDRLDRvAEATCgerirmmTGLGMTETAPSATFTTGPLS-RAGNIGLPA--------P 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4860 ENHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFiDDpawllEGYgghsgrqgrlYKTGDLVRY----DADGNLVYL 4935
Cdd:PRK08180   400 GCEVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAF-DE-----EGY----------YRSGDAVRFvdpaDPERGLMFD 463

                   ..
gi 1820002560 4936 GR 4937
Cdd:PRK08180   464 GR 465
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
1955-2343 1.51e-10

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 68.38  E-value: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL----DPDHPASRHEDifrqTGAQVV 2030
Cdd:PRK04319    74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDRLED----SEAKVL 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2031 VTSAQHSARWIGTN-----HQVVTVSAGSLE----QFSTLVNPVD-----LPAKPENAAYVMFTSGSTGTPKGVVLEHRA 2096
Cdd:PRK04319   150 ITTPALLERKPADDlpslkHVLLVGEDVEEGpgtlDFNALMEQASdefdiEWTDREDGAILHYTSGSTGKPKGVLHVHNA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2097 VVTsclgHgqafgvtnllraLQFTAYTFDV-------CIAE----------IITTLVHGGCICVpsDSERRDNLA--KAI 2157
Cdd:PRK04319   230 MLQ----H------------YQTGKYVLDLheddvywCTADpgwvtgtsygIFAPWLNGATNVI--DGGRFSPERwyRIL 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2158 TDMQVNWGYLTSSVARLL---DPCLV-----PSLKVLVLGGEQVN--STDWGK-----------WpssvqtingygPTEc 2216
Cdd:PRK04319   292 EDYKVTVWYTAPTAIRMLmgaGDDLVkkydlSSLRHILSVGEPLNpeVVRWGMkvfglpihdnwW-----------MTE- 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2217 cvfcTGYTGIQGFQS-----GNIGTSIASV-SWVVDpeNHGRLAPLGSIGEL-LVEG-PILARGYLNDVDKTQAAFIDDp 2288
Cdd:PRK04319   360 ----TGGIMIANYPAmdikpGSMGKPLPGIeAAIVD--DQGNELPPNRMGNLaIKKGwPSMMRGIWNNPEKYESYFAGD- 432
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 2289 aWllegypghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVE 2343
Cdd:PRK04319   433 -W---------------YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE 471
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
5632-5789 1.52e-10

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 67.97  E-value: 1.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 5711
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 5712 EDTFRHTGAQVVVTSAQHSArwigtnhqvvtVSAGSLGQLSTLVNPVGLPAIPENAVYIMFTSGSTGIPKGVVLEHRA 5789
Cdd:PRK09029    93 EELLPSLTLDFALVLEGENT-----------FSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQA 159
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
3487-3881 1.56e-10

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 68.01  E-value: 1.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVplcfeksmwtvvamlavlkaggafvpldpdhpasrheEIFEQTgaqvvvasa 3566
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKV-------------------------------------AIFAET--------- 39
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3567 qySARW--TSSSCH-----VVTVSKALSSqlPAVVDSTN--------TSVRPENAAYIIFTSGSTGVPKGVVLEHRAVAT 3631
Cdd:cd17639     40 --RAEWliTALGCWsqnipIVTVYATLGE--DALIHSLNetecsaifTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVA 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3632 SCLGHGRAFG--ITNLSRVLqfaSYTFDACIAEIITTLLC---GGCIC-----------------------------VPS 3677
Cdd:cd17639    116 GIAGLGDRVPelLGPDDRYL---AYLPLAHIFELAAENVClyrGGTIGygsprtltdkskrgckgdltefkptlmvgVPA 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3678 --DSDRRNSLAKaISTM--------DVNWAFLTPSVARLLDPGLIPSL---KILAI-GGEQSS--------SADWNRWPG 3735
Cdd:cd17639    193 iwDTIRKGVLAK-LNPMgglkrtlfWTAYQSKLKALKEGPGTPLLDELvfkKVRAAlGGRLRYmlsggaplSADTQEFLN 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3736 SV--QKIHVYGPTECCifCTGYTTKQG-FEPSTIGTSVAS-----VSWvvdPE-NHNRLAPLgSMGELLMEGPILARGYL 3806
Cdd:cd17639    272 IVlcPVIQGYGLTETC--AGGTVQDPGdLETGRVGPPLPCceiklVDW---EEgGYSTDKPP-PRGEILIRGPNVFKGYY 345
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 3807 NDVDKTEAAFIDDpawllegypghpgrqgRLYKTGDLVQYNADGNLVYLGRKDSQVKVR-GQRVELGEVEHHVREC 3881
Cdd:cd17639    346 KNPEKTKEAFDGD----------------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSN 405
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
7067-7139 1.67e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 60.64  E-value: 1.67e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 7067 PSTEAERTMQQLWARMLKVKADSIGLDDSFFR-LGGDSIVAMKLVGEAR-RTGLQLSVADVFRHPRLVDLA-YVQN 7139
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEeEFGIELPDTELFEYPTVADLAdYLEE 77
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
24-258 1.68e-10

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 68.01  E-value: 1.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   24 LRILVMGGEQVnSADWDRWPSSV--QTINGYGPTECCivCTGYTSE-QDFTTGTIGTSIASVSW-VVDPKDHGRLA---- 95
Cdd:cd17639    252 LRYMLSGGAPL-SADTQEFLNIVlcPVIQGYGLTETC--AGGTVQDpGDLETGRVGPPLPCCEIkLVDWEEGGYSTdkpp 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   96 PLGsvgELLVEGPILARGYLSDPEKTAAVFinnpawlleghggyagRQGRLYKTGDLVRYDADGNLVCLGRKDSQVKLR- 174
Cdd:cd17639    329 PRG---EILIRGPNVFKGYYKNPEKTKEAF----------------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQn 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  175 GQRVELGEVEHHVREClpeakqLAVEVVLPLGQKNHATLAAFIQLDKGTHNALLKEKVGGDDSIARVVFLAGVEEELAKR 254
Cdd:cd17639    390 GEYIALEKLESIYRSN------PLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVINSEWEELCEDKKLQKAVLKS 463

                   ....
gi 1820002560  255 LPKH 258
Cdd:cd17639    464 LAET 467
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
1932-2444 1.93e-10

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 67.91  E-value: 1.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1932 HDLFTEQAKARPHAPAI--CAWDGE---LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAF 2006
Cdd:cd05970     20 YDVVDAMAKEYPDKLALvwCDDAGEeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2007 VPldPDHPASRHEDIFRQTGAQV--VVTSA--------QHSARWIGTNHQVVTVSAGSLEQF----------STLVNPVD 2066
Cdd:cd05970    100 IP--ATHQLTAKDIVYRIESADIkmIVAIAednipeeiEKAAPECPSKPKLVWVGDPVPEGWidfrkliknaSPDFERPT 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2067 LPAKP--ENAAYVMFTSGSTGTPKGVvlEHraVVTSCLGHGQAFGVTNLLR--ALQFTAYtfDVCIAEIITTLVHG---- 2138
Cdd:cd05970    178 ANSYPcgEDILLVYFSSGTTGMPKMV--EH--DFTYPLGHIVTAKYWQNVRegGLHLTVA--DTGWGKAVWGKIYGqwia 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2139 GCICVPSDSERRD--NLAKAITDMQVNWGYLTSSVARLL--------DpclVPSLKVLVLGGEQVNSTDWGKWP--SSVQ 2206
Cdd:cd05970    252 GAAVFVYDYDKFDpkALLEKLSKYGVTTFCAPPTIYRFLiredlsryD---LSSLRYCTTAGEALNPEVFNTFKekTGIK 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2207 TINGYGPTECCVFCTGYTGIQGfQSGNIGTSiaSVSW---VVDPEnhGRLAPLGSIGELLV---EG-PI-LARGYLNDVD 2278
Cdd:cd05970    329 LMEGFGQTETTLTIATFPWMEP-KPGSMGKP--APGYeidLIDRE--GRSCEAGEEGEIVIrtsKGkPVgLFGGYYKDAE 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2279 KTQAAFIDdpawlleGYpghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAV 2358
Cdd:cd05970    404 KTAEVWHD-------GY----------YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQ-HPAVLECAV 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2359 EVVPpsgerdhamlaafirldDETRNSplIIKyaednstAQIVFLTGIE--EELSERLPQHM----VPTVFFALVHF--- 2429
Cdd:cd05970    466 TGVP-----------------DPIRGQ--VVK-------ATIVLAKGYEpsEELKKELQDHVkkvtAPYKYPRIVEFvde 519
                          570
                   ....*....|....*.
gi 1820002560 2430 -PTTTSGKTDRKRLRE 2444
Cdd:cd05970    520 lPKTISGKIRRVEIRE 535
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
46-184 1.97e-10

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 67.77  E-value: 1.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   46 VQTINGYGPTECC-IVCTGYTSEQdfTTGTIGTSIASVSW-VVDPKDHGRLAPlGSVGELLVEGPILARGYLSDPEKTAA 123
Cdd:cd17640    238 IEVLNGYGLTETSpVVSARRLKCN--VRGSVGRPLPGTEIkIVDPEGNVVLPP-GEKGIVWVRGPQVMKGYYKNPEATSK 314
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560  124 VfINNPAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGR-KDSQVKLRGQRVELGEVE 184
Cdd:cd17640    315 V-LDSDGWF---------------NTGDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIE 360
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
1919-2314 2.15e-10

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 67.98  E-value: 2.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1919 WNQEVPPAIERCVHDLFTEQAKARPHAPAIC---AWDG--ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTV 1993
Cdd:PRK08180    29 RSAEPLGDYPRRLTDRLVHWAQEAPDRVFLAergADGGwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHA 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1994 VAMLAVLKAGGAFVPLDP-------DHPASRHedIFRQ-TGAQVVVTSAQHSARWI---GTNHQVVTVSAGSLEQ----- 2057
Cdd:PRK08180   109 LLALAAMYAGVPYAPVSPayslvsqDFGKLRH--VLELlTPGLVFADDGAAFARALaavVPADVEVVAVRGAVPGraatp 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2058 FSTLVNPVDLPA--------KPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAF--------------------- 2108
Cdd:PRK08180   187 FAALLATPPTAAvdaahaavGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFpflaeeppvlvdwlpwnhtfg 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2109 GVTNLLRALQftaytfdvciaeiittlvHGGC--IC----VPSDSERR-DNLAKAITDMQVN----WGYLTSSVARllDP 2177
Cdd:PRK08180   267 GNHNLGIVLY------------------NGGTlyIDdgkpTPGGFDETlRNLREISPTVYFNvpkgWEMLVPALER--DA 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2178 CLVPS----LKVLVLGGEQVNSTDWGKW-PSSVQTI-------NGYGPTE---CCVFCTGYTGiqgfQSGNIGTSIasvs 2242
Cdd:PRK08180   327 ALRRRffsrLKLLFYAGAALSQDVWDRLdRVAEATCgerirmmTGLGMTEtapSATFTTGPLS----RAGNIGLPA---- 398
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 2243 wvvdPENHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFiDDpawllEGYpghegrqgrlYKTGDLVRY 2314
Cdd:PRK08180   399 ----PGCEVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAF-DE-----EGY----------YRSGDAVRF 450
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
5217-5520 2.38e-10

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 67.29  E-value: 2.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5217 YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLlQVVVEEK-------IQWTESKRLEEYLREdkAVSM 5289
Cdd:cd19538     24 YNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPY-QLILEEDeatpkleIKEVDEEELESEINE--AVRY 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5290 glgdrlaRYALIKEP--------YDGGKRWFVWTIHHALYDGWSLPRILQAVKQIYSGAVPERQPSFNAF-IQY----LG 5356
Cdd:cd19538    101 -------PFDLSEEPpfratlfeLGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLpVQYadyaLW 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5357 QQDL------EAATL-----YWQTALADCKAALfpTLPPTVTQPVADT----TVEYQCPPP-----SQSATDiTTSTL-- 5414
Cdd:cd19538    174 QQELlgdesdPDSLIarqlaYWKKQLAGLPDEI--ELPTDYPRPAESSyeggTLTFEIDSElhqqlLQLAKD-NNVTLfm 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5415 -VRAAWAIVTSRYTSSDDVVFGATVTGRNApiAGVEAMVGPTIATVPLRVCLQKDQTVSTLLECLQQQSTDMIAHEQTGL 5493
Cdd:cd19538    251 vLQAGFAALLTRLGAGTDIPIGSPVAGRND--DSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAYEHQDIPF 328
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1820002560 5494 QRIAK-MSP---GARHACgFQTLLVVQPTDD 5520
Cdd:cd19538    329 ERLVEaLNPtrsRSRHPL-FQIMLALQNTPQ 358
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
996-1281 2.51e-10

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 66.37  E-value: 2.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  996 NTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQ----FASYTFDA-CIAEIITtllygGCICVPSES 1070
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIinpfFHTFGYKAgIVACLLT-----GATVVPVAV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1071 DRRNNLAKAISTMDVNCALLTPSVARLLepSAVPSLKRLVLQGEQVSFADWNRWPGSV-----------QTINGYGPTEC 1139
Cdd:cd17638     76 FDVDAILEAIERERITVLPGPPTLFQSL--LDHPGRKKFDLSSLRAAVTGAATVPVELvrrmrselgfeTVLTAYGLTEA 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1140 SvcCNTYSgkqgfKSGIIGTSVASLSWVVDAGNHNRLAplgSIGELLVEGPILARGYLNDIDKTEAAfIDDPAWLlegye 1219
Cdd:cd17638    154 G--VATMC-----RPGDDAETVATTCGRACPGFEVRIA---DDGEVLVRGYNVMQGYLDDPEATAEA-IDADGWL----- 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 1220 ghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQLAV 1281
Cdd:cd17638    218 ----------HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAE-HPGVAQVAV 268
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
878-1249 2.57e-10

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 67.63  E-value: 2.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKR--EDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL-DP-GHPASRHeeIFKQIGAQVV 953
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLyDTlGPEAIEY--ILNHAEISIV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  954 LTSSqhamlfasserhqvTVSKVSTSQLPTVVNFAKSPV---DPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSClgHGEA 1030
Cdd:cd05927     84 FCDA--------------GVKVYSLEEFEKLGKKNKVPPpppKPEDLATICYTSGTTGNPKGVMLTHGNIVSNV--AGVF 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1031 FGYTDHARVLQFASY--------TFDACIaeIITTLLYGGCICVPSESDRrnNLAKAISTmdvncalLTP----SVARLL 1098
Cdd:cd05927    148 KILEILNKINPTDVYisylplahIFERVV--EALFLYHGAKIGFYSGDIR--LLLDDIKA-------LKPtvfpGVPRVL 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1099 E---------PSAVPSLKRLVLQG----------EQVSFAD--W---------------NRW------PGSVQTI----- 1131
Cdd:cd05927    217 NriydkifnkVQAKGPLKRKLFNFalnyklaelrSGVVRASpfWdklvfnkikqalggnVRLmltgsaPLSPEVLeflrv 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1132 -------NGYGPTECS-VCCNTYSGKQ--GFKSGIIGTSVASLSWVVD-----AGNHNRlaplgsiGELLVEGPILARGY 1196
Cdd:cd05927    297 algcpvlEGYGQTECTaGATLTLPGDTsvGHVGGPLPCAEVKLVDVPEmnydaKDPNPR-------GEVCIRGPNVFSGY 369
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 1197 LNDIDKTEAAFIDDpAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRK 1249
Cdd:cd05927    370 YKDPEKTAEALDED-GWL---------------HTGDIGEWLPNGTLKIIDRK 406
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
3141-3367 2.58e-10

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 67.01  E-value: 2.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3141 QLNNGKVYLCLDINHAIIDAHSRGILMHDLQEAYDANL---NPQSTSFRDFASYIKQQSQ-------EEAGRYWAEYLDG 3210
Cdd:cd19533    119 TLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLkgrPAPPAPFGSFLDLVEEEQAyrqserfERDRAFWTEQFED 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3211 V-EPCFFPSLGDSGGANTIPRTVEVPSIDSSAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRdlpiHN 3289
Cdd:cd19533    199 LpEPVSLARRAPGRSLAFLRRTAELPPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR----LG 274
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3290 VNSI--FGPLISILPCRIHLHKQLTVLEALKTVQENYASSLSFQTFPLASMHSFLGL--GTSALFNTALSLQRID---DI 3362
Cdd:cd19533    275 AAARqtPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQRYRYEDLRRDLGLtgELHPLFGPTVNYMPFDyglDF 354

                   ....*
gi 1820002560 3363 GPCSA 3367
Cdd:cd19533    355 GGVVG 359
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
90-286 2.61e-10

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 67.29  E-value: 2.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   90 DHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNpaWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDS 169
Cdd:PRK03640   322 KDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG--WF---------------KTGDIGYLDEEGFLYVLDRRSD 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  170 QVKLRGQRVELGEVEhHVRECLPEAKQLAVevvlplgqknhatlaafiqldkgthnallkekVGGDDS------IARVVF 243
Cdd:PRK03640   385 LIISGGENIYPAEIE-EVLLSHPGVAEAGV--------------------------------VGVPDDkwgqvpVAFVVK 431
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560  244 LAGV-EEELA----KRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREI 286
Cdd:PRK03640   432 SGEVtEEELRhfceEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
1919-2445 2.68e-10

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 67.54  E-value: 2.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1919 WNQEVPPAIE--------RCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQ-LGVNPEDVVPLCFEKS 1989
Cdd:PRK12492     6 WNDKRPAGVPstidlaayKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1990 MWTVVAMLAVLKAGGAFVPLDPDHPAS--RHEdiFRQTGAQVVV---------------TSAQH-----------SARWI 2041
Cdd:PRK12492    86 LQYPIAVFGALRAGLIVVNTNPLYTARemRHQ--FKDSGARALVylnmfgklvqevlpdTGIEYlieakmgdllpAAKGW 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2042 GTNHQV----VTVSAGSLEQF----STLVNPVDLPAKP-----ENAAYVMFTSGSTGTPKGVVLEHRAVVT------SCL 2102
Cdd:PRK12492   164 LVNTVVdkvkKMVPAYHLPQAvpfkQALRQGRGLSLKPvpvglDDIAVLQYTGGTTGLAKGAMLTHGNLVAnmlqvrACL 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2103 GHGQAFGVTnLLRALQ---------FTAYTFDV-CIAEIITTlVHGGCICVPSDserrdnLAKAITDMQvNW------GY 2166
Cdd:PRK12492   244 SQLGPDGQP-LMKEGQevmiaplplYHIYAFTAnCMCMMVSG-NHNVLITNPRD------IPGFIKELG-KWrfsallGL 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2167 LTSSVARLLDPCL----VPSLKVLVLGGEQVNSTDWGKWPS--SVQTINGYGPTECC-VFCTGYTGIQGfQSGNIGTSIA 2239
Cdd:PRK12492   315 NTLFVALMDHPGFkdldFSALKLTNSGGTALVKATAERWEQltGCTIVEGYGLTETSpVASTNPYGELA-RLGTVGIPVP 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2240 SVSW-VVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTqAAFIDDPAWLlegypghegrqgrlyKTGDLVRYSSDG 2318
Cdd:PRK12492   394 GTALkVIDDD--GNELPLGERGELCIKGPQVMKGYWQQPEAT-AEALDAEGWF---------------KTGDIAVIDPDG 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2319 NLVCLGRKDSQVKVRGQRVELGEVEH----HmrkclPEANQLAVEVVPpsGERDHAMLAAFIRLDDETRNSPLIIKYAED 2394
Cdd:PRK12492   456 FVRIVDRKKDLIIVSGFNVYPNEIEDvvmaH-----PKVANCAAIGVP--DERSGEAVKLFVVARDPGLSVEELKAYCKE 528
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 2395 NSTAQivfltgieeelseRLPQHMVptVFFALvhfPTTTSGKTDRKRLREI 2445
Cdd:PRK12492   529 NFTGY-------------KVPKHIV--LRDSL---PMTPVGKILRRELRDI 561
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
5626-6144 2.71e-10

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 67.32  E-value: 2.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAkaRPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPED--MVPLCFEKSMWtvVAMLAVLKAGgaFVPLD 5703
Cdd:PRK10946    29 DILTRHA--ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDtaLVQLGNVAEFY--ITFFALLKLG--VAPVN 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5704 PDHPASRHEDT--FRHTGAQVVVTSAQHS------------ARWIGTNHQVVTVSAGSLGqLSTLVN--PVGLPAIPENA 5767
Cdd:PRK10946   103 ALFSHQRSELNayASQIEPALLIADRQHAlfsdddflntlvAEHSSLRVVLLLNDDGEHS-LDDAINhpAEDFTATPSPA 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5768 VYIMF---TSGSTGIPKGVVLEH-------RAVVTSCwgrgrafGITNLSRVLQF--ASYTFDACMDEIITTLMYGGCIC 5835
Cdd:PRK10946   182 DEVAFfqlSGGSTGTPKLIPRTHndyyysvRRSVEIC-------GFTPQTRYLCAlpAAHNYPMSSPGALGVFLAGGTVV 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5836 VPSDSDRRNdLVKAISTMDVS-CALLTPSVARLLEPSSVP-------TLQMLVLQGEQVSFADWNRWPASV--QTINGYG 5905
Cdd:PRK10946   255 LAPDPSATL-CFPLIEKHQVNvTALVPPAVSLWLQAIAEGgsraqlaSLKLLQVGGARLSETLARRIPAELgcQLQQVFG 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5906 PTECSICcntYSGKQGFKSGIIGTSVASVS-----WVVDPENHDrlAPLGSIGELLVEGPILARGYLNDIQKTAAVFiDD 5980
Cdd:PRK10946   334 MAEGLVN---YTRLDDSDERIFTTQGRPMSpddevWVADADGNP--LPQGEVGRLMTRGPYTFRGYYKSPQHNASAF-DA 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5981 pawllEGYpghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHhvreclpearqlaveVILpsgQK 6060
Cdd:PRK10946   408 -----NGF----------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIEN---------------LLL---RH 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6061 DHAMLAAFVQLEEgtqnalldkEASGEDSMAqvvFLASVEE----ELAKRLPEHMV-----PTVFFSLLHFPTTTSGKTD 6131
Cdd:PRK10946   455 PAVIHAALVSMED---------ELMGEKSCA---FLVVKEPlkavQLRRFLREQGIaefklPDRVECVDSLPLTAVGKVD 522
                          570
                   ....*....|...
gi 1820002560 6132 RKRLREIGASFTA 6144
Cdd:PRK10946   523 KKQLRQWLASRAS 535
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
6851-7041 2.78e-10

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 67.35  E-value: 2.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFVNDpawlveghgkhpgrrgRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:cd05920    331 PPGEEGELLTRGPYTIRGYYRAPEHNARAFTPD----------------GFYRTGDLVRRTPDGYLVVEGRIKDQINRGG 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6931 QRVELGEIENRLREcMPRATQMAVEVISPAGAAEQaktmVVAFLqlndeardallggnVPNDDNLSAqvvfpAKVDEKLS 7010
Cdd:cd05920    395 EKIAAEEVENLLLR-HPAVHDAAVVAMPDELLGER----SCAFV--------------VLRDPPPSA-----AQLRRFLR 450
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1820002560 7011 NL-LPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd05920    451 ERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
1933-2116 2.88e-10

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 67.59  E-value: 2.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGG--AFV--- 2007
Cdd:PRK08279    41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLntq 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2008 ----PL-------DPDHPASRHE--DIFRQTGAQVvvtSAQHSARWIGTNHQVVTVSAGSLEQFSTLVNPVDLPAKP--- 2071
Cdd:PRK08279   121 qrgaVLahslnlvDAKHLIVGEElvEAFEEARADL---ARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSgvt 197
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 2072 -ENAAYVMFTSGSTGTPKGVVLEHRAVVTSclghGQAFGVtnLLRA 2116
Cdd:PRK08279   198 aKDTAFYIYTSGTTGLPKAAVMSHMRWLKA----MGGFGG--LLRL 237
PRK06178 PRK06178
acyl-CoA synthetase; Validated
6847-7043 2.93e-10

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 67.37  E-value: 2.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6847 AALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNdpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQV 6926
Cdd:PRK06178   406 GELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD--GWL---------------HTGDIGKIDEQGFLHYLGRRKEML 468
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6927 KVRGQRVELGEIENRLrecmprATQMAVEVISPAGAAEQAKTMV-VAFLQLNDEARdallggnvpnddnlsaqvVFPAKV 7005
Cdd:PRK06178   469 KVNGMSVFPSEVEALL------GQHPAVLGSAVVGRPDPDKGQVpVAFVQLKPGAD------------------LTAAAL 524
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1820002560 7006 DEKLSNLLPSYMMPEVYFaVPQLPMMISGKTDRKRLRE 7043
Cdd:PRK06178   525 QAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDLQA 561
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
3487-3978 3.26e-10

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 67.23  E-value: 3.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHPASRHEEIF---EQTGAQVVV 3563
Cdd:PRK04319    74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPL---FEAFMEEAVRdrlEDSEAKVLI 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3564 AS-AQYS---ARWTSSSCHVVTVsKALSSQLPAVVD--------STNTS---VRPENAAYIIFTSGSTGVPKGVVLEHRA 3628
Cdd:PRK04319   151 TTpALLErkpADDLPSLKHVLLV-GEDVEEGPGTLDfnalmeqaSDEFDiewTDREDGAILHYTSGSTGKPKGVLHVHNA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3629 VatscLGHgrafgitnlsrvLQFASYTFDA-------CIAE----------IITTLLCGGCICVpsDSDRRNSLA--KAI 3689
Cdd:PRK04319   230 M----LQH------------YQTGKYVLDLheddvywCTADpgwvtgtsygIFAPWLNGATNVI--DGGRFSPERwyRIL 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3690 STMDVNWAFLTPSVARLL---DPGLI-----PSLK-ILAIGGEQSSSADWnrWPGSV--QKIH-VYGPTEC-CIFCTGYT 3756
Cdd:PRK04319   292 EDYKVTVWYTAPTAIRMLmgaGDDLVkkydlSSLRhILSVGEPLNPEVVR--WGMKVfgLPIHdNWWMTETgGIMIANYP 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3757 TkQGFEPSTIGTSVASV-SWVVDPENhNRLAPlGSMGEL-LMEG-PILARGYLNDVDKTEAAFIDDpaWllegypghpgr 3833
Cdd:PRK04319   370 A-MDIKPGSMGKPLPGIeAAIVDDQG-NELPP-NRMGNLaIKKGwPSMMRGIWNNPEKYESYFAGD--W----------- 433
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3834 qgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVRE--CLPEArqlavEVIlpsGQKDH---AMLAAFV 3908
Cdd:PRK04319   434 ----YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEhpAVAEA-----GVI---GKPDPvrgEIIKAFV 501
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 3909 QLEEGTQnallDKEAGGEDSMAQVvflasveeelAKRLPEHMVP--TVFFSLLhfPTTTSGKTDRKRL--REIG 3978
Cdd:PRK04319   502 ALRPGYE----PSEELKEEIRGFV----------KKGLGAHAAPreIEFKDKL--PKTRSGKIMRRVLkaWELG 559
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
3471-3976 3.38e-10

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 66.94  E-value: 3.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVplcfeksmwTVV-----AML----AVLKAGGAFVPL 3541
Cdd:cd12118     14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTV---------AVLapntpAMYelhfGVPMAGAVLNAL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3542 DPDHPASRHEEIFEQTGAQVVVASAQYSARwtssschvvtvskalssQLPAVVDSTNTSVRPENAAYII---FTSGSTGV 3618
Cdd:cd12118     85 NTRLDAEEIAFILRHSEAKVLFVDREFEYE-----------------DLLAEGDPDFEWIPPADEWDPIalnYTSGTTGR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3619 PKGVVLEHRAVATSCLGHGRAFGITNLSRVL----QF--ASYTFDACIAEIittllCGGCICVpsdsdrRNSLAKAI--- 3689
Cdd:cd12118    148 PKGVVYHHRGAYLNALANILEWEMKQHPVYLwtlpMFhcNGWCFPWTVAAV-----GGTNVCL------RKVDAKAIydl 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3690 ---------------STMDVNWAfltPSVARLLD-------PGLIPSLKILAiggeqsssadwNRWPGSVQKIHVYGPTE 3747
Cdd:cd12118    217 iekhkvthfcgaptvLNMLANAP---PSDARPLPhrvhvmtAGAPPPAAVLA-----------KMEELGFDVTHVYGLTE 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3748 C---CIFCT--------------GYTTKQGfepstIGTSVASVSWVVDPENHNRLAPLG-SMGELLMEGPILARGYLNDV 3809
Cdd:cd12118    283 TygpATVCAwkpewdelpteeraRLKARQG-----VRYVGLEEVDVLDPETMKPVPRDGkTIGEIVFRGNIVMKGYLKNP 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3810 DKTEAAFIDdpAWllegypghpgrqgrlYKTGDLVQYNADGnlvYLGRKDSQVKV---RGQRVELGEVE----HHvrecl 3882
Cdd:cd12118    358 EATAEAFRG--GW---------------FHSGDLAVIHPDG---YIEIKDRSKDIiisGGENISSVEVEgvlyKH----- 412
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3883 PEARQLAVeVILPSgQKDHAMLAAFVQLEEGtqnalldKEAGGEDSMAQVvflasveeelAKRLPEHMVP-TVFFSllHF 3961
Cdd:cd12118    413 PAVLEAAV-VARPD-EKWGEVPCAFVELKEG-------AKVTEEEIIAFC----------REHLAGFMVPkTVVFG--EL 471
                          570
                   ....*....|....*
gi 1820002560 3962 PTTTSGKTDRKRLRE 3976
Cdd:cd12118    472 PKTSTGKIQKFVLRD 486
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
6298-6570 3.79e-10

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 66.52  E-value: 3.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6298 YIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLlQVVVEEK-------IQWTESKRLEEYLREDKAVSM 6370
Cdd:cd19538     24 YNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPY-QLILEEDeatpkleIKEVDEEELESEINEAVRYPF 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6371 GLGDPLARYAIIKEAWGGKRWFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSFNAF-IQY----LSQQ------- 6438
Cdd:cd19538    103 DLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLpVQYadyaLWQQellgdes 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6439 ----DLEATAAYWQTALADCEATLfpPLPSSVKQlVADTTVE------------HQCPLPSRSTSDTTTSTLIRAAWAIV 6502
Cdd:cd19538    183 dpdsLIARQLAYWKKQLAGLPDEI--ELPTDYPR-PAESSYEggtltfeidselHQQLLQLAKDNNVTLFMVLQAGFAAL 259
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 6503 ASRYTSSDDVVFGTTITGRNApvTSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQqaTEMIAYEQ 6570
Cdd:cd19538    260 LTRLGAGTDIPIGSPVAGRND--DSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKE--TNLEAYEH 323
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
6710-6808 3.82e-10

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 66.85  E-value: 3.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6710 EQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 6789
Cdd:PRK07656    13 RAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
                           90
                   ....*....|....*....
gi 1820002560 6790 RHEDILRQTGAQVILASAQ 6808
Cdd:PRK07656    93 EAAYILARGDAKALFVLGL 111
PRK09192 PRK09192
fatty acyl-AMP ligase;
1955-2106 4.03e-10

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 66.95  E-value: 4.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVvvTSA 2034
Cdd:PRK09192    50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIAQLRGML--ASA 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2035 QHSA-----RWIGTNHQVVT----VSAGSLEQFSTLVNP-VDLP-AKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLG 2103
Cdd:PRK09192   128 QPAAiitpdELLPWVNEATHgnplLHVLSHAWFKALPEAdVALPrPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRA 207

                   ...
gi 1820002560 2104 HGQ 2106
Cdd:PRK09192   208 ISH 210
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
5080-5152 4.10e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 59.48  E-value: 4.10e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 5080 PSTEAERTMQQLWTRVLGIELNGIGLDDSFFR-LGGDSIAAMKLVGEAR-RTGLQLSVADVFRHPRLVDLA-YVQN 5152
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEeEFGIELPDTELFEYPTVADLAdYLEE 77
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
5648-6025 4.23e-10

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 66.86  E-value: 4.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVK--PEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdhpasrhEDTFrhtGAQvvvt 5725
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPL---------YDTL---GPE---- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5726 saqhSARWIgTNH---QVVTVSAG----SLGQLSTL-----VNPVglPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTS 5793
Cdd:cd05927     70 ----AIEYI-LNHaeiSIVFCDAGvkvySLEEFEKLgkknkVPPP--PPKPEDLATICYTSGTTGNPKGVMLTHGNIVSN 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5794 CWGRGRAFGITNLSRVLQ-FASY-----TFDACMdeIITTLMYGGCICVPSDSDR--RNDLVKAISTMdvscallTPSVA 5865
Cdd:cd05927    143 VAGVFKILEILNKINPTDvYISYlplahIFERVV--EALFLYHGAKIGFYSGDIRllLDDIKALKPTV-------FPGVP 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5866 RLLE---------PSSVPTLQMLVLQG----------EQVSFAD--W---------------NRW------PASVQTI-- 5901
Cdd:cd05927    214 RVLNriydkifnkVQAKGPLKRKLFNFalnyklaelrSGVVRASpfWdklvfnkikqalggnVRLmltgsaPLSPEVLef 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5902 ----------NGYGPTECS-ICCNTYSGKqgFKSGIIGTSVASVSW-VVD-PE-NHDRLAPLGSiGELLVEGPILARGYL 5967
Cdd:cd05927    294 lrvalgcpvlEGYGQTECTaGATLTLPGD--TSVGHVGGPLPCAEVkLVDvPEmNYDAKDPNPR-GEVCIRGPNVFSGYY 370
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 5968 NDIQKTAAVFIDDpAWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKL 6025
Cdd:cd05927    371 KDPEKTAEALDED-GWL---------------HTGDIGEWLPNGTLKIIDRKKNIFKL 412
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
6161-6229 4.39e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 59.48  E-value: 4.39e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 6161 PSTEAEQTMQKLWAQVLGIELNGIGLDDSFFR-LGGDSIAAMKLVGEAR-RIGLQLSVADIFRYARLVDLA 6229
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEeEFGIELPDTELFEYPTVADLA 72
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
7597-8123 4.71e-10

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 66.77  E-value: 4.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7597 WN----ADVPPAIE----RCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQ-LGVNPEDVVPLCFEKS 7667
Cdd:PRK12492     6 WNdkrpAGVPSTIDlaayKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7668 MWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARW----------------------TSSSCHV 7725
Cdd:PRK12492    86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVqevlpdtgieylieakmgdllpAAKGWLV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7726 VTVSKALSSQLP------------AVVDSTNTSVRP-----ENAAYIIFTSGSTGVPKGVVLEH-RAVAT-----SCLGH 7782
Cdd:PRK12492   166 NTVVDKVKKMVPayhlpqavpfkqALRQGRGLSLKPvpvglDDIAVLQYTGGTTGLAKGAMLTHgNLVANmlqvrACLSQ 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7783 GRAFG---ITNLSRVL-----QFASYTFDA-CIAEIIT---TLLcggcICVPSDSdrrNSLAKAIStmdvNWAFL----- 7845
Cdd:PRK12492   246 LGPDGqplMKEGQEVMiaplpLYHIYAFTAnCMCMMVSgnhNVL----ITNPRDI---PGFIKELG----KWRFSallgl 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7846 -TPSVARLLDPGL----IPSLKILAIGGEQSSSADWNRWPG--SVQKIHVYGPTECC-IFCT---GYTTKQGfepsTIGT 7914
Cdd:PRK12492   315 nTLFVALMDHPGFkdldFSALKLTNSGGTALVKATAERWEQltGCTIVEGYGLTETSpVASTnpyGELARLG----TVGI 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7915 SVASVSWVVDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTGDLVQYNA 7994
Cdd:PRK12492   391 PVPGTALKVIDDDGNEL-PLGERGELCIKGPQVMKGYWQQPEATAEA-LDAEGWF---------------KTGDIAVIDP 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7995 DGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVeVILPSGQKNHAMLAVFVQLGKGTHIAHLeeKAGGEDS 8074
Cdd:PRK12492   454 DGFVRIVDRKKDLIIVSGFNVYPNEIE-DVVMAHPKVANCAA-IGVPDERSGEAVKLFVVARDPGLSVEEL--KAYCKEN 529
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 8075 maqvvfLTGTeeelakRLPKHMVptVFFALlhfPMTTSGKADRKRLREI 8123
Cdd:PRK12492   530 ------FTGY------KVPKHIV--LRDSL---PMTPVGKILRRELRDI 561
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3486-3862 4.80e-10

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 66.33  E-value: 4.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3486 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVAs 3565
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIG- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3566 aqysarwtssschvvtVSKALssqlpavvdstntsvrpENAAyIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNL 3645
Cdd:cd05910     81 ----------------IPKAD-----------------EPAA-ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPG 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3646 SRVLQ----FAsyTFDACIAeiITTLLCGGCICVPSDSDRRnSLAKAISTMDVNWAFLTPSVARLL-----DPGL-IPSL 3715
Cdd:cd05910    127 EVDLAtfplFA--LFGPALG--LTSVIPDMDPTRPARADPQ-KLVGAIRQYGVSIVFGSPALLERVarycaQHGItLPSL 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3716 KILAIGGEQSSSADWNRW----PGSVQKIHVYGPTECCIFC----------TGYTTKQGfEPSTIGTSVASVSWVV---- 3777
Cdd:cd05910    202 RRVLSAGAPVPIALAARLrkmlSDEAEILTPYGATEALPVSsigsrellatTTAATSGG-AGTCVGRPIPGVRVRIieid 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3778 ---DPENHNRLA-PLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPawllegypghpgRQGRLYKTGDLVQYNADGNLV 3853
Cdd:cd05910    281 depIAEWDDTLElPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN------------SEGFWHRMGDLGYLDDEGRLW 348

                   ....*....
gi 1820002560 3854 YLGRKDSQV 3862
Cdd:cd05910    349 FCGRKAHRV 357
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
4567-5069 4.81e-10

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 66.86  E-value: 4.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVK--PEDMVPLCFEKSMWTVVAMLAVLKAGGAFVP----LDPDhpASrhEHIFRQTGAQ 4640
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPlydtLGPE--AI--EYILNHAEIS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4641 VVLASAQYaTLWT-----SLGRSvvivseastSQLPVVTKTADpsvnpgNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLG 4715
Cdd:cd05927     82 IVFCDAGV-KVYSleefeKLGKK---------NKVPPPPPKPE------DLATICYTSGTTGNPKGVMLTHGNIVSNVAG 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4716 ------HGQAFGITD---------HT--RVLQFASYTFDACIA----------EIITTL---LCCGcicVP--------- 4756
Cdd:cd05927    146 vfkileILNKINPTDvyisylplaHIfeRVVEALFLYHGAKIGfysgdirlllDDIKALkptVFPG---VPrvlnriydk 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4757 ------SDSDRRNNLAKAinAMDVNWALLTPSVAR---MLDPCV---VQSL-----KILVLGGEQVNSADWD--RWPKSI 4817
Cdd:cd05927    223 ifnkvqAKGPLKRKLFNF--ALNYKLAELRSGVVRaspFWDKLVfnkIKQAlggnvRLMLTGSAPLSPEVLEflRVALGC 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4818 QTINAYGPTECS-ICCTTYSGKqgFKSGTIGTSIVSVSW-VVD-PE-NHNRLAPLGSiGELLVEGPILARGYLNDMEKTE 4893
Cdd:cd05927    301 PVLEGYGQTECTaGATLTLPGD--TSVGHVGGPLPCAEVkLVDvPEmNYDAKDPNPR-GEVCIRGPNVFSGYYKDPEKTA 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4894 AAFIDDpAWLlegygghsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQVKL-RGQRVELGEVEH-HVRECLTEA------ 4965
Cdd:cd05927    378 EALDED-GWL---------------HTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENiYARSPFVAQifvygd 441
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4966 --KQLAVEVIVPEGEggYAMLAAFVQLGDD-TYNTLVKEKaggdsltvqvVFLDRVEEELaKRVPEHMMLTTF------- 5035
Cdd:cd05927    442 slKSFLVAIVVPDPD--VLKEWAASKGGGTgSFEELCKNP----------EVKKAILEDL-VRLGKENGLKGFeqvkaih 508
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1820002560 5036 -----FTLEAMPTTTSGKIDRKRLREigasFTAQQLAEM 5069
Cdd:cd05927    509 lepepFSVENGLLTPTFKLKRPQLKK----YYKKQIDEM 543
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
4000-4068 4.89e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 59.48  E-value: 4.89e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 4000 PSTEAEQTMQQLWAQVLSLGADIIGLDDSFFR-LGGDSIAAMKLVGEAR-RMGLHLSVADIFRHPKLADFA 4068
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEeEFGIELPDTELFEYPTVADLA 72
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
4567-5058 5.08e-10

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 66.84  E-value: 5.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL----DPDHPASRHEhifrQTGAQVV 4642
Cdd:PRK04319    74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDRLE----DSEAKVL 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4643 LAS-AQY----ATLWTSLgRSVVIVSEASTSQLPVVT-----KTADPS-----VNPGNAAYAIFTSGSTGIPKGVVLEHK 4707
Cdd:PRK04319   150 ITTpALLerkpADDLPSL-KHVLLVGEDVEEGPGTLDfnalmEQASDEfdiewTDREDGAILHYTSGSTGKPKGVLHVHN 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4708 AVVTsclghgqafgitdHtrvLQFASYTFDA-------CIAE----------IITTLLCCGCICVpsDSDRRNNLA--KA 4768
Cdd:PRK04319   229 AMLQ-------------H---YQTGKYVLDLheddvywCTADpgwvtgtsygIFAPWLNGATNVI--DGGRFSPERwyRI 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4769 INAMDVNWALLTPSVARML---DPCVVQ-----SLKILVLGGEQVNsADWDRWPKSI----------QTinaygPTECSI 4830
Cdd:PRK04319   291 LEDYKVTVWYTAPTAIRMLmgaGDDLVKkydlsSLRHILSVGEPLN-PEVVRWGMKVfglpihdnwwMT-----ETGGIM 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4831 CCTTYSgkQGFKSGTIGTSIVSV-SWVVDPENhNRLAPlGSIGEL-LVEG-PILARGYLNDMEKTEAAFIDDpaWllegy 4907
Cdd:PRK04319   365 IANYPA--MDIKPGSMGKPLPGIeAAIVDDQG-NELPP-NRMGNLaIKKGwPSMMRGIWNNPEKYESYFAGD--W----- 433
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4908 gghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhhvrECLTEAKQLA-VEVI-VPE---GEggya 4982
Cdd:PRK04319   434 ----------YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE----SKLMEHPAVAeAGVIgKPDpvrGE---- 495
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 4983 MLAAFVQLGDDTyntlvkekAGGDSLTVQVvfLDRVEEELAKRV-PEHMmltTFftLEAMPTTTSGKIDRKRL--REIG 5058
Cdd:PRK04319   496 IIKAFVALRPGY--------EPSEELKEEI--RGFVKKGLGAHAaPREI---EF--KDKLPKTRSGKIMRRVLkaWELG 559
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
1956-2444 5.44e-10

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 66.54  E-value: 5.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1956 TYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSAQ 2035
Cdd:PLN02330    57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2036 HSARWIGTNHQVVTVSAGSLE---QFSTLVNPVDLPAKPENAAYVM--------FTSGSTGTPKGVVLEHRAVV----TS 2100
Cdd:PLN02330   137 NYGKVKGLGLPVIVLGEEKIEgavNWKELLEAADRAGDTSDNEEILqtdlcalpFSSGTTGISKGVMLTHRNLVanlcSS 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2101 CLGHG-QAFG-VTNLLRALQFTAYTF-DVCIAeiitTLVHGGCICVPSDSERRDNLAKAITDmQVNWGYLTSSVARLL-- 2175
Cdd:PLN02330   217 LFSVGpEMIGqVVTLGLIPFFHIYGItGICCA----TLRNKGKVVVMSRFELRTFLNALITQ-EVSFAPIVPPIILNLvk 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2176 DPCL----VPSLKVLV-------LGGEQVNSTDwGKWPsSVQTINGYGPTE--CCVFCTGytgiqgfqSGNIGTSIA--- 2239
Cdd:PLN02330   292 NPIVeefdLSKLKLQAimtaaapLAPELLTAFE-AKFP-GVQVQEAYGLTEhsCITLTHG--------DPEKGHGIAkkn 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2240 SVSWV--------VDPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTqAAFIDDPAWLlegypghegrqgrlyKTGDL 2311
Cdd:PLN02330   362 SVGFIlpnlevkfIDPDT-GRSLPKNTPGELCVRSQCVMQGYYNNKEET-DRTIDEDGWL---------------HTGDI 424
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2312 VRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMrkcLPEANQLAVEVVPPSGERDHAMLAAFIRLDDETRNSpliiky 2391
Cdd:PLN02330   425 GYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAIL---LTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKES------ 495
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 2392 aednstaqivfltgiEEELSERLPQHMVPTVFFALVHF----PTTTSGKTDRKRLRE 2444
Cdd:PLN02330   496 ---------------EEDILNFVAANVAHYKKVRVVQFvdsiPKSLSGKIMRRLLKE 537
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
4536-4958 5.65e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 66.61  E-value: 5.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4536 PPAIERCVHDQFAEQARARPDTPAIC-------AWDGeLTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAM 4608
Cdd:PRK12582    44 LGPYPRSIPHLLAKWAAEAPDRPWLAqrepghgQWRK-VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMT 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4609 LAVLKAGgafVPLDPDHPA--------SRHEHIFRQTGAQVVLA--SAQYATLWTSL---GRSVVIVS-----EASTSQL 4670
Cdd:PRK12582   123 LAAMQAG---VPAAPVSPAyslmshdhAKLKHLFDLVKPRVVFAqsGAPFARALAALdllDVTVVHVTgpgegIASIAFA 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4671 PVVTKTADPSV-------NPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAF------GITDHTRVLQFaSYTFD 4737
Cdd:PRK12582   200 DLAATPPTAAVaaaiaaiTPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRprepdpPPPVSLDWMPW-NHTMG 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4738 ACIA---------------------EIITTLlccgcicvpsdsdrrNNLAK----AINAMDVNWALLTPSVARmlDPCVV 4792
Cdd:PRK12582   279 GNANfngllwgggtlyiddgkplpgMFEETI---------------RNLREisptVYGNVPAGYAMLAEAMEK--DDALR 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4793 QS----LKILVLGGEQVNSADWDRWPK-SIQTI-------NAYGPTEcsiccttysgkqgfksgTIGTSiVSVSWVVD-- 4858
Cdd:PRK12582   342 RSffknLRLMAYGGATLSDDLYERMQAlAVRTTghripfyTGYGATE-----------------TAPTT-TGTHWDTErv 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4859 -------PENHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFiDDpawllEGYgghsgrqgrlYKTGDLVRY----D 4927
Cdd:PRK12582   404 gliglplPGVELKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAF-DE-----EGF----------YRLGDAARFvdpdD 467
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1820002560 4928 ADGNLVYLGRKDSQVKL-RGQRVELGEVEHHV 4958
Cdd:PRK12582   468 PEKGLIFDGRVAEDFKLsTGTWVSVGTLRPDA 499
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
456-707 6.06e-10

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 65.80  E-value: 6.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  456 DVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLLQV-------VVEEKMQWTESESLEEYLNEDKAASMGL-GDRLARYA 527
Cdd:cd20484     35 KLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIepskplsFQEEDISSLKESEIIAYLREKAKEPFVLeNGPLMRVH 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  528 LIkeSCGGKRWFVW-TIHHALYDGWS-LPLV---LDAVKQVYSGAALERQPSFNTFIQYVS-QQDVKAAA------AYWQ 595
Cdd:cd20484    115 LF--SRSEQEHFVLiTIHHIIFDGSSsLTLIhslLDAYQALLQGKQPTLASSPASYYDFVAwEQDMLAGAegeehrAYWK 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  596 TALADCEAVL--FPPLPSTVTQPVADTTVKYQCPP--SPEVTS----SNITTSTLIRAAWAIIASRYTSSEDIVFGTTVT 667
Cdd:cd20484    193 QQLSGTLPILelPADRPRSSAPSFEGQTYTRRLPSelSNQIKSfarsQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTM 272
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1820002560  668 GRnaPITGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQ 707
Cdd:cd20484    273 GR--PEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQ 310
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
6706-6808 6.12e-10

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 66.66  E-value: 6.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6706 DLFTEQALARPNAPAVCAWDG----ELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP 6781
Cdd:COG1022     15 DLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
                           90       100
                   ....*....|....*....|....*..
gi 1820002560 6782 LDPDHPASRHEDILRQTGAQVILASAQ 6808
Cdd:COG1022     95 IYPTSSAEEVAYILNDSGAKVLFVEDQ 121
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
10-285 6.28e-10

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 66.34  E-value: 6.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   10 PSVARLLEPSHI-----PSLRILVMGGEQVNSADWDRWP--SSVQTINGYGPTECCIVCTGYTSEQdFTTGTIGTsiASV 82
Cdd:cd05928    274 PTVYRMLVQQDLssykfPSLQHCVTGGEPLNPEVLEKWKaqTGLDIYEGYGQTETGLICANFKGMK-IKPGSMGK--ASP 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   83 SW---VVDpkDHGRLAPLGSVGELLVE-GPI----LARGYLSDPEKTAAVFinnpawlleghggyagrQGRLYKTGDLVR 154
Cdd:cd05928    351 PYdvqIID--DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATI-----------------RGDFYLTGDRGI 411
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  155 YDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAV---------EVVlplgqknhatlAAFIQLDKGthn 225
Cdd:cd05928    412 MDEDGYFWFMGRADDVINSSGYRIGPFEVESALIE-HPAVVESAVvsspdpirgEVV-----------KAFVVLAPQ--- 476
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560  226 allkekvggddsiarvvFLAGVEEELAKRLPKHM--------VPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:cd05928    477 -----------------FLSHDPEQLTKELQQHVksvtapykYPRKVEFVQELPKTVTGKIQRNELRD 527
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
3471-3840 6.38e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 66.25  E-value: 6.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPA-ICAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 3548
Cdd:PRK13391     7 AQTTPDKPAvIMASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3549 RHEEIFEQTGAQVVVASAQYSArwtssschvvtVSKALSSQLPAV-----VDSTNTSVRPEN-----AAY---------- 3608
Cdd:PRK13391    87 EAAYIVDDSGARALITSAAKLD-----------VARALLKQCPGVrhrlvLDGDGELEGFVGyaeavAGLpatpiadesl 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3609 ---IIFTSGSTGVPKGVV--LEHRAVATSC----LGHgRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDS 3679
Cdd:PRK13391   156 gtdMLYSSGTTGRPKGIKrpLPEQPPDTPLpltaFLQ-RLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHF 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3680 DRRNSLAkAISTMDVNWAFLTPSV-ARLL-------DPGLIPSLKIlAIGGEQSSSADWNR----WPGSVqkIH-VYGPT 3746
Cdd:PRK13391   235 DAEQYLA-LIEEYGVTHTQLVPTMfSRMLklpeevrDKYDLSSLEV-AIHAAAPCPPQVKEqmidWWGPI--IHeYYAAT 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3747 ECCIFcTGYTTKQGFE-PSTIGTSVASVSWVVDPenHNRLAPLGSMGELLMEGPILARgYLNDVDKTEAAFIDDPAWLLE 3825
Cdd:PRK13391   311 EGLGF-TACDSEEWLAhPGTVGRAMFGDLHILDD--DGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGTWSTV 386
                          410
                   ....*....|....*
gi 1820002560 3826 GYPGHPGRQGRLYKT 3840
Cdd:PRK13391   387 GDIGYVDEDGYLYLT 401
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
994-1366 6.85e-10

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 65.19  E-value: 6.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  994 PGNTAYIIFTSGTTGIPKgvVLQHR----AVTTSCLGHGEAFGYTDharVLQFASYTF--DACIAEIITTLLYGGCICVP 1067
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPK--LAQHThsneVYNAWMLALNSLFDPDD---VLLCGLPLFhvNGSVVTLLTPLASGAHVVLA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1068 SESDRRN-----NLAKAISTMDVNCALLTPSV-ARLLepsAVP------SLKRLVLQGEQVSFADWNRWPGS--VQTING 1133
Cdd:cd05944     76 GPAGYRNpglfdNFWKLVERYRITSLSTVPTVyAALL---QVPvnadisSLRFAMSGAAPLPVELRARFEDAtgLPVVEG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1134 YGPTE--CSVCCNTYSGKQgfKSGIIGTSVASLS---WVVDA-GNHNRLAPLGSIGELLVEGPILARGYLNDIDKtEAAF 1207
Cdd:cd05944    153 YGLTEatCLVAVNPPDGPK--RPGSVGLRLPYARvriKVLDGvGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGN-KNAF 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1208 IDDpAWLlegyeghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhhvrECLpeARQLAVEVILPS 1287
Cdd:cd05944    230 VAD-GWL---------------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIE----EAL--LRHPAVAFAGAV 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1288 GQKE-HA--LLAAFIQLDKGnhnALFEEKAsgedsmaqvvfltgVEEELAKRLPEH-MVPTILFTVKAMPITTSGKIDRK 1363
Cdd:cd05944    288 GQPDaHAgeLPVAYVQLKPG---AVVEEEE--------------LLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKP 350

                   ...
gi 1820002560 1364 RLQ 1366
Cdd:cd05944    351 ALR 353
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
22-280 6.94e-10

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 64.97  E-value: 6.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   22 PSLRILVMGGEQVNSAD--WDRWPSSVQTINGYGPTECCIVCTGYTSEQDFTTGTIGTSIASVSWVVDPKDhGRLAPLGS 99
Cdd:cd17635    117 PSLRLIGYGGSRAIAADvrFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATD-GIAGPSAS 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  100 VGELLVEGPILARGYLSDPEKTAAVFInnpawlleghGGYagrqgrlYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVE 179
Cdd:cd17635    196 FGTIWIKSPANMLGYWNNPERTAEVLI----------DGW-------VNTGDLGERREDGFLFITGRSSESINCGGVKIA 258
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  180 LGEVEHhVRECLPEAKQLAVEVVlplgqkNHATLAAFIQLdkgthnALLKEKVGgDDSIARvvflaGVEEELAKRLPKHM 259
Cdd:cd17635    259 PDEVER-IAEGVSGVQECACYEI------SDEEFGELVGL------AVVASAEL-DENAIR-----ALKHTIRRELEPYA 319
                          250       260
                   ....*....|....*....|.
gi 1820002560  260 VPTVFFALLHFPTTTSGKTDR 280
Cdd:cd17635    320 RPSTIVIVTDIPRTQSGKVKR 340
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
6303-6569 7.00e-10

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 65.74  E-value: 7.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6303 VLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQVVVE-----EKIQWTESK----RLEEYLREDKAVSMGLG 6373
Cdd:cd20483     29 VCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDpsfhlIVIDLSEAAdpeaALDQLVRNLRRQELDIE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6374 D-PLARYAIIKEAwgGKRW-FVWTIHHALYDGWSLPRVLQAVKQAYN----GAVLET--QPSFNaFIQY-------LSQQ 6438
Cdd:cd20483    109 EgEVIRGWLVKLP--DEEFaLVLASHHIAWDRGSSKSIFEQFTALYDalraGRDLATvpPPPVQ-YIDFtlwhnalLQSP 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6439 DLEATAAYWQTALADC-EATLFPPLPSSVKQLVADT-TVEHQCPLPSR---------STSDTTTSTLIRAAWAIVASRYT 6507
Cdd:cd20483    186 LVQPLLDFWKEKLEGIpDASKLLPFAKAERPPVKDYeRSTVEATLDKEllarmkricAQHAVTPFMFLLAAFRAFLYRYT 265
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 6508 SSDDVVFGttITGRNAPVTSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEmiAYE 6569
Cdd:cd20483    266 EDEDLTIG--MVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLE--AYE 323
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
8142-8214 7.35e-10

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 59.19  E-value: 7.35e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  8142 PKRQPLTEAEQTMQQLWARVLGI-DADIIGLDDSFFRLGGDSIAAMKLVGE-ARRTGLQLSVADIFRHPRLIDLA 8214
Cdd:smart00823    5 PPAERRRLLLDLVREQVAAVLGHaAAEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALA 79
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
6850-7042 8.10e-10

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 65.39  E-value: 8.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6850 APLGSIGELLV---EGPILARGYLNDADKTAAAFvndpawlveghgkhpgrRGRLYKTGDLVYYNKDGNLVYIGRKDGQV 6926
Cdd:cd05934    267 LPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-----------------RNGWFHTGDLGYRDADGFFYFVDRKKDMI 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6927 KVRGQRVELGEIENRL------RECmpratqMAVEVISPAGAAEqaktmVVAFLQLNDEARDAllggnvpnddnlsaqvv 7000
Cdd:cd05934    330 RRRGENISSAEVERAIlrhpavREA------AVVAVPDEVGEDE-----VKAVVVLRPGETLD----------------- 381
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 7001 fPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLR 7042
Cdd:cd05934    382 -PEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
8288-8511 8.63e-10

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 65.47  E-value: 8.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8288 IDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIPRHQDLPFSIFEVNGALAEESQAIHI--RDLDQTSPLGL 8365
Cdd:cd19533     30 LEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHIDLSGDPDPEGAAQQWmqEDLRKPLPLDN 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8366 PT--SFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQ---QEPLLSTTGFHSYLAYV----------HNQRSA 8430
Cdd:cd19533    110 DPlfRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTallKGRPAPPAPFGSFLDLVeeeqayrqseRFERDR 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8431 siNYWSRLLKG----SHITNITSKLRPKLGKDTTIRSVKVERVIRTPQLPTGLTMASLVSSAWAVVLSHISGEEDVVYGL 8506
Cdd:cd19533    190 --AFWTEQFEDlpepVSLARRAPGRSLAFLRRTAELPPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGV 267

                   ....*
gi 1820002560 8507 VVAGR 8511
Cdd:cd19533    268 PVMGR 272
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
1939-2314 8.69e-10

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 65.92  E-value: 8.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGE-----LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP-- 2011
Cdd:cd05921      5 ARQAPDRTWLAEREGNggwrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPay 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2012 -----DHPASRHedIFRQ-TGAQVVVTSAQHSARWIGTN---HQVVTVSAGSLE-----QFSTL--------VNPVDLPA 2069
Cdd:cd05921     85 slmsqDLAKLKH--LFELlKPGLVFAQDAAPFARALAAIfplGTPLVVSRNAVAgrgaiSFAELaatpptaaVDAAFAAV 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2070 KPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTN-----LLRALQFTaYTFDVCIAeIITTLVHGGCICV- 2143
Cdd:cd05921    163 GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGeeppvLVDWLPWN-HTFGGNHN-FNLVLYNGGTLYId 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2144 ---PSD---SERRDNLAKAITDMQVN----WGYLTSSVARllDPCLVPS----LKVLVLGGEQVNSTDWGKWPS-SVQTI 2208
Cdd:cd05921    241 dgkPMPggfEETLRNLREISPTVYFNvpagWEMLVAALEK--DEALRRRffkrLKLMFYAGAGLSQDVWDRLQAlAVATV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2209 N-------GYGPTECCVFCTGYTGIQGfQSGNIGTSIasvswvvdPENHGRLAPLGSIGELLVEGPILARGYLNDVDKTQ 2281
Cdd:cd05921    319 GeripmmaGLGATETAPTATFTHWPTE-RSGLIGLPA--------PGTELKLVPSGGKYEVRVKGPNVTPGYWRQPELTA 389
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1820002560 2282 AAFiDDpawllEGYpghegrqgrlYKTGDLVRY 2314
Cdd:cd05921    390 QAF-DE-----EGF----------YCLGDAAKL 406
PRK06145 PRK06145
acyl-CoA synthetase; Validated
23-285 8.80e-10

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 65.68  E-value: 8.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSA---DWDRWPSSVQTINGYGPTECCIVCTGYTSEQDF-TTGTIGTSIASVSWVVdPKDHGRLAPLG 98
Cdd:PRK06145   265 SLAWCIGGGEKTPESrirDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIeKIGSTGRALAHVEIRI-ADGAGRWLPPN 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   99 SVGELLVEGPILARGYLSDPEKTAAVFINNpaWLLEGHGGYAGRQGRLYKTgdlvrydadgnlvclGRKDSQVKLRGQRV 178
Cdd:PRK06145   344 MKGEICMRGPKVTKGYWKDPEKTAEAFYGD--WFRSGDVGYLDEEGFLYLT---------------DRKKDMIISGGENI 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  179 ELGEVEHHVREcLPEAKQLAVevvlplgqknhatlaafiqldKGTHNALLKEKVggddsIARVVFLAGVEEELA------ 252
Cdd:PRK06145   407 ASSEVERVIYE-LPEVAEAAV---------------------IGVHDDRWGERI-----TAVVVLNPGATLTLEaldrhc 459
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1820002560  253 -KRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:PRK06145   460 rQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
7634-8021 8.88e-10

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 65.98  E-value: 8.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7634 TYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPldPDHPASRHEEIF--EQTGAQVVVAS 7711
Cdd:cd05970     49 TFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP--ATHQLTAKDIVYriESADIKMIVAI 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7712 A----QYSARWTSSSCHVVTVSKALSSQLP-------AVVDSTNTSVRP---------ENAAYIIFTSGSTGVPKGVvlE 7771
Cdd:cd05970    127 AedniPEEIEKAAPECPSKPKLVWVGDPVPegwidfrKLIKNASPDFERptansypcgEDILLVYFSSGTTGMPKMV--E 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7772 HraVATSCLGH-GRAFGITNL---SRVLQFASYTFDACI-AEIITTLLCGGCICVpSDSDR---RNSLAKaISTMDVNWA 7843
Cdd:cd05970    205 H--DFTYPLGHiVTAKYWQNVregGLHLTVADTGWGKAVwGKIYGQWIAGAAVFV-YDYDKfdpKALLEK-LSKYGVTTF 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7844 FLTPSVARLL--------DpglIPSLKILAIGGEQSSSADWNRWPG--SVQKIHVYGPTECCIfCTGytTKQGFEPSTIG 7913
Cdd:cd05970    281 CAPPTIYRFLiredlsryD---LSSLRYCTTAGEALNPEVFNTFKEktGIKLMEGFGQTETTL-TIA--TFPWMEPKPGS 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7914 TSVASVSWVVDPENHN-RLAPLGSMGEL---LMEG-PI-LARGYLNDVDKTEAAFIDdpawlleGYpghpgrqgrlYKTG 7987
Cdd:cd05970    355 MGKPAPGYEIDLIDREgRSCEAGEEGEIvirTSKGkPVgLFGGYYKDAEKTAEVWHD-------GY----------YHTG 417
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1820002560 7988 DLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 8021
Cdd:cd05970    418 DAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVE 451
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
1954-2343 9.33e-10

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 65.54  E-value: 9.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1954 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTS 2033
Cdd:cd05914      7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2034 aqhsarwigtnhqvvtvsagsleqfstlvnpvdlpaKPENAAYVMFTSGSTGTPKGVVLEHRAVVT-------------- 2099
Cdd:cd05914     87 ------------------------------------DEDDVALINYTSGTTGNSKGVMLTYRNIVSnvdgvkevvllgkg 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2100 ----SCLGHGQAFG-VTNLLRALQFTAY-------TFDVCIA----EIITTLVhggcICVPSDSERRD------------ 2151
Cdd:cd05914    131 dkilSILPLHHIYPlTFTLLLPLLNGAHvvfldkiPSAKIIAlafaQVTPTLG----VPVPLVIEKIFkmdiipkltlkk 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2152 ---NLAKAITDMQVnwgylTSSVARLLDPCLVPSLKVLVLGGEQVN---STDWGKwpSSVQTINGYGPTECCVFCTgYTG 2225
Cdd:cd05914    207 fkfKLAKKINNRKI-----RKLAFKKVHEAFGGNIKEFVIGGAKINpdvEEFLRT--IGFPYTIGYGMTETAPIIS-YSP 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2226 IQGFQSGNIGTSIASVSWVVDPENhgrlaPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpAWLlegypghegrqgrl 2305
Cdd:cd05914    279 PNRIRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKD-GWF-------------- 338
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1820002560 2306 yKTGDLVRYSSDGNLVCLGRKDSQ-VKVRGQRVELGEVE 2343
Cdd:cd05914    339 -HTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIE 376
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
4690-5051 1.11e-09

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 64.21  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4690 IFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITD-----------HTRVLQFASYTFDACIAEIITTLLccgcicvpsD 4758
Cdd:cd17637      6 IHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEadvylnmlplfHIAGLNLALATFHAGGANVVMEKF---------D 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4759 SDRrnnLAKAINAMDVN-WALLTPSVARMLD-----PCVVQSLKIlVLGGEQvnsadwdrwPKSIQ----TINA-----Y 4823
Cdd:cd17637     77 PAE---ALELIEEEKVTlMGSFPPILSNLLDaaeksGVDLSSLRH-VLGLDA---------PETIQrfeeTTGAtfwslY 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4824 GPTECSiCCTTYSgKQGFKSGTIG-TSIVSVSWVVDPENhnRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDdpaw 4902
Cdd:cd17637    144 GQTETS-GLVTLS-PYRERPGSAGrPGPLVRVRIVDDND--RPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRN---- 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4903 llegyGGHsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQ--VKLRGQRVELGEVEHHVRE--CLTEakqlaVEVI-VPEG 4977
Cdd:cd17637    216 -----GWH--------HTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEhpAIAE-----VCVIgVPDP 277
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 4978 EGGYAMLAafvqlgddtyntlVKEKAGGDSLTVQVVfLDRVEEELA--KRvPEHMMLTtfftlEAMPTTTSGKIDR 5051
Cdd:cd17637    278 KWGEGIKA-------------VCVLKPGATLTADEL-IEFVGSRIAryKK-PRYVVFV-----EALPKTADGSIDR 333
PRK07638 PRK07638
acyl-CoA synthetase; Validated
7621-8123 1.34e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 65.19  E-value: 1.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7621 PGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLcFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIF 7700
Cdd:PRK07638    15 PNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAIL-LENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7701 EQTGAQVVVASAQYSARWTSSSCHVVTVSK---ALSSQLPAVVDSTNTSVRPenaAYIIFTSGSTGVPKGVVLEHRAVAT 7777
Cdd:PRK07638    94 AISNADMIVTERYKLNDLPDEEGRVIEIDEwkrMIEKYLPTYAPIENVQNAP---FYMGFTSGSTGKPKAFLRAQQSWLH 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7778 SCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICV-----PsdsdrrNSLAKAISTMDVNWAFLTPSVARL 7852
Cdd:PRK07638   171 SFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLmrkfiP------NQVLDKLETENISVMYTVPTMLES 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7853 L---DPGLIPSLKILaiggeqSSSADW---------NRWPgSVQKIHVYGPTECCiFCTgYTTKQGFE--PSTIGTSVAS 7918
Cdd:PRK07638   245 LykeNRVIENKMKII------SSGAKWeaeakekikNIFP-YAKLYEFYGASELS-FVT-ALVDEESErrPNSVGRPFHN 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7919 VSWVVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAafIDDPAWLLEGYPGHPGRQGRLYKTGdlvqynADGNL 7998
Cdd:PRK07638   316 VQVRICNEAGEEVQK-GEIGTVYVKSPQFFMGYIIGGVLARE--LNADGWMTVRDVGYEDEEGFIYIVG------REKNM 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7999 VYLGrkdsqvkvrGQRVELGEVEHHVREClPEARQLAVevilpsgqknhamlavfvqLGKgthiahlEEKAGGEDSMAqV 8078
Cdd:PRK07638   387 ILFG---------GINIFPEEIESVLHEH-PAVDEIVV-------------------IGV-------PDSYWGEKPVA-I 429
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 8079 VFLTGTEEELA----KRLPKHMVPTVFFALLHFPMTTSGKADRKRLREI 8123
Cdd:PRK07638   430 IKGSATKQQLKsfclQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSW 478
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
1939-2442 1.36e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 65.02  E-value: 1.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKAR-PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 2017
Cdd:PRK13383    44 TAARwPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2018 HEDIFRQTGAQVVVTSAQHSARWIGTNHQVVTVSAGSleqfstlVNPVDLPAKPENAA---YVMFTSGSTGTPKGV---- 2090
Cdd:PRK13383   124 LAAALRAHHISTVVADNEFAERIAGADDAVAVIDPAT-------AGAEESGGRPAVAApgrIVLLTSGTTGKPKGVprap 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2091 -----------VLEH-------RAVVTSCLGHGQAFGVTNLLRALQFTAYT---FDVCIAEIITTLvhggcicvpsdsER 2149
Cdd:PRK13383   197 qlrsavgvwvtILDRtrlrtgsRISVAMPMFHGLGLGMLMLTIALGGTVLThrhFDAEAALAQASL------------HR 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2150 RDNLAkAITDMqvnwgyltssVARLLD-PCLV------PSLKVLVLGGEQVNSTDWGKWPSSVQTI--NGYGPTEccvfc 2220
Cdd:PRK13383   265 ADAFT-AVPVV----------LARILElPPRVrarnplPQLRVVMSSGDRLDPTLGQRFMDTYGDIlyNGYGSTE----- 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2221 tgyTGIqgfqsGNIGTSIASVSWvvdPENHGRLA-------------PLGS--IGELLVEGPILARGYLNDVDKtqaAFI 2285
Cdd:PRK13383   329 ---VGI-----GALATPADLRDA---PETVGKPVagcpvrildrnnrPVGPrvTGRIFVGGELAGTRYTDGGGK---AVV 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2286 DDPAwllegypghegrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMrKCLPEANQLAVEVVPpsG 2365
Cdd:PRK13383   395 DGMT-----------------STGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENAL-AAHPAVADNAVIGVP--D 454
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 2366 ERDHAMLAAFIrlddetrnsplIIKYAEDNSTAQivfltgIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRL 2442
Cdd:PRK13383   455 ERFGHRLAAFV-----------VLHPGSGVDAAQ------LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
PRK09192 PRK09192
fatty acyl-AMP ligase;
878-1027 1.39e-09

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 65.41  E-value: 1.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQvvLTSS 957
Cdd:PRK09192    50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIAQLRGM--LASA 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  958 QHAMLFASSERHQVTVSKVSTSQLPTVVNFAK-----------SPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLG 1026
Cdd:PRK09192   128 QPAAIITPDELLPWVNEATHGNPLLHVLSHAWfkalpeadvalPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRA 207

                   .
gi 1820002560 1027 H 1027
Cdd:PRK09192   208 I 208
PRK07867 PRK07867
acyl-CoA synthetase; Validated
910-1365 1.45e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 65.09  E-value: 1.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  910 EKSMWTVVAMLAvlkaGGAFVPLDPghpASRHEEIFKQIG---AQVVLTSSQHAMLFASSE---RHQVTVSKVSTSQL-- 981
Cdd:PRK07867    66 EFSLLLGAAALS----GIVPVGLNP---TRRGAALARDIAhadCQLVLTESAHAELLDGLDpgvRVINVDSPAWADELaa 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  982 PTVVNFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYT-DHARVLQFASYTFDACIAEIITTLLY 1060
Cdd:PRK07867   139 HRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGpDDVCYVSMPLFHSNAVMAGWAVALAA 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1061 GGCICVP---SESD-----RR------NNLAKAISTMdvncaLLTPSvarllEPSAVPSLKRLVLqGEQVSFADWNRWPG 1126
Cdd:PRK07867   219 GASIALRrkfSASGflpdvRRygatyaNYVGKPLSYV-----LATPE-----RPDDADNPLRIVY-GNEGAPGDIARFAR 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1127 --SVQTINGYGPTECSVccnTYSGKQGFKSGIIGTSVASLSwVVDA-----------GNHNRLAPLGSIGELL-VEGPIL 1192
Cdd:PRK07867   288 rfGCVVVDGFGSTEGGV---AITRTPDTPPGALGPLPPGVA-IVDPdtgtecppaedADGRLLNADEAIGELVnTAGPGG 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1193 ARGYLNDIDKTEAAfiddpawllegyeghagRRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREc 1272
Cdd:PRK07867   364 FEGYYNDPEADAER-----------------MRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLR- 425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1273 LPEARQLAVEVIlPSGQKEHALLAAfIQLDKGnhnALFEEKASGEdsmaqvvFLTGvEEELAKRlpehMVPTILFTVKAM 1352
Cdd:PRK07867   426 YPDATEVAVYAV-PDPVVGDQVMAA-LVLAPG---AKFDPDAFAE-------FLAA-QPDLGPK----QWPSYVRVCAEL 488
                          490
                   ....*....|...
gi 1820002560 1353 PITTSGKIDRKRL 1365
Cdd:PRK07867   489 PRTATFKVLKRQL 501
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
8251-8648 1.50e-09

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 65.65  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8251 PSLRIDDITDVVPASYIQQFYIATGVRAPREAFNYPFIDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIPR 8330
Cdd:COG1020      9 LPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8331 HQDLPFSI------FEVNGALAEESQAIHIRDLDQTSPLGLPTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLAS 8404
Cdd:COG1020     89 VVAAPLPVvvllvdLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLR 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8405 IYQQEPLLSTTG----FHSYLAYVHNQR--------SASINYWSRLLKGSHitniTSKLRPKLGKDTTIRSVKVERVIRT 8472
Cdd:COG1020    169 LYLAAYAGAPLPlpplPIQYADYALWQRewlqgeelARQLAYWRQQLAGLP----PLLELPTDRPRPAVQSYRGARVSFR 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8473 pqLP-------------TGLTMASLVSSAWAVVLSHISGEEDVVYGLVVAGRN---------------------SDLPSI 8518
Cdd:COG1020    245 --LPaeltaalralarrHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPrpeleglvgffvntlplrvdlSGDPSF 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8519 TEV--SVQDQYISLGESDSIGLDDIVQHCTdwPAKSE-----FDSIIQHQNiEEQPEIQFAGETTKLQWFKNSFAVSrQL 8591
Cdd:COG1020    323 AELlaRVRETLLAAYAHQDLPFERLVEELQ--PERDLsrnplFQVMFVLQN-APADELELPGLTLEPLELDSGTAKF-DL 398
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 8592 FVFSHPRGNSLTITITGNTGILTDQCAEKLLVMLCDTISQLSDSLDTPLAACKLLLP 8648
Cdd:COG1020    399 TLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTA 455
PRK07638 PRK07638
acyl-CoA synthetase; Validated
4545-5057 1.56e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 64.80  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4545 DQFAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDmVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPD 4624
Cdd:PRK07638     5 KEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4625 -HPASRHEHIFRQTGAQVVLASAQYATLWTSLGRsvVIVSEASTSQLPVVTKTADPSVNPGNAA-YAIFTSGSTGIPKGV 4702
Cdd:PRK07638    84 wKQDELKERLAISNADMIVTERYKLNDLPDEEGR--VIEIDEWKRMIEKYLPTYAPIENVQNAPfYMGFTSGSTGKPKAF 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4703 VLEHKAVVTS--CLGHgqAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVpsdsDRRNNLAKAINAMDVNWALLT 4780
Cdd:PRK07638   162 LRAQQSWLHSfdCNVH--DFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHL----MRKFIPNQVLDKLETENISVM 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4781 PSVARMLDPCVV------QSLKILVLGgeqvnsADWDRWPK-SIQTINA-------YGPTECSICCTTYSGKQGFKSGTI 4846
Cdd:PRK07638   236 YTVPTMLESLYKenrvieNKMKIISSG------AKWEAEAKeKIKNIFPyaklyefYGASELSFVTALVDEESERRPNSV 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4847 GTSIVSVSWVVDPENHNRLAPlGSIGELLVEGPILARGYLNDMEKTEAafIDDPAWLlegygghsgrqgrlyKTGDLVRY 4926
Cdd:PRK07638   310 GRPFHNVQVRICNEAGEEVQK-GEIGTVYVKSPQFFMGYIIGGVLARE--LNADGWM---------------TVRDVGYE 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4927 DADGNLVYLGRKDSQVKLRGQRVELGEVEHHVRECltEAKQLAVEVIVPEGEGGYAMLAafVQLGDDTYNTLVKekaggd 5006
Cdd:PRK07638   372 DEEGFIYIVGREKNMILFGGINIFPEEIESVLHEH--PAVDEIVVIGVPDSYWGEKPVA--IIKGSATKQQLKS------ 441
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 5007 sltvqvvfldRVEEELAK-RVPEHMMLTtfftlEAMPTTTSGKIDRKRLREI 5057
Cdd:PRK07638   442 ----------FCLQRLSSfKIPKEWHFV-----DEIPYTNSGKIARMEAKSW 478
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
6727-6808 1.62e-09

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 64.93  E-value: 1.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6727 ELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHPASRHEDI---LRQTGAQVI 6803
Cdd:cd05911     10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAA---NPIYTADELahqLKISKPKVI 86

                   ....*
gi 1820002560 6804 LASAQ 6808
Cdd:cd05911     87 FTDPD 91
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
878-1266 1.88e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 64.92  E-value: 1.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpgHPASRHEEIFKQI---GAQVVL 954
Cdd:PRK04319    74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPL---FEAFMEEAVRDRLedsEAKVLI 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  955 TSsqhAMLFA-------SSERHQVTVSKVSTSQlPTVVNFAK-----------SPVDPGNTAYIIFTSGTTGIPKGVVLQ 1016
Cdd:PRK04319   151 TT---PALLErkpaddlPSLKHVLLVGEDVEEG-PGTLDFNAlmeqasdefdiEWTDREDGAILHYTSGSTGKPKGVLHV 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1017 HRAVTTsclghgeafgytdHarvLQFASYTFDA-------CIAE----------IITTLLYGGCICVPSESDRRNNLAKA 1079
Cdd:PRK04319   227 HNAMLQ-------------H---YQTGKYVLDLheddvywCTADpgwvtgtsygIFAPWLNGATNVIDGGRFSPERWYRI 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1080 ISTMDVNCALLTPSVARLL-----EPSA---VPSLkRLVLQ-GEQVsfadwN----RWPGSV----------QTingygP 1136
Cdd:PRK04319   291 LEDYKVTVWYTAPTAIRMLmgagdDLVKkydLSSL-RHILSvGEPL-----NpevvRWGMKVfglpihdnwwMT-----E 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1137 TECSVCCNTYSgkQGFKSGIIGTSVASlswvVDAG----NHNRLAPlGSIGEL-LVEG-PILARGYLNDIDKTEAAFIDD 1210
Cdd:PRK04319   360 TGGIMIANYPA--MDIKPGSMGKPLPG----IEAAivddQGNELPP-NRMGNLaIKKGwPSMMRGIWNNPEKYESYFAGD 432
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 1211 paWllegyeghagrrgrlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIE 1266
Cdd:PRK04319   433 --W---------------YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE 471
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
5770-6129 1.95e-09

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 63.67  E-value: 1.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 IMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQ----FASYTFDAcmdEIITTLMYGGCIcVPSDSDRRND 5845
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIinpfFHTFGYKA---GIVACLLTGATV-VPVAVFDVDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5846 LVKAISTMDVSCALLTPSV--ARLLEPS----SVPTLQMLVLQGEQVSFADWNRWPA--SVQTI-NGYGPTECSicCNTY 5916
Cdd:cd17638     81 ILEAIERERITVLPGPPTLfqSLLDHPGrkkfDLSSLRAAVTGAATVPVELVRRMRSelGFETVlTAYGLTEAG--VATM 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5917 SgkqgfKSGIIGTSVASVSWVVDPENHDRLAplgSIGELLVEGPILARGYLNDIQKTAAVfIDDPAWLlegypghpgrqg 5996
Cdd:cd17638    159 C-----RPGDDAETVATTCGRACPGFEVRIA---DDGEVLVRGYNVMQGYLDDPEATAEA-IDADGWL------------ 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5997 rlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAVevilpSGQKDHAMLA---AFVQLEE 6073
Cdd:cd17638    218 ---HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAE-HPGVAQVAV-----IGVPDERMGEvgkAFVVARP 288
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6074 GTQnalLDKEAsgedsmaqvvFLASVEEELAKrlpeHMVPTVFFSLLHFPTTTSGK 6129
Cdd:cd17638    289 GVT---LTEED----------VIAWCRERLAN----YKVPRFVRFLDELPRNASGK 327
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
7617-7986 2.11e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 64.33  E-value: 2.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPA-ICAWDGE-LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 7694
Cdd:PRK13391     7 AQTTPDKPAvIMASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7695 RHEEIFEQTGAQVVVASAQYSArwtssschvvtVSKALSSQLPAV-----VDSTNTSVRPEN-----AAY---------- 7754
Cdd:PRK13391    87 EAAYIVDDSGARALITSAAKLD-----------VARALLKQCPGVrhrlvLDGDGELEGFVGyaeavAGLpatpiadesl 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7755 ---IIFTSGSTGVPKGVV--LEHRAVATSC----LGHgRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDS 7825
Cdd:PRK13391   156 gtdMLYSSGTTGRPKGIKrpLPEQPPDTPLpltaFLQ-RLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHF 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7826 DRRNSLAkAISTMDVNWAFLTPSV-ARLL-------DPGLIPSLKIlAIGGEQSSSADWNR----WPGSVqkIH-VYGPT 7892
Cdd:PRK13391   235 DAEQYLA-LIEEYGVTHTQLVPTMfSRMLklpeevrDKYDLSSLEV-AIHAAAPCPPQVKEqmidWWGPI--IHeYYAAT 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7893 ECCIFcTGYTTKQGFE-PSTIGTSVASVSWVVDPenHNRLAPLGSMGELLMEGPILARgYLNDVDKTEAAFIDDPAWLLE 7971
Cdd:PRK13391   311 EGLGF-TACDSEEWLAhPGTVGRAMFGDLHILDD--DGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGTWSTV 386
                          410
                   ....*....|....*
gi 1820002560 7972 GYPGHPGRQGRLYKT 7986
Cdd:PRK13391   387 GDIGYVDEDGYLYLT 401
PRK07529 PRK07529
AMP-binding domain protein; Validated
1908-2327 2.22e-09

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 64.59  E-value: 2.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1908 TTPEDRQQLwawnQEVPPA---IERCVHDLFTEQAKARPHAPAIC------AWDG--ELTYGELDALSSKLASHLVQLGV 1976
Cdd:PRK07529     5 ATLADIEAI----EAVPLAardLPASTYELLSRAAARHPDAPALSflldadPLDRpeTWTYAELLADVTRTANLLHSLGV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1977 NPEDVV----PLCFEksmwTVVAMLAVLKAGGAFvP----LDPDHPASrhedIFRQTGAQVVVTSA--------QHSARW 2040
Cdd:PRK07529    81 GPGDVVafllPNLPE----THFALWGGEAAGIAN-PinplLEPEQIAE----LLRAAGAKVLVTLGpfpgtdiwQKVAEV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2041 IGTNHQVVTV-----------------------SAGSLEQFSTLVN--PVDL-----PAKPENAAYVMFTSGSTGTPKGV 2090
Cdd:PRK07529   152 LAALPELRTVvevdlarylpgpkrlavplirrkAHARILDFDAELArqPGDRlfsgrPIGPDDVAAYFHTGGTTGMPKLA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2091 VLEHRAVVTSCLGHGQAFGVT---NLLRALQFtaytFDV--CIAEIITTLVHGGCICVPSDSERRD-----NLAKAITDM 2160
Cdd:PRK07529   232 QHTHGNEVANAWLGALLLGLGpgdTVFCGLPL----FHVnaLLVTGLAPLARGAHVVLATPQGYRGpgviaNFWKIVERY 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2161 QVNwgYLtSSV----ARLLDpclVP-------SLKVLVLGG-----------EQVnstdwgkwpSSVQTINGYGPTEC-C 2217
Cdd:PRK07529   308 RIN--FL-SGVptvyAALLQ---VPvdghdisSLRYALCGAaplpvevfrrfEAA---------TGVRIVEGYGLTEAtC 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2218 VFCTGYTGiQGFQSGNIG-----TSIASVswVVDPENHG-RLAPLGSIGELLVEGPILARGYLNDvDKTQAAFIDDpAWL 2291
Cdd:PRK07529   373 VSSVNPPD-GERRIGSVGlrlpyQRVRVV--ILDDAGRYlRDCAVDEVGVLCIAGPNVFSGYLEA-AHNKGLWLED-GWL 447
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1820002560 2292 legypghegrqgrlyKTGDLVRYSSDGNLVCLGR-KD 2327
Cdd:PRK07529   448 ---------------NTGDLGRIDADGYFWLTGRaKD 469
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
9-285 2.30e-09

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 63.94  E-value: 2.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    9 TPSVARLLE-----PSHIPSLRILVMGGEQVnsadwdrwPSSV----QTING------YGPTECCIVCTGYTS-EQDFTT 72
Cdd:cd05903    190 TPFLTDLLNaveeaGEPLSRLRTFVCGGATV--------PRSLarraAELLGakvcsaYGSTECPGAVTSITPaPEDRRL 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   73 GTIGTSIASVSW-VVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinnpawllegHGGYagrqgrlYKTGD 151
Cdd:cd05903    262 YTDGRPLPGVEIkVVD--DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA----------PEGW-------FRTGD 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  152 LVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECL---PEAKQLAVeVVLP---LGQKnhatLAAFIQLDKGthn 225
Cdd:cd05903    323 LARLDEDGYLRITGRSKDIIIRGGENIPVLEVE----DLLlghPGVIEAAV-VALPderLGER----ACAVVVTKSG--- 390
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  226 allkekvggddsiARVVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:cd05903    391 -------------ALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4567-5056 2.32e-09

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 64.13  E-value: 2.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVP----LDPDHPASRHEhifrqtgaqvv 4642
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRVD----------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4643 lasaqyatlwtsLGRSVVIVSEAstsqlpvVTKTADPSVnpgnaayAIFTSGSTGIPKGVVLEHkavVTSCLGHGQAF-- 4720
Cdd:cd05974     70 ------------RGGAVYAAVDE-------NTHADDPML-------LYFTSGTTSKPKLVEHTH---RSYPVGHLSTMyw 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4721 ---------------GITDHTRVLQFASYTFDACIAEIITTLLccgcicvpsDSDRrnnLAKAINAMDVNWALLTPSVAR 4785
Cdd:cd05974    121 iglkpgdvhwnisspGWAKHAWSCFFAPWNAGATVFLFNYARF---------DAKR---VLAALVRYGVTTLCAPPTVWR 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4786 MLDPCVVQSLKI----LVLGGEQVNSADWDR----WPKSIQtiNAYGPTEcSICCTTYSGKQGFKSGTIGTsivsvswvv 4857
Cdd:cd05974    189 MLIQQDLASFDVklreVVGAGEPLNPEVIEQvrraWGLTIR--DGYGQTE-TTALVGNSPGQPVKAGSMGR--------- 256
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4858 dPENHNRLAPLGSIGELLVEGPILArgylnDMEKTEaafiddPAWLLEGYGGHSGR-----QGRLYKTGDLVRYDADGNL 4932
Cdd:cd05974    257 -PLPGYRVALLDPDGAPATEGEVAL-----DLGDTR------PVGLMKGYAGDPDKtahamRGGYYRTGDIAMRDEDGYL 324
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4933 VYLGRKDSQVKLRGQRVELGEVEhhvrECLTEAKQLAVEVIVPEGEG-------GYAMLAAFVQLGDDTyntlvkekagg 5005
Cdd:cd05974    325 TYVGRADDVFKSSDYRISPFELE----SVLIEHPAVAEAAVVPSPDPvrlsvpkAFIVLRAGYEPSPET----------- 389
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 5006 dsltvQVVFLDRVEEELA--KRVPEhmmlttfFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:cd05974    390 -----ALEIFRFSRERLApyKRIRR-------LEFAELPKTISGKIRRVELRR 430
PRK06178 PRK06178
acyl-CoA synthetase; Validated
6686-6805 2.36e-09

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 64.68  E-value: 2.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6686 RQQLwAWNAELPLAV-----DRCVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVV----P 6756
Cdd:PRK06178    13 LQQA-AWPAGIPREPeyphgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVavflP 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 6757 LC--FeksmwtVVAMLAVLKAGGAFVPLDPdhPASRHEDI--LRQTGAQVILA 6805
Cdd:PRK06178    92 NCpqF------HIVFFGILKLGAVHVPVSP--LFREHELSyeLNDAGAEVLLA 136
PRK05850 PRK05850
acyl-CoA synthetase; Validated
854-1024 2.38e-09

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 64.58  E-value: 2.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  854 IHDLFAEQARARPDASAVC------AWDG---ELTYGELDELSSKLAAHLVQLGVKREDVVPLCfEKSMWTVVAMLAVLK 924
Cdd:PRK05850     3 VPSLLRERASLQPDDAAFTfidyeqDPAGvaeTLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGALQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  925 AGGAFVPLDPGHPASRHEEI---FKQIGAQVVLTSSQ---HAMLFASSERHQVT--VSKVSTSQLPTVVNFAKSPVDPGN 996
Cdd:PRK05850    82 AGLIAVPLSVPQGGAHDERVsavLRDTSPSVVLTTSAvvdDVTEYVAPQPGQSAppVIEVDLLDLDSPRGSDARPRDLPS 161
                          170       180
                   ....*....|....*....|....*...
gi 1820002560  997 TAYIIFTSGTTGIPKGVVLQHRAVTTSC 1024
Cdd:PRK05850   162 TAYLQYTSGSTRTPAGVMVSHRNVIANF 189
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
2075-2444 2.55e-09

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 63.12  E-value: 2.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2075 AYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLRALqftaytfdVCI--------AEIITTLVHGGCICVPsd 2146
Cdd:cd17630      3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL--------LSLplyhvgglAILVRSLLAGAELVLL-- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2147 sERRDNLAKAITDMQVNWgylTSSVA----RLLD----PCLVPSLKVLVLGGEQVNS------TDWGkWPssvqTINGYG 2212
Cdd:cd17630     73 -ERNQALAEDLAPPGVTH---VSLVPtqlqRLLDsgqgPAALKSLRAVLLGGAPIPPelleraADRG-IP----LYTTYG 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2213 PTEccvfctgytgiqgfQSGNIGTSIASVSW--VVDPENHGRLAPLGSIGELLVEGPILARGYLNDVDKTQAafiDDPAW 2290
Cdd:cd17630    144 MTE--------------TASQVATKRPDGFGrgGVGVLLPGRELRIVEDGEIWVGGASLAMGYLRGQLVPEF---NEDGW 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2291 llegypghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEhhmrKCL---PEANQLAVEVVPPS--G 2365
Cdd:cd17630    207 ---------------FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIE----AALaahPAVRDAFVVGVPDEelG 267
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 2366 ERdhamLAAFIRLDDETRNSPLIikyaednstaqivfltgieEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLRE 2444
Cdd:cd17630    268 QR----PVAVIVGRGPADPAELR-------------------AWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
2562-2750 2.55e-09

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 63.86  E-value: 2.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2562 TPIQHLYLTLDPSGRSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFQRQTG-GRWQQYISEHDSSSLivnHIH 2640
Cdd:cd19542      5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAeGTFLQVVLKSLDPPI---EEV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2641 TRDTTEIVEALRQS-RGSLDIERGPVLAAVLCDAGERQSLFVAIHHLVVDLVSWRILLEELEDLLLGQTLPPAlsTPFqa 2719
Cdd:cd19542     82 ETDEDSLDALTRDLlDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPA--PPF-- 157
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1820002560 2720 whAAQAKYIEEHVppsavaqvelDPDQLSYW 2750
Cdd:cd19542    158 --SDYISYLQSQS----------QEESLQYW 176
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
5764-6007 2.56e-09

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 64.45  E-value: 2.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5764 PENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITN----LSRVLQFASYTFDACMdeiITTLMYGGCICVPSD 5839
Cdd:PRK06334   182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEddvmMSFLPPFHAYGFNSCT---LFPLLSGVPVVFAYN 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5840 SDRRNDLVKAISTMDVSCALLTP-------SVARLLEpSSVPTLQMLVLQGEQVS---FADWNRWPASVQTINGYGPTEC 5909
Cdd:PRK06334   259 PLYPKKIVEMIDEAKVTFLGSTPvffdyilKTAKKQE-SCLPSLRFVVIGGDAFKdslYQEALKTFPHIQLRQGYGTTEC 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5910 S--ICCNTYSGKQgfKSGIIGTSVASVS-WVVDPENHdrlAPL--GSIGELLVEGPILARGYLNDIQKTAAVFIDDPAWL 5984
Cdd:PRK06334   338 SpvITINTVNSPK--HESCVGMPIRGMDvLIVSEETK---VPVssGETGLVLTRGTSLFSGYLGEDFGQGFVELGGETWY 412
                          250       260
                   ....*....|....*....|...
gi 1820002560 5985 LEGYPGHPGRQGRLYKTGDLVRY 6007
Cdd:PRK06334   413 VTGDLGYVDRHGELFLKGRLSRF 435
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
7590-8122 2.63e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 64.28  E-value: 2.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7590 DRQQLWAWNADVPPAIERCVHDL--FAEQARAR-PGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEK 7666
Cdd:PRK06710     4 EKPWLKSYPEEIPSTISYDIQPLhkYVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7667 SMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVV---------VASAQYSAR-------------------- 7717
Cdd:PRK06710    84 CPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlcldlvfprVTNVQSATKiehvivtriadflpfpknll 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7718 ----WTSSSCHVVTVSKALSSQL-PAVVDSTNTSVR----PEN-AAYIIFTSGSTGVPKGVVLEHRAVATSCLghgraFG 7787
Cdd:PRK06710   164 ypfvQKKQSNLVVKVSESETIHLwNSVEKEVNTGVEvpcdPENdLALLQYTGGTTGFPKGVMLTHKNLVSNTL-----MG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7788 ITNLSRVLQ-----------FASYTFDACIAeiiTTLLCGGCICVPSDSDRRnSLAKAISTMDVNWAFLTPSV-ARLLDP 7855
Cdd:PRK06710   239 VQWLYNCKEgeevvlgvlpfFHVYGMTAVMN---LSIMQGYKMVLIPKFDMK-MVFEAIKKHKVTLFPGAPTIyIALLNS 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7856 GLIPSLKILAIGGEQSSSADWnrwPGSVQK----------IHVYGPTECCIFCTGYTTKQGFEPSTIGtsvasVSW---- 7921
Cdd:PRK06710   315 PLLKEYDISSIRACISGSAPL---PVEVQEkfetvtggklVEGYGLTESSPVTHSNFLWEKRVPGSIG-----VPWpdte 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7922 --VVDPENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDdpAWLlegypghpgrqgrlyKTGDLVQYNADGNLV 7999
Cdd:PRK06710   387 amIMSLETGEALPP-GEIGEIVVKGPQIMKGYWNKPEETAAVLQD--GWL---------------HTGDVGYMDEDGFFY 448
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8000 YLGRKDSQVKVRGQRVELGEVEHHVREclPEARQLAVEVILPSGQKNHAMLAvFVQLGKGTHIahleekaggedsmaqvv 8079
Cdd:PRK06710   449 VKDRKKDMIVASGFNVYPREVEEVLYE--HEKVQEVVTIGVPDPYRGETVKA-FVVLKEGTEC----------------- 508
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 8080 fltgTEEEL----AKRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:PRK06710   509 ----SEEELnqfaRKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
1939-2444 2.87e-09

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 63.86  E-value: 2.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1939 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVplcfeksmwTVV-----AML----AVLKAGGAFVPL 2009
Cdd:cd12118     14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTV---------AVLapntpAMYelhfGVPMAGAVLNAL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2010 DPDHPASRHEDIFRQTGAQVVVTSAQHsarwigtnhqvvtvsagSLEQFSTLVNPVDLPAKPEN---AAYVMFTSGSTGT 2086
Cdd:cd12118     85 NTRLDAEEIAFILRHSEAKVLFVDREF-----------------EYEDLLAEGDPDFEWIPPADewdPIALNYTSGTTGR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2087 PKGVVLEHRAVVTSCLGHGQAFGVTNLLRAL----QFTA--YTFDVCIAEIITTLVhggCIcvpsdserRDNLAKAITDM 2160
Cdd:cd12118    148 PKGVVYHHRGAYLNALANILEWEMKQHPVYLwtlpMFHCngWCFPWTVAAVGGTNV---CL--------RKVDAKAIYDL 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2161 QVNWGyltssVARLldpCLVPSLKVLVLGG---------EQVNSTDWGKWPS-----SVQTING-----------YGPTE 2215
Cdd:cd12118    217 IEKHK-----VTHF---CGAPTVLNMLANAppsdarplpHRVHVMTAGAPPPaavlaKMEELGFdvthvygltetYGPAT 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2216 CCVFCTGYTGI-----------QGfqsgnIGTSIASVSWVVDPENHGRLAPLG-SIGELLVEGPILARGYLNDVDKTQAA 2283
Cdd:cd12118    289 VCAWKPEWDELpteerarlkarQG-----VRYVGLEEVDVLDPETMKPVPRDGkTIGEIVFRGNIVMKGYLKNPEATAEA 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2284 FIDdpAWllegypghegrqgrlYKTGDLVRYSSDGNLvclgrkdsQVKVR--------GQRVELGEVE----HHmrkclP 2351
Cdd:cd12118    364 FRG--GW---------------FHSGDLAVIHPDGYI--------EIKDRskdiiisgGENISSVEVEgvlyKH-----P 413
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2352 EANQLAVEVVPPS--GERDHamlaAFIRL-DDETRNSPLIIKYAEdnstaqivfltgieeelsERLPQHMVP-TVFFalV 2427
Cdd:cd12118    414 AVLEAAVVARPDEkwGEVPC----AFVELkEGAKVTEEEIIAFCR------------------EHLAGFMVPkTVVF--G 469
                          570
                   ....*....|....*..
gi 1820002560 2428 HFPTTTSGKTDRKRLRE 2444
Cdd:cd12118    470 ELPKTSTGKIQKFVLRD 486
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
831-1236 2.88e-09

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 64.13  E-value: 2.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  831 TTLEDRQQ--LWVWNADMPPAVDRCIHDLFAEQARARPDASAVC---AWDG--ELTYGELDELSSKLAAHLVQLGVKRED 903
Cdd:PRK08180    16 VEVERRADgtIYLRSAEPLGDYPRRLTDRLVHWAQEAPDRVFLAergADGGwrRLTYAEALERVRAIAQALLDRGLSAER 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  904 VVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP-----GHPASRHEEIFKQI-----------------------GAQVVLT 955
Cdd:PRK08180    96 PLMILSGNSIEHALLALAAMYAGVPYAPVSPayslvSQDFGKLRHVLELLtpglvfaddgaafaralaavvpaDVEVVAV 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  956 SSQHAmlfassERHQVTVSKVSTSQLPTVVNFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTD 1035
Cdd:PRK08180   176 RGAVP------GRAATPFAALLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLA 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1036 HAR--VLQFA--SYTFDAciAEIITTLLY-GGC--IC----VPSESDR--RNNlaKAIS-TMDVNC----ALLTPSV--- 1094
Cdd:PRK08180   250 EEPpvLVDWLpwNHTFGG--NHNLGIVLYnGGTlyIDdgkpTPGGFDEtlRNL--REISpTVYFNVpkgwEMLVPALerd 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1095 --------ARL---------LEPSAVPSLKRLVLQ--GEQVSFAdwnrwpgsvqtiNGYGPTECSVCCnTYSGKQGFKSG 1155
Cdd:PRK08180   326 aalrrrffSRLkllfyagaaLSQDVWDRLDRVAEAtcGERIRMM------------TGLGMTETAPSA-TFTTGPLSRAG 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1156 IIGTSVAslswvvdaGNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFiDDpawllEGYeghagrrgrlYKTGDLV 1235
Cdd:PRK08180   393 NIGLPAP--------GCEVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAF-DE-----EGY----------YRSGDAV 448

                   .
gi 1820002560 1236 R 1236
Cdd:PRK08180   449 R 449
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
23-286 2.94e-09

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 64.07  E-value: 2.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRWPS--SVQTINGYGPTECCIVCTGYTSEQDFTTGTIGTSIASVSW-VVDpkDHGRLAPLGS 99
Cdd:PRK12492   334 ALKLTNSGGTALVKATAERWEQltGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALkVID--DDGNELPLGE 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  100 VGELLVEGPILARGYLSDPEKTAAVfINNPAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVE 179
Cdd:PRK12492   412 RGELCIKGPQVMKGYWQQPEATAEA-LDAEGWF---------------KTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVY 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  180 LGEVEhhvreclpeakqlavEVVlpLGQKNHATLAAFIQLDKGTHNALLKEKVGGDDSIARVVFLAGVEEEL-AKRLPKH 258
Cdd:PRK12492   476 PNEIE---------------DVV--MAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFtGYKVPKH 538
                          250       260
                   ....*....|....*....|....*...
gi 1820002560  259 MVptVFFALlhfPTTTSGKTDRKRLREI 286
Cdd:PRK12492   539 IV--LRDSL---PMTPVGKILRRELRDI 561
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7748-8008 2.99e-09

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 64.02  E-value: 2.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7748 RPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQ----FAsyTFDACIAeiITTLLCGGCICVPS 7823
Cdd:cd05910     83 KADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLAtfplFA--LFGPALG--LTSVIPDMDPTRPA 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7824 DSDRRnSLAKAISTMDVNWAFLTPSVARLL-----DPGL-IPSLKILAIGGEQSSSADWNRW----PGSVQKIHVYGPTE 7893
Cdd:cd05910    159 RADPQ-KLVGAIRQYGVSIVFGSPALLERVarycaQHGItLPSLRRVLSAGAPVPIALAARLrkmlSDEAEILTPYGATE 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7894 CCIFC----------TGYTTKQGfEPSTIGTSVASVSWVV-------DPENHNRLA-PLGSMGELLMEGPILARGYLNDV 7955
Cdd:cd05910    238 ALPVSsigsrellatTTAATSGG-AGTCVGRPIPGVRVRIieiddepIAEWDDTLElPRGEIGEITVTGPTVTPTYVNRP 316
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 7956 DKTEAAFIDDPawllegypghpgRQGRLYKTGDLVQYNADGNLVYLGRKDSQV 8008
Cdd:cd05910    317 VATALAKIDDN------------SEGFWHRMGDLGYLDDEGRLWFCGRKAHRV 357
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
3451-3875 3.15e-09

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 64.07  E-value: 3.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3451 WN----ADVPPAIE----RCVHDLFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQ-LGVNPEDVVPLCFEKS 3521
Cdd:PRK12492     6 WNdkrpAGVPSTIDlaayKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3522 MWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARW----------------------TSSSCHV 3579
Cdd:PRK12492    86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVqevlpdtgieylieakmgdllpAAKGWLV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3580 VTVSKALSSQLP------------AVVDSTNTSVRP-----ENAAYIIFTSGSTGVPKGVVLEH-RAVAT-----SCLGH 3636
Cdd:PRK12492   166 NTVVDKVKKMVPayhlpqavpfkqALRQGRGLSLKPvpvglDDIAVLQYTGGTTGLAKGAMLTHgNLVANmlqvrACLSQ 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3637 GRAFG---ITNLSRVL-----QFASYTFDA-CIAEIIT---TLLcggcICVPSDSdrrNSLAKAIStmdvNWAFL----- 3699
Cdd:PRK12492   246 LGPDGqplMKEGQEVMiaplpLYHIYAFTAnCMCMMVSgnhNVL----ITNPRDI---PGFIKELG----KWRFSallgl 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3700 -TPSVARLLDPGL----IPSLKILAIGGEQSSSADWNRWPG--SVQKIHVYGPTECC-IFCT---GYTTKQGfepsTIGT 3768
Cdd:PRK12492   315 nTLFVALMDHPGFkdldFSALKLTNSGGTALVKATAERWEQltGCTIVEGYGLTETSpVASTnpyGELARLG----TVGI 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3769 SVASVSWVVDPENHNRLaPLGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTGDLVQYNA 3848
Cdd:PRK12492   391 PVPGTALKVIDDDGNEL-PLGERGELCIKGPQVMKGYWQQPEATAEA-LDAEGWF---------------KTGDIAVIDP 453
                          490       500
                   ....*....|....*....|....*..
gi 1820002560 3849 DGNLVYLGRKDSQVKVRGQRVELGEVE 3875
Cdd:PRK12492   454 DGFVRIVDRKKDLIIVSGFNVYPNEIE 480
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
7-286 3.15e-09

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 63.68  E-value: 3.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    7 LLTPSVARLLEPSHIPSLRILVMGGEQVNSaDWDRWPSSVQTI---NGYGPTEC-CIVCTGYTSeQDFTTGTIGTSIASV 82
Cdd:cd05969    192 MLMKEGDELARKYDLSSLRFIHSVGEPLNP-EAIRWGMEVFGVpihDTWWQTETgSIMIANYPC-MPIKPGSMGKPLPGV 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   83 -SWVVDpkDHGRLAPLGSVGELLVEG--PILARGYLSDPEKTAAVFINnpawlleghgGYagrqgrlYKTGDLVRYDADG 159
Cdd:cd05969    270 kAAVVD--ENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFID----------GW-------YLTGDLAYRDEDG 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  160 NLVCLGRKDSQVKLRGQRVELGEVEHHVRE--CLPEAKQLAVEVVLpLGQKnhatLAAFIQLDKG-THNALLKEKVGGdd 236
Cdd:cd05969    331 YFWFVGRADDIIKTSGHRVGPFEVESALMEhpAVAEAGVIGKPDPL-RGEI----IKAFISLKEGfEPSDELKEEIIN-- 403
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560  237 sIARVVFLAGV---EEELAKRLPKhmvptvffallhfptTTSGKTDRKRLREI 286
Cdd:cd05969    404 -FVRQKLGAHVaprEIEFVDNLPK---------------TRSGKIMRRVLKAK 440
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
1000-1367 3.16e-09

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 64.02  E-value: 3.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1000 IIFTSGTTGIPKgvVLQHravTTSCLGHGEAFG---YTD--HARVLQFASYT--FDACIAEIITTLLYGGCICVPSESD- 1071
Cdd:cd05928    179 IYFTSGTTGSPK--MAEH---SHSSLGLGLKVNgryWLDltASDIMWNTSDTgwIKSAWSSLFEPWIQGACVFVHHLPRf 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1072 RRNNLAKAISTMDVNCALLTPSVARLLEPSAV-----PSLKRLVLQGEQVSFADWNRWpgSVQT----INGYGPTECSVC 1142
Cdd:cd05928    254 DPLVILKTLSSYPITTFCGAPTVYRMLVQQDLssykfPSLQHCVTGGEPLNPEVLEKW--KAQTgldiYEGYGQTETGLI 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1143 CNTYSGKQgFKSGIIGTsvASLSWVV----DAGNhnrLAPLGSIGELLVE-GPI----LARGYLNDIDKTEAAFiddpaw 1213
Cdd:cd05928    332 CANFKGMK-IKPGSMGK--ASPPYDVqiidDNGN---VLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATI------ 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1214 llegyeghagrRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREcLPEARQLAVeVILPSgQKEHA 1293
Cdd:cd05928    400 -----------RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIE-HPAVVESAV-VSSPD-PIRGE 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1294 LLAAFIQLDKGnhnalfeekasgedsmaqvvFLTGVEEELAKRLPEHM--------VPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:cd05928    466 VVKAFVVLAPQ--------------------FLSHDPEQLTKELQQHVksvtapykYPRKVEFVQELPKTVTGKIQRNEL 525

                   ..
gi 1820002560 1366 QD 1367
Cdd:cd05928    526 RD 527
PRK07514 PRK07514
malonyl-CoA synthase; Validated
6712-6782 3.17e-09

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 63.74  E-value: 3.17e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 6712 ALARPNAPAVCAWDGE-LTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL 6782
Cdd:PRK07514    12 AFADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
21-284 3.23e-09

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 63.65  E-value: 3.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   21 IPSLRILVMGGEQVNSADWDRWPSS--VQTINGYGPTECCIVctgYTS--EQDFTTGTIGTSIASVSW-VVDpkDHGRLA 95
Cdd:cd05958    212 LSSLRKCVSAGEALPAALHRAWKEAtgIPIIDGIGSTEMFHI---FISarPGDARPGATGKPVPGYEAkVVD--DEGNPV 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   96 PLGSVGELLVEGPIlarGYLSDPEKTAAVFINNpAWLLeghggyagrqgrlykTGDLVRYDADGNLVCLGRKDSQVKLRG 175
Cdd:cd05958    287 PDGTIGRLAVRGPT---GCRYLADKRQRTYVQG-GWNI---------------TGDTYSRDPDGYFRHQGRSDDMIVSGG 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  176 QRVELGEVEhhvrECL---PEAKQLAVevvlpLGQKNHATLA---AFIqldkgthnaLLKEKVGGDDSIARVVflagveE 249
Cdd:cd05958    348 YNIAPPEVE----DVLlqhPAVAECAV-----VGHPDESRGVvvkAFV---------VLRPGVIPGPVLAREL------Q 403
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1820002560  250 ELAKR-LPKHMVPTVFFALLHFPTTTSGKTDRKRLR 284
Cdd:cd05958    404 DHAKAhIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
PRK05850 PRK05850
acyl-CoA synthetase; Validated
4548-4713 3.24e-09

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 64.19  E-value: 3.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4548 AEQARARPDTPAIC------AWDG---ELTYGELDTLSSKLASHLVQLGVkPEDMVPLCFEKSMWTVVAMLAVLKAGGAF 4618
Cdd:PRK05850     8 RERASLQPDDAAFTfidyeqDPAGvaeTLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGLIA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4619 VPLDPDHPASRHEHI---FRQTGAQVVLASAQYA-----TLWTSLGRSVVIVSEASTSQLPVVTKTADPSVNPGNAAYAI 4690
Cdd:PRK05850    87 VPLSVPQGGAHDERVsavLRDTSPSVVLTTSAVVddvteYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPRDLPSTAYLQ 166
                          170       180
                   ....*....|....*....|...
gi 1820002560 4691 FTSGSTGIPKGVVLEHKAVVTSC 4713
Cdd:PRK05850   167 YTSGSTRTPAGVMVSHRNVIANF 189
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
988-1361 3.47e-09

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 64.35  E-value: 3.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  988 AKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTT------------------SCLGHGEAFGYT--------DHARVLQ 1041
Cdd:PRK08043   358 AQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLAnveqiktiadftpndrfmSALPLFHSFGLTvglftpllTGAEVFL 437
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1042 FAS---YtfdaciaEIITTLLYggcicvpsesDRRNNLAKAISTMDVNCAlltpsvaRLLEPSAVPSLKRLVLQGEQVSF 1118
Cdd:PRK08043   438 YPSplhY-------RIVPELVY----------DRNCTVLFGTSTFLGNYA-------RFANPYDFARLRYVVAGAEKLQE 493
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1119 ADWNRWPGS--VQTINGYGPTECS--VCCNTysgKQGFKSGIIGTsvaslswvVDAGNHNRLAPLGSI---GELLVEGPI 1191
Cdd:PRK08043   494 STKQLWQDKfgLRILEGYGVTECApvVSINV---PMAAKPGTVGR--------ILPGMDARLLSVPGIeqgGRLQLKGPN 562
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1192 LARGYLNdidkteaafIDDPAwLLE---GYEGHAGRRGRLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhh 1268
Cdd:PRK08043   563 IMNGYLR---------VEKPG-VLEvptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE-- 630
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1269 vreclpearQLAVEVilpSGQKEHallAAFIQLD--KGNHNALFEEKAS-GEDSMAQVVFLTGVeeelakrlPEHMVPTI 1345
Cdd:PRK08043   631 ---------QLALGV---SPDKQH---ATAIKSDasKGEALVLFTTDSElTREKLQQYAREHGV--------PELAVPRD 687
                          410
                   ....*....|....*.
gi 1820002560 1346 LFTVKAMPITTSGKID 1361
Cdd:PRK08043   688 IRYLKQLPLLGSGKPD 703
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
15-285 3.64e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 63.90  E-value: 3.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   15 LLEPSHIPSLRILVMGGEQVNSADWDRWPSSV--QTINGYGPTECCIVCTGYTSEQDFTTGTIGTSIASVSWVVDPKDHG 92
Cdd:PRK06710   316 LLKEYDISSIRACISGSAPLPVEVQEKFETVTggKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETG 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   93 RLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinNPAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVK 172
Cdd:PRK06710   396 EALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL--QDGWL---------------HTGDVGYMDEDGFFYVKDRKKDMIV 458
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  173 LRGQRVELGEVEHHVREclPEAKQLAVEVVLPLGQKNHaTLAAFIQLDKGTHNAllKEKVggdDSIARvvflagveeela 252
Cdd:PRK06710   459 ASGFNVYPREVEEVLYE--HEKVQEVVTIGVPDPYRGE-TVKAFVVLKEGTECS--EEEL---NQFAR------------ 518
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1820002560  253 KRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:PRK06710   519 KYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
6701-6808 3.65e-09

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 63.63  E-value: 3.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6701 DRCVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVV----PLCFEksmwTVVAMLAVLKAG 6776
Cdd:COG1021     24 GETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVvvqlPNVAE----FVIVFFALFRAG 99
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1820002560 6777 GAFVPLDPDHPASRHEDILRQTGAQVILASAQ 6808
Cdd:COG1021    100 AIPVFALPAHRRAEISHFAEQSEAVAYIIPDR 131
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
7754-8117 3.94e-09

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 62.42  E-value: 3.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7754 YIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAK 7833
Cdd:cd17633      4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7834 aISTMDVNWAFLTPSVARLLDPGLIPSLKILAIggeqSSSADwnRWPGSVQKihvygpteccifctgyTTKQGFEPSTI- 7912
Cdd:cd17633     84 -INQYNATVIYLVPTMLQALARTLEPESKIKSI----FSSGQ--KLFESTKK----------------KLKNIFPKANLi 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7913 ---GTSVAS-VSWVVDPEnhnrLAPLGSMGELLMEGPILARGYLNDVD-----KTEAAFiddpawllEGYPGHPGRQ-GR 7982
Cdd:cd17633    141 efyGTSELSfITYNFNQE----SRPPNSVGRPFPNVEIEIRNADGGEIgkifvKSEMVF--------SGYVRGGFSNpDG 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7983 LYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClpEARQLAVEVILPSGQKNHamLAVFVQLGKGTHI 8062
Cdd:cd17633    209 WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAI--PGIEEAIVVGIPDARFGE--IAVALYSGDKLTY 284
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 8063 AHLEEKaggedsmaqvvfltgteeeLAKRLPKHMVPTVFFALLHFPMTTSGKADR 8117
Cdd:cd17633    285 KQLKRF-------------------LKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
1947-2090 4.07e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 63.38  E-value: 4.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1947 AICAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQT 2025
Cdd:PRK08276     3 VIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 2026 GAQVVVTSA------QHSARWIGTNHQVVTVSAGSLEQFSTLVNPVDL-PAKP---ENAAYVM-FTSGSTGTPKGV 2090
Cdd:PRK08276    83 GAKVLIVSAaladtaAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAqPDTPiadETAGADMlYSSGTTGRPKGI 158
PRK08315 PRK08315
AMP-binding domain protein; Validated
5617-6141 4.45e-09

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 63.68  E-value: 4.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5617 PPAIERCVHDLFTEQAKARPHAPAICAWDGEL--TYGELDALSSKLAGHLTQLGVKPEDMV----PLCFEksmWTVVaML 5690
Cdd:PRK08315    11 VPLLEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVgiwaPNVPE---WVLT-QF 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5691 AVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSAQ-------------------------HSAR--------WIGTN 5737
Cdd:PRK08315    87 ATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamlyelapelatcepgqlQSARlpelrrviFLGDE 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5738 HQVVTVSAGSLGQLSTLVNPVGLPAI-----PENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVlqf 5812
Cdd:PRK08315   167 KHPGMLNFDELLALGRAVDDAELAARqatldPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRL--- 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5813 asytfdacmdeiittlmyggCICVPsdsdrrndL---------VKAISTmdVSCALLTPSVArlLEPSS----------- 5872
Cdd:PRK08315   244 --------------------CIPVP--------LyhcfgmvlgNLACVT--HGATMVYPGEG--FDPLAtlaaveeerct 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5873 ----VPTlqMLVLQGEQVSFADWN----R--------WPASVQ------------TInGYGPTECSiccntysgkqgfkS 5924
Cdd:PRK08315   292 alygVPT--MFIAELDHPDFARFDlsslRtgimagspCPIEVMkrvidkmhmsevTI-AYGMTETS-------------P 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5925 GIIGTSVAS-----VSWV-----------VDPENHDRLaPLGSIGELLVEGPILARGYLNDIQKTAAVfIDDPAWLlegy 5988
Cdd:PRK08315   356 VSTQTRTDDplekrVTTVgralphlevkiVDPETGETV-PRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDADGWM---- 429
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5989 pgHpgrqgrlykTGDLVRYDANGNLVCLGR-KDsqVKLRGqrvelG------EVE----HHvreclPEArqLAVEVI-LP 6056
Cdd:PRK08315   430 --H---------TGDLAVMDEEGYVNIVGRiKD--MIIRG-----GeniyprEIEeflyTH-----PKI--QDVQVVgVP 484
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6057 SgQKDHAMLAAFVQLEEGTqnalldkEASGEDsmaqvvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:PRK08315   485 D-EKYGEEVCAWIILRPGA-------TLTEED----------VRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546

                   ....*
gi 1820002560 6137 EIGAS 6141
Cdd:PRK08315   547 EMMIE 551
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
5617-6110 4.67e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 63.53  E-value: 4.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5617 PPAIERCVHDLFTEQAKARPHAPAIC-------AWDGeLTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAM 5689
Cdd:PRK12582    44 LGPYPRSIPHLLAKWAAEAPDRPWLAqrepghgQWRK-VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMT 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5690 LAVLKAGgafVPLDPDHPA----SRHEDTFRHTGAQVV--VTSAQHSARWIGTNH-------QVVTVSAGSLGQLST--- 5753
Cdd:PRK12582   123 LAAMQAG---VPAAPVSPAyslmSHDHAKLKHLFDLVKprVVFAQSGAPFARALAaldlldvTVVHVTGPGEGIASIafa 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5754 --LVNPVG------LPAI-PENAVYIMFTSGSTGIPKGVVLEHRAVVtscwgrgrafgiTNLSRVLQFASytfDACMDEI 5824
Cdd:PRK12582   200 dlAATPPTaavaaaIAAItPDTVAKYLFTSGSTGMPKAVINTQRMMC------------ANIAMQEQLRP---REPDPPP 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5825 ITTL-------MYGGCICVpsdsdrrNDLVKAISTMDVS-----CALLTPSVARLLEPS-----SVPT------------ 5875
Cdd:PRK12582   265 PVSLdwmpwnhTMGGNANF-------NGLLWGGGTLYIDdgkplPGMFEETIRNLREISptvygNVPAgyamlaeamekd 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5876 ----------LQMLVLQGEQVSFADWNRWPA-SVQTI-------NGYGPTECS-ICCNTYSGKQgfKSGIIGTSVASVSW 5936
Cdd:PRK12582   338 dalrrsffknLRLMAYGGATLSDDLYERMQAlAVRTTghripfyTGYGATETApTTTGTHWDTE--RVGLIGLPLPGVEL 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5937 vvdpenhdRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFiDDpawllEGYpghpgrqgrlYKTGDLVRY----DANGN 6012
Cdd:PRK12582   416 --------KLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAF-DE-----EGF----------YRLGDAARFvdpdDPEKG 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6013 LVCLGRKDSQVKL-RGQRVELGEVEHH-VRECLPEARQLAVevilpSGQ-KDHAMLAAFVQLeEGTQNALLDKEASGEDs 6089
Cdd:PRK12582   472 LIFDGRVAEDFKLsTGTWVSVGTLRPDaVAACSPVIHDAVV-----AGQdRAFIGLLAWPNP-AACRQLAGDPDAAPED- 544
                          570       580
                   ....*....|....*....|.
gi 1820002560 6090 maqVVFLASVEEELAKRLPEH 6110
Cdd:PRK12582   545 ---VVKHPAVLAILREGLSAH 562
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
84-292 5.05e-09

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 63.47  E-value: 5.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   84 WVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNpawlleghgGYagrqgrlYKTGDLVRYDADGNLVC 163
Cdd:PRK10946   366 WVAD--ADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDAN---------GF-------YCSGDLVSIDPDGYITV 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  164 LGRKDSQVKLRGQRVELGEVEHHVreclpeakqLAVEVVLplgqknHATLAAFiqldkgtHNALLKEKvggddSIARVVf 243
Cdd:PRK10946   428 VGREKDQINRGGEKIAAEEIENLL---------LRHPAVI------HAALVSM-------EDELMGEK-----SCAFLV- 479
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560  244 lagVEEEL-AKRLPKHM---------VPTVFFALLHFPTTTSGKTDRKRLREIGASFTA 292
Cdd:PRK10946   480 ---VKEPLkAVQLRRFLreqgiaefkLPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
2067-2358 5.49e-09

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 63.58  E-value: 5.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2067 LPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVT------------------SCLGHGQAFGVT-NLLRALQFTAYTFdvc 2127
Cdd:PRK08043   360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSLLAnveqiktiadftpndrfmSALPLFHSFGLTvGLFTPLLTGAEVF--- 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2128 iaeiittlvhggciCVPSDSERRdNLAKAITDMQVNWGYLTSSV----ARLLDPCLVPSLKVLVLGGEQVNSTDWGKWPS 2203
Cdd:PRK08043   437 --------------LYPSPLHYR-IVPELVYDRNCTVLFGTSTFlgnyARFANPYDFARLRYVVAGAEKLQESTKQLWQD 501
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2204 S--VQTINGYGPTECCVFCTgytgiqgfqsgnIGTSIASVSWVVD---PENHGRLAPLGSI---GELLVEGPILARGYLN 2275
Cdd:PRK08043   502 KfgLRILEGYGVTECAPVVS------------INVPMAAKPGTVGrilPGMDARLLSVPGIeqgGRLQLKGPNIMNGYLR 569
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2276 dvdktqaafIDDPAwLLEGyPGHEGRQGRL----YKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKCLP 2351
Cdd:PRK08043   570 ---------VEKPG-VLEV-PTAENARGEMergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSP 638

                   ....*..
gi 1820002560 2352 EANQLAV 2358
Cdd:PRK08043   639 DKQHATA 645
PRK09274 PRK09274
peptide synthase; Provisional
1-178 5.49e-09

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 63.38  E-value: 5.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    1 MRVNWALLTPsVARLLEPSHI--PSLRILVMGGEQVNSADWDRW----PSSVQTINGYGPTECCIVCTGYTSEQDFTT-- 72
Cdd:PRK09274   266 LFGSPALLER-LGRYGEANGIklPSLRRVISAGAPVPIAVIERFramlPPDAEILTPYGATEALPISSIESREILFATra 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   73 ------GT-IGTSIASVSWVV-----DPKDH---GRLAPLGSVGELLVEGPILARGYLSDPEKTAAvfinnpAWLLEGHG 137
Cdd:PRK09274   345 atdngaGIcVGRPVDGVEVRIiaisdAPIPEwddALRLATGEIGEIVVAGPMVTRSYYNRPEATRL------AKIPDGQG 418
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1820002560  138 GYAGRqgrlykTGDLVRYDADGNLVCLGRKDSQVKLRGQRV 178
Cdd:PRK09274   419 DVWHR------MGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
4550-5055 5.51e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 63.10  E-value: 5.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4550 QARARPDTPA-ICAWDGE-LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPA 4627
Cdd:PRK13390     6 HAQIAPDRPAvIVAETGEqVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4628 SRHEHIFRQTGAQVVLASAQYATLWTSLGRSV-VIVS-----EASTSQLPVVTKTADPSVNPGNAAYAIFTSGSTGIPKG 4701
Cdd:PRK13390    86 PEADYIVGDSGARVLVASAALDGLAAKVGADLpLRLSfggeiDGFGSFEAALAGAGPRLTEQPCGAVMLYSSGTTGFPKG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4702 VVLEHKAVVTSCLGH------GQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLaKAINAMDVN 4775
Cdd:PRK13390   166 IQPDLPGRDVDAPGDpivaiaRAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQATL-GHVERYRIT 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4776 WALLTPSV-ARM--LDPCV-----VQSLKILVLGGE----QVNSADWDrWPKSIqTINAYGPTECSICCTTYSGKQGFKS 4843
Cdd:PRK13390   245 VTQMVPTMfVRLlkLDADVrtrydVSSLRAVIHAAApcpvDVKHAMID-WLGPI-VYEYYSSTEAHGMTFIDSPDWLAHP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4844 GTIGTSIVSVSWVVDPENHNrlAPLGSIGELLVEGPILARGYLNDMEKT-EAAFIDDPAWLlegygghsgrqgrlyKTGD 4922
Cdd:PRK13390   323 GSVGRSVLGDLHICDDDGNE--LPAGRIGTVYFERDRLPFRYLNDPEKTaAAQHPAHPFWT---------------TVGD 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4923 LVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVreCLTEAKQLAVEVIVPEGEGGyAMLAAFVQlgddtyntLVKEK 5002
Cdd:PRK13390   386 LGSVDEDGYLYLADRKSFMIISGGVNIYPQETENAL--TMHPAVHDVAVIGVPDPEMG-EQVKAVIQ--------LVEGI 454
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 5003 AGGDSLTVQVVFLDRveeelaKRVPEHMMLTTFFTLEAMPTTTSGKIDRKRLR 5055
Cdd:PRK13390   455 RGSDELARELIDYTR------SRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
6856-6980 5.82e-09

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 63.20  E-value: 5.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6856 GELLVEGPILARGYLNDADKTAAAFVNDpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVR-GQRVE 6934
Cdd:COG1022    415 GEILVRGPNVMKGYYKNPEATAEAFDAD-GWL---------------HTGDIGELDEDGFLRITGRKKDLIVTSgGKNVA 478
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 6935 LGEIENRLRECmPRATQ-MAVevispaGaaeQAKTMVVAFLQLNDEA 6980
Cdd:COG1022    479 PQPIENALKAS-PLIEQaVVV------G---DGRPFLAALIVPDFEA 515
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
4675-5050 5.89e-09

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 63.83  E-value: 5.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4675 KTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSClghGQAFGITDHTR------VLQ-FASYTFDAciAEIITTL 4747
Cdd:PRK06814   784 LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANR---AQVAARIDFSPedkvfnALPvFHSFGLTG--GLVLPLL 858
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4748 LCCGCICVPSDSDRRnnlakAINAM--DVNWALL--TPSV----ARMLDPCVVQSLKILVLGGEQVNSADWDRWPKS--I 4817
Cdd:PRK06814   859 SGVKVFLYPSPLHYR-----IIPELiyDTNATILfgTDTFlngyARYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKfgI 933
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4818 QTINAYGPTECS--ICCTTysgKQGFKSGTIGTSIvsvswvvdPENHNRLAPLGSI---GELLVEGPILARGYLndmeKT 4892
Cdd:PRK06814   934 RILEGYGVTETApvIALNT---PMHNKAGTVGRLL--------PGIEYRLEPVPGIdegGRLFVRGPNVMLGYL----RA 998
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4893 EAAFIDDPawLLEGYgghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVRECLTEAKQLAVEv 4972
Cdd:PRK06814   999 ENPGVLEP--PADGW----------YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVS- 1065
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 4973 iVPEGEGGYAMLaafvqlgddtyntLVKEKAGGDSLTVQVVFLDRVEEELAkrVPEHMMlttffTLEAMPTTTSGKID 5050
Cdd:PRK06814  1066 -IPDARKGERII-------------LLTTASDATRAAFLAHAKAAGASELM--VPAEII-----TIDEIPLLGTGKID 1122
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3027-3329 6.03e-09

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 62.86  E-value: 6.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3027 PM---QEGI--LTSQGKDPDAYWVCFIYEVipnqETSISLARLQQAWKGVVHQHSLLRTLLVDNvPGSTGTTNVVLKDPQ 3101
Cdd:cd19532      3 PMsfgQSRFwfLQQYLEDPTTFNVTFSYRL----TGPLDVARLERAVRAVGQRHEALRTCFFTD-PEDGEPMQGVLASSP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3102 PSISVFSSEGTAtielfrsrynpAAQRSIGQLQHHlsICQLNNGKV-------------YLCLDINHAIIDAHSRGILMH 3168
Cdd:cd19532     78 LRLEHVQISDEA-----------EVEEEFERLKNH--VYDLESGETmrivllslsptehYLIFGYHHIAMDGVSFQIFLR 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3169 DLQEAYD-ANLNPQSTSFRDFAsyIKQQSQEEAGR------YW-AEYLDGVEPcfFPSL----------GDSGGANTIpr 3230
Cdd:cd19532    145 DLERAYNgQPLLPPPLQYLDFA--ARQRQDYESGAldedlaYWkSEFSTLPEP--LPLLpfakvksrppLTRYDTHTA-- 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3231 TVEVPSIDSSAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPiHNVNSIfGPLISILPCRIHLHKQ 3310
Cdd:cd19532    219 ERRLDAALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDE-DFMETI-GFFLNLLPLRFRRDPS 296
                          330
                   ....*....|....*....
gi 1820002560 3311 LTVLEALKTVQENYASSLS 3329
Cdd:cd19532    297 QTFADVLKETRDKAYAALA 315
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
2077-2362 6.21e-09

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 62.13  E-value: 6.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2077 VMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLRALQFTAY--TFDVcIAEIITTLVHGGCIcVPSDSERRDNLA 2154
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFfhTFGY-KAGIVACLLTGATV-VPVAVFDVDAIL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2155 KAITDMQVNW--GYLTSSVARLLDPCL----VPSLKVLVLGGEQVNSTDWGKWPS--SVQTI-NGYGPTECCV--FCtgy 2223
Cdd:cd17638     83 EAIERERITVlpGPPTLFQSLLDHPGRkkfdLSSLRAAVTGAATVPVELVRRMRSelGFETVlTAYGLTEAGVatMC--- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2224 tgiqgfQSGNIGTSIASVSwvvdpenhGRLAP-----LGSIGELLVEGPILARGYLNDVDKTQAAfIDDPAWLlegypgh 2298
Cdd:cd17638    160 ------RPGDDAETVATTC--------GRACPgfevrIADDGEVLVRGYNVMQGYLDDPEATAEA-IDADGWL------- 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 2299 egrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVP 2362
Cdd:cd17638    218 --------HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAE-HPGVAQVAVIGVP 272
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3023-3430 6.54e-09

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 62.72  E-value: 6.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3023 FPCTPMQEGILTSQGKDPD--AYWV--CFIYEvipnqeTSISLARLQQAWKGVVHQHSLLRTLLV--DNVPGSTGTTNVV 3096
Cdd:cd20484      2 SPLSEGQKGLWMLQKMSPEmsAYNVplCFRFS------SKLDVEKFKQACQFVLEQHPILKSVIEeeDGVPFQKIEPSKP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3097 LKDPQPSISVFSSEgtATIELFRSRYNPAAQRSIGQLQ--HHLSICQLNNgkvYLCLDINHAIIDAHSRGILMHDLQEAY 3174
Cdd:cd20484     76 LSFQEEDISSLKES--EIIAYLREKAKEPFVLENGPLMrvHLFSRSEQEH---FVLITIHHIIFDGSSSLTLIHSLLDAY 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3175 DA-------NLNPQSTSFRDFASYIKQ----QSQEEAGRYWAEYLDGVEPCF-FPSlgDSGGANTIPR-----TVEVPSI 3237
Cdd:cd20484    151 QAllqgkqpTLASSPASYYDFVAWEQDmlagAEGEEHRAYWKQQLSGTLPILeLPA--DRPRSSAPSFegqtyTRRLPSE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3238 DSSAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRdlPIHNVNSIFGPLISILPCRIHLHKQLTVLEAL 3317
Cdd:cd20484    229 LSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGR--PEERFDSLIGYFINMLPIRSRILGEETFSDFI 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3318 KTVQENYASSLSFQTFPLASMHSFLGL----GTSALFNTAL---------SLQRIDDigPCSAS-EITLkMKEGLDPTEY 3383
Cdd:cd20484    307 RKLQLTVLDGLDHAAYPFPAMVRDLNIprsqANSPVFQVAFfyqnflqstSLQQFLA--EYQDVlSIEF-VEGIHQEGEY 383
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 3384 NITLSAGYSKDAIDISMTFRAGCMDLVQAKRLASNFSQAIKAVTTEP 3430
Cdd:cd20484    384 ELVLEVYEQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
4690-5016 6.55e-09

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 61.75  E-value: 6.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4690 IFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQ----FASYTFDA-CIAEIITtllccGCICVPSDSDRRNN 4764
Cdd:cd17638      6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIinpfFHTFGYKAgIVACLLT-----GATVVPVAVFDVDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4765 LAKAINAMDVNWALLTPSVAR-MLD-PCV----VQSLKILVLGGEQVNSADWDRWPK--SIQTI-NAYGPTECSicCTTY 4835
Cdd:cd17638     81 ILEAIERERITVLPGPPTLFQsLLDhPGRkkfdLSSLRAAVTGAATVPVELVRRMRSelGFETVlTAYGLTEAG--VATM 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4836 SgkqgfKSGTIGTSIVSVSWVVDPENHNRLAplgSIGELLVEGPILARGYLNDMEKTEAAfIDDPAWLlegygghsgrqg 4915
Cdd:cd17638    159 C-----RPGDDAETVATTCGRACPGFEVRIA---DDGEVLVRGYNVMQGYLDDPEATAEA-IDADGWL------------ 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4916 rlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREcLTEAKQLAVeVIVPE---GEGG--YAMLAAFVQL 4990
Cdd:cd17638    218 ---HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAE-HPGVAQVAV-IGVPDermGEVGkaFVVARPGVTL 292
                          330       340
                   ....*....|....*....|....*.
gi 1820002560 4991 GDDTYNTLVKEKAGGDSLTVQVVFLD 5016
Cdd:cd17638    293 TEEDVIAWCRERLANYKVPRFVRFLD 318
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2468-2539 6.57e-09

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 56.40  E-value: 6.57e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 2468 PSTEAERTMQQLWAQVLGIELESIGLDDSFFR-LGGDSITAMQISSSAR-ALHLSVSTGDILKKKTIALIAREI 2539
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEeEFGIELPDTELFEYPTVADLADYL 75
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
7617-8122 6.97e-09

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 62.78  E-value: 6.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 7696
Cdd:cd05929      2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7697 EEIFE-QTGAQVVVASAQYSARWtssschvvtvskALSSQLPAVVDSTNTSVRPE-NAAYIIFTSGSTGVPKGVVLEHRA 7774
Cdd:cd05929     82 CAIIEiKAAALVCGLFTGGGALD------------GLEDYEAAEGGSPETPIEDEaAGWKMLYSGGTTGRPKGIKRGLPG 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7775 V-------ATSCLGHGRAFGITNLSRVLQFASYTFDACiaeiITTLLCGGCICVPSDSDRRNSLaKAISTMDVNWAFLTP 7847
Cdd:cd05929    150 GppdndtlMAAALGFGPGADSVYLSPAPLYHAAPFRWS----MTALFMGGTLVLMEKFDPEEFL-RLIERYRVTFAQFVP 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7848 SV-ARLLD-PGLIP------SLKILAIGGEQSS---SADWNRWPGsvQKIH-VYGPTEccifCTGYTTKQGFE----PST 7911
Cdd:cd05929    225 TMfVRLLKlPEAVRnaydlsSLKRVIHAAAPCPpwvKEQWIDWGG--PIIWeYYGGTE----GQGLTIINGEEwlthPGS 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7912 IGTSVASVSWVVDpENHNRLAPlGSMGELLMEGPIlARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTGDLVQ 7991
Cdd:cd05929    299 VGRAVLGKVHILD-EDGNEVPP-GEIGEVYFANGP-GFEYTNDPEKTAAA-RNEGGWS---------------TLGDVGY 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7992 YNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVeVILPS---GQKNHAMlavfVQLGKGthiahleek 8068
Cdd:cd05929    360 LDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH-PKVLDAAV-VGVPDeelGQRVHAV----VQPAPG--------- 424
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 8069 aggedSMAQVVFLTGTEEELAKRLPKHMVPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:cd05929    425 -----ADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
5631-6136 7.26e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 62.72  E-value: 7.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5631 QAKARPHAPA-ICAWDGE-LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPA 5708
Cdd:PRK13390     6 HAQIAPDRPAvIVAETGEqVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5709 SRHEDTFRHTGAQVVVTSAQHS--ARWIGTNHQVVTVSAGSL---GQLSTLVNPVGLPAI--PENAVyIMFTSGSTGIPK 5781
Cdd:PRK13390    86 PEADYIVGDSGARVLVASAALDglAAKVGADLPLRLSFGGEIdgfGSFEAALAGAGPRLTeqPCGAV-MLYSSGTTGFPK 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5782 GVV--LEHRAV------VTSCwgRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRnDLVKAISTM 5853
Cdd:PRK13390   165 GIQpdLPGRDVdapgdpIVAI--ARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQ-ATLGHVERY 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5854 DVSCALLTPSV-ARLLEPSS-------VPTLQMLVLQGEQVsfadwnrwPASVQ--TINGYGP--------TECSICCNT 5915
Cdd:PRK13390   242 RITVTQMVPTMfVRLLKLDAdvrtrydVSSLRAVIHAAAPC--------PVDVKhaMIDWLGPivyeyyssTEAHGMTFI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5916 YSGKQGFKSGIIGTSVASVSWVVDPENHDrlAPLGSIGELLVEGPILARGYLNDIQKTAAVfiddpawlleGYPGHPgrq 5995
Cdd:PRK13390   314 DSPDWLAHPGSVGRSVLGDLHICDDDGNE--LPAGRIGTVYFERDRLPFRYLNDPEKTAAA----------QHPAHP--- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5996 grLYKT-GDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVrECLPEARQLAVevilpSGQKDHAM---LAAFVQL 6071
Cdd:PRK13390   379 --FWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENAL-TMHPAVHDVAV-----IGVPDPEMgeqVKAVIQL 450
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 6072 EEGTQnalldkeasGEDSMAQVVFlasveEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:PRK13390   451 VEGIR---------GSDELARELI-----DYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
5760-6138 8.11e-09

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 63.19  E-value: 8.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5760 LPAIPENAVYIMFTSGSTGIPKGVVLEHRAVvtscwgrgrafgITNLSRVLQFASYT-FDACMDE------------IIT 5826
Cdd:PRK08043   360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSL------------LANVEQIKTIADFTpNDRFMSAlplfhsfgltvgLFT 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5827 TLMYGGCICV-PSDSDRR--NDLVkaistMDVSCALL--TPSV----ARLLEPSSVPTLQMLVLQGEQVSFADWNRWPAS 5897
Cdd:PRK08043   428 PLLTGAEVFLyPSPLHYRivPELV-----YDRNCTVLfgTSTFlgnyARFANPYDFARLRYVVAGAEKLQESTKQLWQDK 502
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5898 --VQTINGYGPTECS--ICCNTysgKQGFKSGIIGTsvasvswvVDPENHDRLAPLGSI---GELLVEGPILARGYLNdi 5970
Cdd:PRK08043   503 fgLRILEGYGVTECApvVSINV---PMAAKPGTVGR--------ILPGMDARLLSVPGIeqgGRLQLKGPNIMNGYLR-- 569
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5971 qktaavfIDDPAwLLEGyPGHPGRQGRL----YKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVRECLPEA 6046
Cdd:PRK08043   570 -------VEKPG-VLEV-PTAENARGEMergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDK 640
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6047 RQLAveVILPSGQKDHAmLAAFvqleegTQNALLDKEAsgedsmaqvvfLASVEEELAkrLPEHMVPTVFFSLLHFPTTT 6126
Cdd:PRK08043   641 QHAT--AIKSDASKGEA-LVLF------TTDSELTREK-----------LQQYAREHG--VPELAVPRDIRYLKQLPLLG 698
                          410
                   ....*....|..
gi 1820002560 6127 SGKTDRKRLREI 6138
Cdd:PRK08043   699 SGKPDFVTLKSM 710
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
4548-4944 9.29e-09

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 62.45  E-value: 9.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4548 AEQARARPDTPAICAWDGE-----LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 4622
Cdd:cd05921      2 AHWARQAPDRTWLAEREGNggwrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4623 P-------DHpaSRHEHIFRQTGAQVVLASA------QYATLwTSLGRSVVI----------VSEASTSQLPVVTKTAD- 4678
Cdd:cd05921     82 PayslmsqDL--AKLKHLFELLKPGLVFAQDaapfarALAAI-FPLGTPLVVsrnavagrgaISFAELAATPPTAAVDAa 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4679 -PSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHT--RVLQFA--SYTFDACIAEIIT-----TLL 4748
Cdd:cd05921    159 fAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLpwNHTFGGNHNFNLVlynggTLY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4749 CCGCICVPSD-SDRRNNLAK----AINAMDVNWALLTPSVARmlDPCVVQS----LKILVLGGEQVNSADWDRWPK-SIQ 4818
Cdd:cd05921    239 IDDGKPMPGGfEETLRNLREisptVYFNVPAGWEMLVAALEK--DEALRRRffkrLKLMFYAGAGLSQDVWDRLQAlAVA 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4819 TIN-------AYGPTECSICCTTYSGKQGfKSGTIGTSIvsvswvvdPENHNRLAPLGSIGELLVEGPILARGYLNDMEK 4891
Cdd:cd05921    317 TVGeripmmaGLGATETAPTATFTHWPTE-RSGLIGLPA--------PGTELKLVPSGGKYEVRVKGPNVTPGYWRQPEL 387
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 4892 TEAAFiDDpawllEGYgghsgrqgrlYKTGDLVRY----DADGNLVYLGRKDSQVKL 4944
Cdd:cd05921    388 TAQAF-DE-----EGF----------YCLGDAAKLadpdDPAKGLVFDGRVAEDFKL 428
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
3609-3968 1.01e-08

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 61.36  E-value: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3609 IIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQ----FASYTFDA-CIAEIITtllcgGCICVPSDSDRRN 3683
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIinpfFHTFGYKAgIVACLLT-----GATVVPVAVFDVD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3684 SLAKAISTMDVNWAFLTPSVAR-LLD-PGL----IPSLKiLAIGGEQSSSadwnrwPGSVQKIH----------VYGPTE 3747
Cdd:cd17638     80 AILEAIERERITVLPGPPTLFQsLLDhPGRkkfdLSSLR-AAVTGAATVP------VELVRRMRselgfetvltAYGLTE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3748 CCI--FCtgyttkqgfEPSTIGTSVASVSWVVDPENHNRLAplgSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLle 3825
Cdd:cd17638    153 AGVatMC---------RPGDDAETVATTCGRACPGFEVRIA---DDGEVLVRGYNVMQGYLDDPEATAEA-IDADGWL-- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3826 gypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVevilpSGQKDHAMLA 3905
Cdd:cd17638    218 -------------HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAE-HPGVAQVAV-----IGVPDERMGE 278
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 3906 ---AFVQLEEGTQnalLDKEAggedsmaqvvFLASVEEELAKrlpeHMVPTVFFSLLHFPTTTSGK 3968
Cdd:cd17638    279 vgkAFVVARPGVT---LTEED----------VIAWCRERLAN----YKVPRFVRFLDELPRNASGK 327
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
7755-8036 1.15e-08

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 60.98  E-value: 1.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7755 IIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQ----FASYTFDA-CIAEIITtllcgGCICVPSDSDRRN 7829
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIinpfFHTFGYKAgIVACLLT-----GATVVPVAVFDVD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7830 SLAKAISTMDVNWAFLTPSVAR-LLD-PGL----IPSLKiLAIGGEQSSSadwnrwPGSVQKIH----------VYGPTE 7893
Cdd:cd17638     80 AILEAIERERITVLPGPPTLFQsLLDhPGRkkfdLSSLR-AAVTGAATVP------VELVRRMRselgfetvltAYGLTE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7894 CCI--FCtgyttkqgfEPSTIGTSVASVSWVVDPENHNRLAplgSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLle 7971
Cdd:cd17638    153 AGVatMC---------RPGDDAETVATTCGRACPGFEVRIA---DDGEVLVRGYNVMQGYLDDPEATAEA-IDADGWL-- 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 7972 gypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAV 8036
Cdd:cd17638    218 -------------HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAE-HPGVAQVAV 268
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
6851-7042 1.23e-08

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 61.68  E-value: 1.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVE--GPILARGYLNDADKTAAAFVNDpaWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKV 6928
Cdd:cd05971    282 PPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD--WL---------------LTGDLGRKDSDGYFWYVGRDDDVITS 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6929 RGQRVELGEIENRLREcMPRATQMAVEVISPAGAAEQAKtmvvAFLQLNDeardallgGNVPnDDNLSAQvvfpakVDEK 7008
Cdd:cd05971    345 SGYRIGPAEIEECLLK-HPAVLMAAVVGIPDPIRGEIVK----AFVVLNP--------GETP-SDALARE------IQEL 404
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1820002560 7009 LSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLR 7042
Cdd:cd05971    405 VKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
3486-3975 1.27e-08

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 62.01  E-value: 1.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3486 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVAS 3565
Cdd:PRK08008    37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3566 AQY------SARWTSSSCHVVTVSKALSSQLPAVVD-STNTSVRP-----------ENAAYIIFTSGSTGVPKGVVLEH- 3626
Cdd:PRK08008   117 AQFypmyrqIQQEDATPLRHICLTRVALPADDGVSSfTQLKAQQPatlcyapplstDDTAEILFTSGTTSRPKGVVITHy 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3627 -----------------------------------RAVATSCLG---------HGRAFgitnLSRVLQFASyTFDACIAE 3662
Cdd:PRK08008   197 nlrfagyysawqcalrdddvyltvmpafhidcqctAAMAAFSAGatfvllekySARAF----WGQVCKYRA-TITECIPM 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3663 IITTLLcggcICVPSDSDRRNSLAKAISTMDVN----WAFLTPSVARLLDP-GLIPSLkILAIGgeqSSSADWNRWPgSV 3737
Cdd:PRK08008   272 MIRTLM----VQPPSANDRQHCLREVMFYLNLSdqekDAFEERFGVRLLTSyGMTETI-VGIIG---DRPGDKRRWP-SI 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3738 QKIHVygpteccifctGYTTKqgfepstigtsvasvswVVDpeNHNRLAPLGSMGELLMEG---PILARGYLNDVDKTEA 3814
Cdd:PRK08008   343 GRPGF-----------CYEAE-----------------IRD--DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAK 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3815 AFIDDpAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHhVRECLPEARQLAVeVIL 3894
Cdd:PRK08008   393 VLEAD-GWL---------------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELEN-IIATHPKIQDIVV-VGI 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3895 PSGQKDHAmLAAFVQLEEGTQnalLDKEAggedsmaqvvFLASVEEELAKrlpeHMVPTVFFSLLHFPTTTSGKTDRKRL 3974
Cdd:PRK08008   455 KDSIRDEA-IKAFVVLNEGET---LSEEE----------FFAFCEQNMAK----FKVPSYLEIRKDLPRNCSGKIIKKNL 516

                   .
gi 1820002560 3975 R 3975
Cdd:PRK08008   517 K 517
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
7613-8114 1.29e-08

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 62.29  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7613 FAEQARAR---PGAPAICAWDG----ELTYGELDVLSSNLAGHLVQLGVNPED----VVPLCFEksmwTVVAMLAVLKAG 7681
Cdd:cd05943     72 YAENLLRHadaDDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDrvagYLPNIPE----AVVAMLATASIG 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7682 GAFVPLDPDHPASRHEEIFEQTGAQVV--VASAQYSARWTSSSCHVVTVSKALSSQLPAV-VDSTNTSVRPENAA----- 7753
Cdd:cd05943    148 AIWSSCSPDFGVPGVLDRFGQIEPKVLfaVDAYTYNGKRHDVREKVAELVKGLPSLLAVVvVPYTVAAGQPDLSKiakal 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7754 -------------------------YIIFTSGSTGVPKGVVleHRAVATsCLGHGRAFGI-TNLS---RVLQFAS----- 7799
Cdd:cd05943    228 tledflatgaagelefeplpfdhplYILYSSGTTGLPKCIV--HGAGGT-LLQHLKEHILhCDLRpgdRLFYYTTcgwmm 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7800 YTFdaciaeIITTLLCGGCIC-------VPsDSDRRNSLAKA--ISTMDVNWAFLtpsvARLLDPGLIP-------SLKI 7863
Cdd:cd05943    305 WNW------LVSGLAVGATIVlydgspfYP-DTNALWDLADEegITVFGTSAKYL----DALEKAGLKPaethdlsSLRT 373
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7864 LAIGGE--QSSSADW--NRWPGSVQKIHVYGPTE-CCIFCTGYTTKQGF--EPSTIGTSVASVSWvvDPENHnrlAPLGS 7936
Cdd:cd05943    374 ILSTGSplKPESFDYvyDHIKPDVLLASISGGTDiISCFVGGNPLLPVYrgEIQCRGLGMAVEAF--DEEGK---PVWGE 448
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7937 MGELLMEGPILAR--GYLNDVD--KTEAAFIDDpawllegYPGhpgrqgrLYKTGDLVQYNADGNLVYLGRKDSQVKVRG 8012
Cdd:cd05943    449 KGELVCTKPFPSMpvGFWNDPDgsRYRAAYFAK-------YPG-------VWAHGDWIEITPRGGVVILGRSDGTLNPGG 514
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8013 QRVELGE----VEHH--VRECL---PEARQLAVEVILpsgqknhamlavFVQLGKGthiahleekaggedsmaqvVFLTg 8083
Cdd:cd05943    515 VRIGTAEiyrvVEKIpeVEDSLvvgQEWKDGDERVIL------------FVKLREG-------------------VELD- 562
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 1820002560 8084 teEELAKRL---------PKHmVPTVFFALLHFPMTTSGK 8114
Cdd:cd05943    563 --DELRKRIrstirsalsPRH-VPAKIIAVPDIPRTLSGK 599
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
51-286 1.31e-08

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 61.80  E-value: 1.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   51 GYGPTEccivcTGYT----SEQDF--TTGTIGTSIASVSW-VVDPKdhGRLAPLGSVGELLVEGPILARGYLSDPEKTAA 123
Cdd:PRK06839   294 GFGMTE-----TSPTvfmlSEEDArrKVGSIGKPVLFCDYeLIDEN--KNKVEVGEVGELLIRGPNVMKEYWNRPDATEE 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  124 VFinnpawlleghggyagRQGRLYkTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVeVVL 203
Cdd:PRK06839   367 TI----------------QDGWLC-TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINK-LSDVYEVAV-VGR 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  204 P---LGQKNHatlaAFIQLDKGThnallkekvggddsiarVVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDR 280
Cdd:PRK06839   428 QhvkWGEIPI----AFIVKKSSS-----------------VLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQK 486

                   ....*.
gi 1820002560  281 KRLREI 286
Cdd:PRK06839   487 AQLVNQ 492
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
6856-7044 1.35e-08

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 62.16  E-value: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6856 GELLVEGPILARGYLNDADKTAAAFVNDpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVEL 6935
Cdd:cd17642    382 GELCVKGPMIMKGYVNNPEATKALIDKD-GWL---------------HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPP 445
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6936 GEIENRLREcMPRATQMAVEVISPAGAAEQAKTMVV--AFLQLNDEARDALLGGNVPNDDNLSAQVVFpakVDEklsnll 7013
Cdd:cd17642    446 AELESILLQ-HPKIFDAGVAGIPDEDAGELPAAVVVleAGKTMTEKEVMDYVASQVSTAKRLRGGVKF---VDE------ 515
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1820002560 7014 psymmpevyfavpqLPMMISGKTDRKRLREI 7044
Cdd:cd17642    516 --------------VPKGLTGKIDRRKIREI 532
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
7633-8021 1.39e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 61.83  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHPASRHEEIF---EQTGAQVVV 7709
Cdd:PRK04319    74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPL---FEAFMEEAVRdrlEDSEAKVLI 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7710 AS-AQYS---ARWTSSSCHVVTVsKALSSQLPAVVD--------STNTS---VRPENAAYIIFTSGSTGVPKGVVLEHRA 7774
Cdd:PRK04319   151 TTpALLErkpADDLPSLKHVLLV-GEDVEEGPGTLDfnalmeqaSDEFDiewTDREDGAILHYTSGSTGKPKGVLHVHNA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7775 VatscLGHgrafgitnlsrvLQFASYTFDA-------CIAE----------IITTLLCGGCICVpsDSDRRNSLA--KAI 7835
Cdd:PRK04319   230 M----LQH------------YQTGKYVLDLheddvywCTADpgwvtgtsygIFAPWLNGATNVI--DGGRFSPERwyRIL 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7836 STMDVNWAFLTPSVARLL---DPGLI-----PSLK-ILAIGGEQSSSADWnrWPGSV--QKIH-VYGPTEC-CIFCTGYT 7902
Cdd:PRK04319   292 EDYKVTVWYTAPTAIRMLmgaGDDLVkkydlSSLRhILSVGEPLNPEVVR--WGMKVfgLPIHdNWWMTETgGIMIANYP 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7903 TkQGFEPSTIGTSVASV-SWVVDPENhNRLAPlGSMGEL-LMEG-PILARGYLNDVDKTEAAFIDDpaWllegypghpgr 7979
Cdd:PRK04319   370 A-MDIKPGSMGKPLPGIeAAIVDDQG-NELPP-NRMGNLaIKKGwPSMMRGIWNNPEKYESYFAGD--W----------- 433
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 7980 qgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVE 8021
Cdd:PRK04319   434 ----YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE 471
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
5214-5476 1.41e-08

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 61.67  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5214 AGDYIMQSVLELRVDVDEDAFRAAWEHVVQLTAALRTRIVQHsELGLLQVVVEekiqwTESKRLEeyLREDKAVSMGLGD 5293
Cdd:cd19540     21 SAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPED-DGGPYQVVLP-----AAEARPD--LTVVDVTEDELAA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5294 RLARYAliKEPYD--------------GGKRW-FVWTIHHALYDGWSLPRILQAVKQIYS----GAVPERQPsfnAFIQY 5354
Cdd:cd19540     93 RLAEAA--RRGFDltaelplrarlfrlGPDEHvLVLVVHHIAADGWSMAPLARDLATAYAarraGRAPDWAP---LPVQY 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5355 ----------LGQQDLEAATL-----YWQTALADCKAALfpTLP-----PTVTQPVADTtVEYQCPPPSQSA-------T 5407
Cdd:cd19540    168 adyalwqrelLGDEDDPDSLAarqlaYWRETLAGLPEEL--ELPtdrprPAVASYRGGT-VEFTIDAELHARlaalareH 244
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 5408 DITTSTLVRAAWAIVTSRYTSSDDVVFGATVTGRNAPiaGVEAMVGPTIATVPLRVCLQKDQTVSTLLE 5476
Cdd:cd19540    245 GATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDE--ALDDLVGMFVNTLVLRTDVSGDPTFAELLA 311
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
49-285 1.45e-08

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 61.59  E-value: 1.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   49 INGYGPTECCI-VCTGYTSEQDFTTGTIGTSIASVSW-VVDPkdhgrLAPLGSVGELLVEGPILARGYLSDPEKTAAVFI 126
Cdd:cd05912    217 YQSYGMTETCSqIVTLSPEDALNKIGSAGKPLFPVELkIEDD-----GQPPYEVGEILLKGPNVTKGYLNRPDATEESFE 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  127 NNpaWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVeVVLP-- 204
Cdd:cd05912    292 NG--WF---------------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS-HPAIKEAGV-VGIPdd 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  205 -LGQKNHatlaAFIQLDkgthnallkekvggddsiaRVVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:cd05912    353 kWGQVPV----AFVVSE-------------------RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409

                   ..
gi 1820002560  284 RE 285
Cdd:cd05912    410 KQ 411
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
51-184 1.58e-08

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 60.75  E-value: 1.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   51 GYGPTE-CCIVCTGYTSEQDFTTGTIGTsIASVSwVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINnp 129
Cdd:cd17637    142 LYGQTEtSGLVTLSPYRERPGSAGRPGP-LVRVR-IVD--DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRN-- 215
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  130 AWlleghggyagrqgrlYKTGDLVRYDADGNLVCLGRKDSQ--VKLRGQRVELGEVE 184
Cdd:cd17637    216 GW---------------HHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVE 257
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
4547-4720 1.74e-08

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 61.90  E-value: 1.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQARAR---PDTPAICAWDG----ELTYGELDTLSSKLASHLVQLGVKPED----MVPLCFEksmwTVVAMLAVLKAG 4615
Cdd:cd05943     72 YAENLLRHadaDDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDrvagYLPNIPE----AVVAMLATASIG 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4616 GAFVPLDPDHPA----SRhehiFRQTGAQVVLASAQY-------------ATLWTSLG--RSVVIVSEASTSQLPVVTKT 4676
Cdd:cd05943    148 AIWSSCSPDFGVpgvlDR----FGQIEPKVLFAVDAYtyngkrhdvrekvAELVKGLPslLAVVVVPYTVAAGQPDLSKI 223
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 4677 ADPS-----VNPGNAA-------------YAIFTSGSTGIPK-------GVVLEH-KAVVTSC-LGHGQAF 4720
Cdd:cd05943    224 AKALtledfLATGAAGelefeplpfdhplYILYSSGTTGLPKcivhgagGTLLQHlKEHILHCdLRPGDRL 294
PRK13382 PRK13382
bile acid CoA ligase;
4547-5056 1.79e-08

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 61.70  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHP 4626
Cdd:PRK13382    49 FAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFA 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4627 ASRHEHIFRQTGAQVV-------------LASAQYATlwtslgRSVVIVSEASTSQLPVVTKT---ADPSVNPGNAAYAI 4690
Cdd:PRK13382   129 GPALAEVVTREGVDTViydeefsatvdraLADCPQAT------RIVAWTDEDHDLTVEVLIAAhagQRPEPTGRKGRVIL 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4691 FTSGSTGIPKGvvlehkAVVTSCLGHGQAFGITDHT-----RVLQFASYTFDAC-IAEI-ITTLLCCGCIcvpsdSDRRN 4763
Cdd:PRK13382   203 LTSGTTGTPKG------ARRSGPGGIGTLKAILDRTpwraeEPTVIVAPMFHAWgFSQLvLAASLACTIV-----TRRRF 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4764 NLAKAINAMDVNWALLTPSVARMLD-----------PCVVQSLKILVLGGE----QVNSADWDRWPKSIqtINAYGPTEC 4828
Cdd:PRK13382   272 DPEATLDLIDRHRATGLAVVPVMFDrimdlpaevrnRYSGRSLRFAAASGSrmrpDVVIAFMDQFGDVI--YNNYNATEA 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4829 SICCTTYSGKQGFKSGTIGTSIVSVSWVVDPENHNRLaPLGSIGELLVEGPILARGYLNDMEKteaAFIDdpawlleGYg 4908
Cdd:PRK13382   350 GMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREV-PTGEVGTIFVRNDTQFDGYTSGSTK---DFHD-------GF- 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4909 ghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHV--RECLTEAKQLAveviVPEGEGGYAmLAA 4986
Cdd:PRK13382   418 ---------MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLatHPDVAEAAVIG----VDDEQYGQR-LAA 483
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 4987 FVQLGDDTYNTLVKEKAggdsltvqvvfldRVEEELAK-RVPEHmmlttFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:PRK13382   484 FVVLKPGASATPETLKQ-------------HVRDNLANyKVPRD-----IVVLDELPRGATGKILRRELQA 536
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1387-1460 1.84e-08

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 55.33  E-value: 1.84e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560  1387 PKRQPSTEVEQTMQQLWAQVLSIEPNS-IGLDDSFFRLGGDSIVAMKLVGE-ARRTGLQLSVADIFRHPRLVDLAR 1460
Cdd:smart00823    5 PPAERRRLLLDLVREQVAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALAE 80
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
862-1231 1.85e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 61.63  E-value: 1.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  862 ARARPDASAVC-AWDGE-LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPAS 939
Cdd:PRK13391     7 AQTTPDKPAVImASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  940 RHEEIFKQIGAQVVLTSSQHAMLFASSE------RHQVTVSKVSTSQ----LPTVVnfAKSPVDPGNT----AYIIFTSG 1005
Cdd:PRK13391    87 EAAYIVDDSGARALITSAAKLDVARALLkqcpgvRHRLVLDGDGELEgfvgYAEAV--AGLPATPIADeslgTDMLYSSG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1006 TTGIPKGVV--LQHRAV--TTSCLGHGE-AFGYTDHARVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNNLAkAI 1080
Cdd:PRK13391   165 TTGRPKGIKrpLPEQPPdtPLPLTAFLQrLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLA-LI 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1081 STMDVNCALLTPSV-ARLLE-PSA------VPSLKRLVLQGEqvsfadwnrwPGSVQT----INGYGPtecsVCCNTYSG 1148
Cdd:PRK13391   244 EEYGVTHTQLVPTMfSRMLKlPEEvrdkydLSSLEVAIHAAA----------PCPPQVkeqmIDWWGP----IIHEYYAA 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1149 KQGfkSGIigTSVASLSWVVDAG--------------NHNRLAPLGSIGELLVEGPILARgYLNDIDKTEAAFIDDPAWL 1214
Cdd:PRK13391   310 TEG--LGF--TACDSEEWLAHPGtvgramfgdlhildDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGTWS 384
                          410
                   ....*....|....*..
gi 1820002560 1215 LEGYEGHAGRRGRLYKT 1231
Cdd:PRK13391   385 TVGDIGYVDEDGYLYLT 401
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
1938-2381 1.85e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 61.56  E-value: 1.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1938 QAKARPHAPA-ICAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPA 2015
Cdd:PRK13390     6 HAQIAPDRPAvIVAETGEqVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2016 SRHEDIFRQTGAQVVVTSAQHS--ARWIGTNHQVVTVSAGSLEQF----STLVNPVDLPAKPENAAYVMFTSGSTGTPKG 2089
Cdd:PRK13390    86 PEADYIVGDSGARVLVASAALDglAAKVGADLPLRLSFGGEIDGFgsfeAALAGAGPRLTEQPCGAVMLYSSGTTGFPKG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2090 VV--LEHRAV------VTSCLghGQAFGVTN----LLRALQFTAYTFDVCiaeiitTLVH--GGCICVPSDSERRDNL-- 2153
Cdd:PRK13390   166 IQpdLPGRDVdapgdpIVAIA--RAFYDISEsdiyYSSAPIYHAAPLRWC------SMVHalGGTVVLAKRFDAQATLgh 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2154 --------AKAITDMQVNWGYLTSSVARLLDpclVPSLKVLVLGGEQVnstdwgkwPSSVQ--TINGYGPTECCVFCT-- 2221
Cdd:PRK13390   238 veryritvTQMVPTMFVRLLKLDADVRTRYD---VSSLRAVIHAAAPC--------PVDVKhaMIDWLGPIVYEYYSSte 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2222 --GYTGIQGFQ----SGNIGTSIASVSWVVDPENHGrlAPLGSIGELLVEGPILARGYLNDVDKTQAAfiddpawlleGY 2295
Cdd:PRK13390   307 ahGMTFIDSPDwlahPGSVGRSVLGDLHICDDDGNE--LPAGRIGTVYFERDRLPFRYLNDPEKTAAA----------QH 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2296 PGHEgrqgrLYKT-GDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMrKCLPEANQLAVEVVP-PS-GERDHAM- 2371
Cdd:PRK13390   375 PAHP-----FWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENAL-TMHPAVHDVAVIGVPdPEmGEQVKAVi 448
                          490
                   ....*....|.
gi 1820002560 2372 -LAAFIRLDDE 2381
Cdd:PRK13390   449 qLVEGIRGSDE 459
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
7633-8123 1.89e-08

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 61.56  E-value: 1.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAG-------GAFVPldpDHPASRHEEife 7701
Cdd:cd05967     83 YTYAELLDEVSRLAGVLRKLGVVKGDRViiymPMIPE----AAIAMLACARIGaihsvvfGGFAA---KELASRIDD--- 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7702 qtgAQ-VVVASAQYSARWTSSSCHVVTVSKALS--------------SQLPAV------------------------VDS 7742
Cdd:cd05967    153 ---AKpKLIVTASCGIEPGKVVPYKPLLDKALElsghkphhvlvlnrPQVPADltkpgrdldwsellakaepvdcvpVAA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7743 TNTSvrpenaaYIIFTSGSTGVPKGVVLEH--RAVA-----TSCLGHGRA---FGITNLSRVLQFaSYtfdaciaeIITT 7812
Cdd:cd05967    230 TDPL-------YILYTSGTTGKPKGVVRDNggHAVAlnwsmRNIYGIKPGdvwWAASDVGWVVGH-SY--------IVYG 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7813 LLCGGCICV-----PSDSDRRNSLAKAISTMDVNWAFLTPSVARLL---DPGL-------IPSLKILAIGGEQ--SSSAD 7875
Cdd:cd05967    294 PLLHGATTVlyegkPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIrkeDPDGkyikkydLSSLRTLFLAGERldPPTLE 373
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7876 WNRWPGSVQKIHVYGPTEccifcTGY---TTKQGFEPSTIGTSVASVSW------VVDPENhNRLAPlGSMGELLMEGPi 7946
Cdd:cd05967    374 WAENTLGVPVIDHWWQTE-----TGWpitANPVGLEPLPIKAGSPGKPVpgyqvqVLDEDG-EPVGP-NELGNIVIKLP- 445
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7947 LARGYLNDVDKTEAAFIDDpawLLEGYPGhpgrqgrLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEH---- 8022
Cdd:cd05967    446 LPPGCLLTLWKNDERFKKL---YLSKFPG-------YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEEsvls 515
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8023 H--VREClpearqlAVeVILPSGQKNHAMLAVFVQlgkgthiahleeKAGGEDSMAQVvfltgtEEELAKRLPKHMVPTV 8100
Cdd:cd05967    516 HpaVAEC-------AV-VGVRDELKGQVPLGLVVL------------KEGVKITAEEL------EKELVALVREQIGPVA 569
                          570       580
                   ....*....|....*....|....*..
gi 1820002560 8101 FFALLHF----PMTTSGKADRKRLREI 8123
Cdd:cd05967    570 AFRLVIFvkrlPKTRSGKILRRTLRKI 596
PRK12467 PRK12467
peptide synthase; Provisional
8257-8562 1.96e-08

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 62.49  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8257 DITDVVPASYIQQ---FYIATGVRAPrEAFNYPFIDLsDAVDIQVLQASCSALLEHFPILRTHFVYfQGKL---YQVIPR 8330
Cdd:PRK12467  2642 DIEDIYPLSPMQQgmlFHTLYEGGAG-DYINQMRVDV-EGLDVERFRTAWQAVIDRHEILRSGFLW-DGELeepLQVVYK 2718
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8331 HQDLPFSIFEVN--GALAEESQAIHIRDLDQTSPLGLP--TSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIY 8406
Cdd:PRK12467  2719 QARLPFSRLDWRdrADLEQALDALAAADRQQGFDLLSAplLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRY 2798
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8407 QQEPLLSTTG-FHSYLAYVHNQ-RSASINYW-SRLLKGSHITNITSKLRPK----LGKDTTIRSVKVErvIRTPQLPT-- 8477
Cdd:PRK12467  2799 FGQPPPAREGrYRDYIAWLQAQdAEASEAFWkEQLAALEEPTRLARALYPApaeaVAGHGAHYLHLDA--TQTRQLIEfa 2876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8478 ---GLTMASLVSSAWAVVLSHISGEEDVVYGLVVAGRNSDLPSITEV-------------------------SVQDQYIS 8529
Cdd:PRK12467  2877 rrhRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQlglfintlpviaspraeqtvsdwlqQVQAQNLA 2956
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1820002560 8530 LGESDSIGLDDIvQHCTDWPAKSEFDSIIQHQN 8562
Cdd:PRK12467  2957 LREFEHTPLADI-QRWAGQGGEALFDSILVFEN 2988
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4686-5055 1.96e-08

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 60.57  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4686 AAYaIFTSGSTGIPKGVVLEHKAVVTS--CLGHGQAFGITDhtrVLQFASYTF--DACIAEIITTLLCCGCICVPSDSDR 4761
Cdd:cd05944      5 AAY-FHTGGTTGTPKLAQHTHSNEVYNawMLALNSLFDPDD---VLLCGLPLFhvNGSVVTLLTPLASGAHVVLAGPAGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4762 RN-----NLAKAINAMDVNWALLTPSV--ARMLDP--CVVQSLKILVLGGEQVNSADWDRWPKS--IQTINAYGPTECSi 4830
Cdd:cd05944     81 RNpglfdNFWKLVERYRITSLSTVPTVyaALLQVPvnADISSLRFAMSGAAPLPVELRARFEDAtgLPVVEGYGLTEAT- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4831 CCTTYSGKQG-FKSGTIGTSI----VSVSwVVDPENHN--RLAPlGSIGELLVEGPILARGYLNDmEKTEAAFIDDpAWL 4903
Cdd:cd05944    160 CLVAVNPPDGpKRPGSVGLRLpyarVRIK-VLDGVGRLlrDCAP-DEVGEICVAGPGVFGGYLYT-EGNKNAFVAD-GWL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4904 legygghsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhhvrECLTEAKQLAVEVIV--PEGEGGy 4981
Cdd:cd05944    236 ---------------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIE----EALLRHPAVAFAGAVgqPDAHAG- 295
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 4982 AMLAAFVQLGDDTyntlvkeKAGGDSLTVQVVflDRVEEELAkrVPEHMMLttfftLEAMPTTTSGKIDRKRLR 5055
Cdd:cd05944    296 ELPVAYVQLKPGA-------VVEEEELLAWAR--DHVPERAA--VPKHIEV-----LEELPVTAVGKVFKPALR 353
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
3479-3840 2.00e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 61.46  E-value: 2.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3479 AICAWDGE-LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdhpaSRH---EE-- 3552
Cdd:PRK08276     3 VIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI------NWHltaAEia 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3553 -IFEQTGAQVVVASAQYSArwtssschvvtVSKALSSQLPA------VVDSTNTSVRP-ENA---------------AYI 3609
Cdd:PRK08276    77 yIVDDSGAKVLIVSAALAD-----------TAAELAAELPAgvplllVVAGPVPGFRSyEEAlaaqpdtpiadetagADM 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3610 IFTSGSTGVPKGVV--LEHRAVATSCLGH----GRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN 3683
Cdd:PRK08276   146 LYSSGTTGRPKGIKrpLPGLDPDEAPGMMlallGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEE 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3684 SLAkAISTMDVNWAFLTPSV-ARLL----------DpglIPSLKiLAIGGEQSSSADWNR----WPGSVqkIH-VYGPTE 3747
Cdd:PRK08276   226 ALA-LIERYRVTHSQLVPTMfVRMLklpeevraryD---VSSLR-VAIHAAAPCPVEVKRamidWWGPI--IHeYYASSE 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3748 CCIFcTGYTTKQGFE-PSTIGTSVASVSWVVDpENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpAWLLEG 3826
Cdd:PRK08276   299 GGGV-TVITSEDWLAhPGSVGKAVLGEVRILD-EDGNELPP-GEIGTVYFEMDGYPFEYHNDPEKTAAARNPH-GWVTVG 374
                          410
                   ....*....|....
gi 1820002560 3827 YPGHPGRQGRLYKT 3840
Cdd:PRK08276   375 DVGYLDEDGYLYLT 388
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2583-2695 2.15e-08

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 60.93  E-value: 2.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2583 FFLELRNRVQPQLLVTALTALVQRHSMLRARF-QRQTGGRWQQYISEhdSSSLIVNHIHTRDTTEIVEALRQSRG-SLDI 2660
Cdd:cd19532     28 FSYRLTGPLDVARLERAVRAVGQRHEALRTCFfTDPEDGEPMQGVLA--SSPLRLEHVQISDEAEVEEEFERLKNhVYDL 105
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1820002560 2661 ERGPVLAAVLCDAGERQSLFV-AIHHLVVDLVSWRI 2695
Cdd:cd19532    106 ESGETMRIVLLSLSPTEHYLIfGYHHIAMDGVSFQI 141
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
5770-6070 2.23e-08

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 60.04  E-value: 2.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 IMFTSGSTGIPKGVVLEHRAVVTS---------CWGRGRAFGITNLSRV--LQFasytfdacmdeIITTLMYGGCICVPs 5838
Cdd:cd17630      5 VILTSGSTGTPKAVVHTAANLLASaaglhsrlgFGGGDSWLLSLPLYHVggLAI-----------LVRSLLAGAELVLL- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5839 dsDRRNDLVKAISTMDVSCALLTPS-VARLLE----PSSVPTLQMLVLQGEQVSFADWNRwpASVQTIN---GYGPTECS 5910
Cdd:cd17630     73 --ERNQALAEDLAPPGVTHVSLVPTqLQRLLDsgqgPAALKSLRAVLLGGAPIPPELLER--AADRGIPlytTYGMTETA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5911 --ICCNTYSGkqgFKSGIIGtsvasvswVVDPenHDRLApLGSIGELLVEGPILARGYLNDIQKTAAvfiDDPAWllegy 5988
Cdd:cd17630    149 sqVATKRPDG---FGRGGVG--------VLLP--GRELR-IVEDGEIWVGGASLAMGYLRGQLVPEF---NEDGW----- 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5989 pghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVE------HHVREC----LPEAR--QLAVEVILP 6056
Cdd:cd17630    207 ----------FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEaalaahPAVRDAfvvgVPDEElgQRPVAVIVG 276
                          330
                   ....*....|....
gi 1820002560 6057 SGQKDHAMLAAFVQ 6070
Cdd:cd17630    277 RGPADPAELRAWLK 290
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
51-288 2.46e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 61.33  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   51 GYGPTECCIVC--TGYTSEQDFTTGTIGTSIASV-SWVVDPKdhGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVfIN 127
Cdd:PRK12583   349 AYGMTETSPVSlqTTAADDLERRVETVGRTQPHLeVKVVDPD--GATVPRGEIGELCTRGYSVMKGYWNNPEATAES-ID 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  128 NPAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVrecLPEAKQLAVEVVLPLGQ 207
Cdd:PRK12583   426 EDGWM---------------HTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFL---FTHPAVADVQVFGVPDE 487
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  208 KNHATLAAFIQLDKGThnallkekvggddsiarvvflAGVEEELAK----RLPKHMVPTVFFALLHFPTTTSGKTDRKRL 283
Cdd:PRK12583   488 KYGEEIVAWVRLHPGH---------------------AASEEELREfckaRIAHFKVPRYFRFVDEFPMTVTGKVQKFRM 546

                   ....*
gi 1820002560  284 REIGA 288
Cdd:PRK12583   547 REISI 551
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
870-1249 2.46e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 61.07  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  870 AVCAWDGE-LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpghpaSRH---EE-- 943
Cdd:PRK08276     3 VIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI------NWHltaAEia 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  944 -IFKQIGAQVVLTSSQHA----MLFASSERHqVTVSKVSTSQLPTVVNF-----AKSPVDPGNT---AYIIFTSGTTGIP 1010
Cdd:PRK08276    77 yIVDDSGAKVLIVSAALAdtaaELAAELPAG-VPLLLVVAGPVPGFRSYeealaAQPDTPIADEtagADMLYSSGTTGRP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1011 KGVV--LQHRAVTTSCLGH---GEAFGYTD------------HARVLQFASytfdaciaeiiTTLLYGGCICVPSESDRR 1073
Cdd:PRK08276   156 KGIKrpLPGLDPDEAPGMMlalLGFGMYGGpdsvylspaplyHTAPLRFGM-----------SALALGGTVVVMEKFDAE 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1074 NNLAkAISTMDVNCALLTPSV-ARLLE-PSAV------PSLKRLVLQGEqvsfadwnrwPGSV----QTINGYGPtecsV 1141
Cdd:PRK08276   225 EALA-LIERYRVTHSQLVPTMfVRMLKlPEEVrarydvSSLRVAIHAAA----------PCPVevkrAMIDWWGP----I 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1142 CCNTYSGKQGF------------KSGIIGTSVASLSWVVDAgNHNRLAPlGSIGELLVEGPILARGYLNDIDKTEAAfid 1209
Cdd:PRK08276   290 IHEYYASSEGGgvtvitsedwlaHPGSVGKAVLGEVRILDE-DGNELPP-GEIGTVYFEMDGYPFEYHNDPEKTAAA--- 364
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 1210 dpawllegyeghagRRGRLYKT-GDLVRCDADGNLVCLGRK 1249
Cdd:PRK08276   365 --------------RNPHGWVTvGDVGYLDEDGYLYLTDRK 391
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
6899-7041 2.50e-08

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 60.95  E-value: 2.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6899 GRLYKTGDLVYYnKDGNLVYIGRKDGQVKVRGQRVELGEIENRLRECMPratqmaveVISPAGAAEQaKTMVVAFLQlnD 6978
Cdd:cd17654    338 GTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLG--------VESCAVTLSD-QQRLIAFIV--G 405
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 6979 EARDALLGgnvpnddnlsaqvvfpakvDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd17654    406 ESSSSRIH-------------------KELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5-171 2.53e-08

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 60.94  E-value: 2.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    5 WALLTPSVARLLEPshIPSLRILVMGGEQVNSADWDRW----PSSVQTINGYGPTECCIVCTGYTSEQDFTTGT------ 74
Cdd:cd05910    184 LERVARYCAQHGIT--LPSLRRVLSAGAPVPIALAARLrkmlSDEAEILTPYGATEALPVSSIGSRELLATTTAatsgga 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   75 ---IGTSIASVSWVVDPKDHGRLA--------PLGSVGELLVEGPILARGYLSDPEKTAAVFINNPawlleghggyagRQ 143
Cdd:cd05910    262 gtcVGRPIPGVRVRIIEIDDEPIAewddtlelPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN------------SE 329
                          170       180
                   ....*....|....*....|....*...
gi 1820002560  144 GRLYKTGDLVRYDADGNLVCLGRKDSQV 171
Cdd:cd05910    330 GFWHRMGDLGYLDDEGRLWFCGRKAHRV 357
PRK07638 PRK07638
acyl-CoA synthetase; Validated
1935-2445 2.82e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 60.95  E-value: 2.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1935 FTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLcFEKSMWTVVAMLAVLKAGGAFVPLDPD-H 2013
Cdd:PRK07638     7 YKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAIL-LENRIEFLQLFAGAAMAGWTCVPLDIKwK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2014 PASRHEDIFRqTGAQVVVTSAQHSARWIGTNHQVVTVSA--GSLEQFSTLVNPVDlpaKPENAAYVM-FTSGSTGTPKGV 2090
Cdd:PRK07638    86 QDELKERLAI-SNADMIVTERYKLNDLPDEEGRVIEIDEwkRMIEKYLPTYAPIE---NVQNAPFYMgFTSGSTGKPKAF 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2091 VLEHRAVVTS--CLGHgqAFGVTNLLRALQFTAYTFDVCIAEIITTLVHGGCICVpsdsERRDNLAKA-----ITDMQVN 2163
Cdd:PRK07638   162 LRAQQSWLHSfdCNVH--DFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHL----MRKFIPNQVldkleTENISVM 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2164 WGY--LTSSVARlLDPCLVPSLKVLVLGGeqvnstDWGK---------WPsSVQTINGYGPTECCvFCTGYTGIQGFQSG 2232
Cdd:PRK07638   236 YTVptMLESLYK-ENRVIENKMKIISSGA------KWEAeakekikniFP-YAKLYEFYGASELS-FVTALVDEESERRP 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2233 N-IGTSIASVSWVVDPENHGRLAPlGSIGELLVEGPILARGYLNDVDKTQAafIDDPAWLLEGYPGHEGRQGRLYKTGdl 2311
Cdd:PRK07638   307 NsVGRPFHNVQVRICNEAGEEVQK-GEIGTVYVKSPQFFMGYIIGGVLARE--LNADGWMTVRDVGYEDEEGFIYIVG-- 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2312 vrysSDGNLVCLGrkdsqvkvrGQRVELGEVEHHMRKClPEANQLAVEVVPPS--GERDHAmlaafirlddetrnsplII 2389
Cdd:PRK07638   382 ----REKNMILFG---------GINIFPEEIESVLHEH-PAVDEIVVIGVPDSywGEKPVA-----------------II 430
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 2390 KYAEDNSTaqivfltgIEEELSERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREI 2445
Cdd:PRK07638   431 KGSATKQQ--------LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSW 478
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
3487-3858 2.94e-08

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 61.08  E-value: 2.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVN--PEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP----LDPDhpASRHeeIFEQTGAQ 3560
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPlydtLGPE--AIEY--ILNHAEIS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3561 VVVASAQYSarwtssschVVTVSKAL---SSQLPAVVDSTntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHG 3637
Cdd:cd05927     82 IVFCDAGVK---------VYSLEEFEklgKKNKVPPPPPK-----PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVF 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3638 RAFGITN--------LS---------RVLQFASYTFDACI--------------AEIITTLLCGgcicVPSDSDR----- 3681
Cdd:cd05927    148 KILEILNkinptdvyISylplahifeRVVEALFLYHGAKIgfysgdirlllddiKALKPTVFPG----VPRVLNRiydki 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3682 RNSLAK--AISTMDVNWAFLTpSVARLLDPGLIPSL--------KI-LAIGGEqsssadwNRW--------PGSVQK--- 3739
Cdd:cd05927    224 FNKVQAkgPLKRKLFNFALNY-KLAELRSGVVRASPfwdklvfnKIkQALGGN-------VRLmltgsaplSPEVLEflr 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3740 ----IHV---YGPTECCifctGYTTKQGFEPSTIGTSVASVSWV----VD-PE-NHNRLAPLGSmGELLMEGPILARGYL 3806
Cdd:cd05927    296 valgCPVlegYGQTECT----AGATLTLPGDTSVGHVGGPLPCAevklVDvPEmNYDAKDPNPR-GEVCIRGPNVFSGYY 370
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 3807 NDVDKTEAAFIDDpAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRK 3858
Cdd:cd05927    371 KDPEKTAEALDED-GWL---------------HTGDIGEWLPNGTLKIIDRK 406
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
5764-6131 3.04e-08

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 61.52  E-value: 3.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5764 PENAVYIMFTSGSTGIPKGVVLEHRAVVTSCwgrGRAFGITNLSR------VLQ-FASYTFDACMdeIITTL------MY 5830
Cdd:PRK06814   792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANR---AQVAARIDFSPedkvfnALPvFHSFGLTGGL--VLPLLsgvkvfLY 866
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5831 ggcicvPSDSDRR--NDLVKAI-STMDVSCALLTPSVARLLEPSSVPTLQMLVLQGEQVSFADWNRWPAS--VQTINGYG 5905
Cdd:PRK06814   867 ------PSPLHYRiiPELIYDTnATILFGTDTFLNGYARYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKfgIRILEGYG 940
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5906 PTECS--ICCNTysgKQGFKSGIIGTsvasvswvVDPENHDRLAPLGSI---GELLVEGPILARGYLndiqktaavfidd 5980
Cdd:PRK06814   941 VTETApvIALNT---PMHNKAGTVGR--------LLPGIEYRLEPVPGIdegGRLFVRGPNVMLGYL------------- 996
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5981 pawLLEGyPG--HPGRQGrLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVRECLPEARQLAVEVilPSG 6058
Cdd:PRK06814   997 ---RAEN-PGvlEPPADG-WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSI--PDA 1069
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 6059 QKdhamlaafvqleeGTQNALLDKEASGEdsmaQVVFLASVEeelAKRLPEHMVPTVFFSLLHFPTTTSGKTD 6131
Cdd:PRK06814  1070 RK-------------GERIILLTTASDAT----RAAFLAHAK---AAGASELMVPAEIITIDEIPLLGTGKID 1122
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1954-2330 3.20e-08

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 60.55  E-value: 3.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1954 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDhpasrhedifrqtgaqvvvts 2033
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG--------------------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2034 aqhsarwIGTNHQVVTVSAGSLEQFstlvnpVDLPAKPENAAyVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGV--- 2110
Cdd:cd05910     61 -------MGRKNLKQCLQEAEPDAF------IGIPKADEPAA-ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIrpg 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2111 -----TNLLRALqftaytFDVCIAeiITTLVHGGCICVPSDSERRDnLAKAITDMQVN--------WGYLTSSVARLLDP 2177
Cdd:cd05910    127 evdlaTFPLFAL------FGPALG--LTSVIPDMDPTRPARADPQK-LVGAIRQYGVSivfgspalLERVARYCAQHGIT 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2178 clVPSLKVLVLGGEQVNSTDWGKW----PSSVQTINGYGPTECC---------VFCTGYTGIQGFQSGNIGTSIASVSWV 2244
Cdd:cd05910    198 --LPSLRRVLSAGAPVPIALAARLrkmlSDEAEILTPYGATEALpvssigsreLLATTTAATSGGAGTCVGRPIPGVRVR 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2245 VDPENHGRLA--------PLGSIGELLVEGPILARGYLNDVDKTQAAFIDDPawllegypghegRQGRLYKTGDLVRYSS 2316
Cdd:cd05910    276 IIEIDDEPIAewddtlelPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN------------SEGFWHRMGDLGYLDD 343
                          410
                   ....*....|....
gi 1820002560 2317 DGNLVCLGRKDSQV 2330
Cdd:cd05910    344 EGRLWFCGRKAHRV 357
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
6851-7042 3.22e-08

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 60.81  E-value: 3.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFvndpawlveGHGkhpgrrgrLYKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:cd05909    337 PIGEGGLLLVRGPNVMLGYLNEPELTSFAF---------GDG--------WYDTGDIGKIDGEGFLTITGRLSRFAKIAG 399
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6931 QRVELGEIENRLRECMPRATQMAVEVISPAGAAEQaktmVVAFLQLNDEARDALlggnvpnDDNLSAQvvfpakvdeKLS 7010
Cdd:cd05909    400 EMVSLEAIEDILSEILPEDNEVAVVSVPDGRKGEK----IVLLTTTTDTDPSSL-------NDILKNA---------GIS 459
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1820002560 7011 NL-LPSYmmpevYFAVPQLPMMISGKTDRKRLR 7042
Cdd:cd05909    460 NLaKPSY-----IHQVEEIPLLGTGKPDYVTLK 487
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
1935-2436 3.32e-08

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 60.75  E-value: 3.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1935 FTEQAKAR---PHAPAICAWDG----ELTYGELDALSSKLASHLVQLGVNPED----VVPLCFEksmwTVVAMLAVLKAG 2003
Cdd:cd05943     72 YAENLLRHadaDDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDrvagYLPNIPE----AVVAMLATASIG 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2004 GAFVPLDPDHPASRHEDIFRQ---------------------------------TGAQVVVTS---------AQHSARWI 2041
Cdd:cd05943    148 AIWSSCSPDFGVPGVLDRFGQiepkvlfavdaytyngkrhdvrekvaelvkglpSLLAVVVVPytvaagqpdLSKIAKAL 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2042 GTNHQVVTVSAGSLEqFSTLvnPVDLPakpenaAYVMFTSGSTGTPK-------GVVLEH-RAVVTSC-LGHGQafgvtn 2112
Cdd:cd05943    228 TLEDFLATGAAGELE-FEPL--PFDHP------LYILYSSGTTGLPKcivhgagGTLLQHlKEHILHCdLRPGD------ 292
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2113 llRALQFTA-----YTFDVCIAEIITTLV-HGGCICVPSDSERRDNLAK-AITDMQVNWGYLTSSVARLLDPCLVPSLKV 2185
Cdd:cd05943    293 --RLFYYTTcgwmmWNWLVSGLAVGATIVlYDGSPFYPDTNALWDLADEeGITVFGTSAKYLDALEKAGLKPAETHDLSS 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2186 LVLGGE-----QVNSTDW--GKWPSSVQTINGYGPTE-CCVFCTG------YTG-IQGfqsgnIGTSIASVSWvvDPEnh 2250
Cdd:cd05943    371 LRTILStgsplKPESFDYvyDHIKPDVLLASISGGTDiISCFVGGnpllpvYRGeIQC-----RGLGMAVEAF--DEE-- 441
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2251 GRlAPLGSIGELLVEGPILAR--GYLNDVD--KTQAAFIDDpawllegYPGhegrqgrLYKTGDLVRYSSDGNLVCLGRK 2326
Cdd:cd05943    442 GK-PVWGEKGELVCTKPFPSMpvGFWNDPDgsRYRAAYFAK-------YPG-------VWAHGDWIEITPRGGVVILGRS 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2327 DSQVKVRGQRVELGEVEHHMRKClPEanqlaVE---VVPPSGERDHAMLAAFIRLDDETRNSPLIIKyaEDNSTaqivfl 2403
Cdd:cd05943    507 DGTLNPGGVRIGTAEIYRVVEKI-PE-----VEdslVVGQEWKDGDERVILFVKLREGVELDDELRK--RIRST------ 572
                          570       580       590
                   ....*....|....*....|....*....|...
gi 1820002560 2404 tgIEEELSerlPQHmVPTVFFALVHFPTTTSGK 2436
Cdd:cd05943    573 --IRSALS---PRH-VPAKIIAVPDIPRTLSGK 599
PRK08315 PRK08315
AMP-binding domain protein; Validated
1924-2448 3.35e-08

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 60.60  E-value: 3.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1924 PPAIERCVHDLFTEQAKARPHAPAICAWDGEL--TYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmWTVVaML 1997
Cdd:PRK08315    11 VPLLEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVgiwaPNVPE---WVLT-QF 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1998 AVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSAQ-------------------------HSAR--------WIGTN 2044
Cdd:PRK08315    87 ATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamlyelapelatcepgqlQSARlpelrrviFLGDE 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2045 HQVVTVSAGSLEQFSTLVNPVDLPA-----KPENAAYVMFTSGSTGTPKGVVLEHRAVVTSclghgqAFGVTnllRALQF 2119
Cdd:PRK08315   167 KHPGMLNFDELLALGRAVDDAELAArqatlDPDDPINIQYTSGTTGFPKGATLTHRNILNN------GYFIG---EAMKL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2120 TAYtfD-VCI--------AEIITTLV---HGGCICVPSdsERRDNLA--KAITDMQVN--WGYLTSSVARLLDP------ 2177
Cdd:PRK08315   238 TEE--DrLCIpvplyhcfGMVLGNLAcvtHGATMVYPG--EGFDPLAtlAAVEEERCTalYGVPTMFIAELDHPdfarfd 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2178 -------------CLVPSLKVLVlggEQVNSTDwgkwpssvQTInGYGPTECC-VFCtgytgiqgfQSGnIGTSIAS-VS 2242
Cdd:PRK08315   314 lsslrtgimagspCPIEVMKRVI---DKMHMSE--------VTI-AYGMTETSpVST---------QTR-TDDPLEKrVT 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2243 WV-----------VDPENhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAfIDDPAWLlegypgHegrqgrlykTGDL 2311
Cdd:PRK08315   372 TVgralphlevkiVDPET-GETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDADGWM------H---------TGDL 434
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2312 VRYSSDGNLVCLGR-KDsqVKVRG-----QRvELGEVEHHMRKClpeanqLAVEVVP-PS---GERdhamLAAFIRL-DD 2380
Cdd:PRK08315   435 AVMDEEGYVNIVGRiKD--MIIRGgeniyPR-EIEEFLYTHPKI------QDVQVVGvPDekyGEE----VCAWIILrPG 501
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 2381 ETrnspliikyaednstaqivfLTgiEEEL----SERLPQHMVPTVFFALVHFPTTTSGKTDRKRLREIGAS 2448
Cdd:PRK08315   502 AT--------------------LT--EEDVrdfcRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIE 551
PRK07867 PRK07867
acyl-CoA synthetase; Validated
4599-5058 3.49e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 60.46  E-value: 3.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4599 EKSMWTVVAMLAvlkaGGAFVPLDPDHPASRHEHIFRQTGAQVVLASAQYATLWTSLGRSVVIVSEASTSQLPVVTKTAD 4678
Cdd:PRK07867    66 EFSLLLGAAALS----GIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRD 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4679 PSVNPGNAAYA-----IFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGIT-DHTRVLQFASYTFDACIAEIITTLLCCGC 4752
Cdd:PRK07867   142 AEPPFRVADPDdlfmlIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGpDDVCYVSMPLFHSNAVMAGWAVALAAGAS 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4753 ICVP---SDSD-----RR------NNLAKAinamdVNWALLTPSVARMLDpcvvQSLKIlVLGGEQVnSADWDRWPK--S 4816
Cdd:PRK07867   222 IALRrkfSASGflpdvRRygatyaNYVGKP-----LSYVLATPERPDDAD----NPLRI-VYGNEGA-PGDIARFARrfG 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4817 IQTINAYGPTECSIcctTYSGKQGFKSGTIGTSIVSVSwVVDPE-----------NHNRLAPLGSIGELL-VEGPILARG 4884
Cdd:PRK07867   291 CVVVDGFGSTEGGV---AITRTPDTPPGALGPLPPGVA-IVDPDtgtecppaedaDGRLLNADEAIGELVnTAGPGGFEG 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4885 YLNDMEKTEAAFiddpawllegygghsgRQGRlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREcLTE 4964
Cdd:PRK07867   367 YYNDPEADAERM----------------RGGV-YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLR-YPD 428
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4965 AKQLAVeVIVPEGEGGYAMLAAfVQLGDDTynTLVKEKAGGdsltvqvvFLDRVEEELAKRVPEHMMLTTfftleAMPTT 5044
Cdd:PRK07867   429 ATEVAV-YAVPDPVVGDQVMAA-LVLAPGA--KFDPDAFAE--------FLAAQPDLGPKQWPSYVRVCA-----ELPRT 491
                          490
                   ....*....|....
gi 1820002560 5045 TSGKIDRKRLREIG 5058
Cdd:PRK07867   492 ATFKVLKRQLSAEG 505
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
989-1367 3.62e-08

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 60.47  E-value: 3.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  989 KSPVDP-GNTAYIIFTSGTTGIPKGV------VLQHRAVTTSCLGhgeAFGYTDHARVLQFASYTFDACIAEIITTLLYG 1061
Cdd:cd05929    118 ETPIEDeAAGWKMLYSGGTTGRPKGIkrglpgGPPDNDTLMAAAL---GFGPGADSVYLSPAPLYHAAPFRWSMTALFMG 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1062 GCICVPSESDRRNNLaKAISTMDVNCALLTPSV-ARLLE-PSAVP------SLKRLVLQGEQVSFA---DWNRWPGSVqT 1130
Cdd:cd05929    195 GTLVLMEKFDPEEFL-RLIERYRVTFAQFVPTMfVRLLKlPEAVRnaydlsSLKRVIHAAAPCPPWvkeQWIDWGGPI-I 272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1131 INGYGPTEC--SVCCNtysGKQGFK-SGIIGTSVASLSWVVDAgNHNRLAPlGSIGELLVEGPIlARGYLNDIDKTEAAF 1207
Cdd:cd05929    273 WEYYGGTEGqgLTIIN---GEEWLThPGSVGRAVLGKVHILDE-DGNEVPP-GEIGEVYFANGP-GFEYTNDPEKTAAAR 346
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1208 IDDpawlleGYEghagrrgrlyKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREClPEARQLAVeVILPS 1287
Cdd:cd05929    347 NEG------GWS----------TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH-PKVLDAAV-VGVPD 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1288 ---GQKEHALlaafIQldkgnhnalfeekaSGEDSMAQVVFLTGVEEELAKRLPEHMVP-TILFtVKAMPITTSGKIDRK 1363
Cdd:cd05929    409 eelGQRVHAV----VQ--------------PAPGADAGTALAEELIAFLRDRLSRYKCPrSIEF-VAELPRDDTGKLYRR 469

                   ....
gi 1820002560 1364 RLQD 1367
Cdd:cd05929    470 LLRD 473
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
6842-7038 3.69e-08

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 60.32  E-value: 3.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPlGSIGELLVEGPILARGYLNDADKTAAAFVNDpaWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGR 6921
Cdd:cd17631    280 VDPDGREVPP-GEVGEIVVRGPHVMAGYWNRPEATAAAFRDG--WF---------------HTGDLGRLDEDGYLYIVDR 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 KDGQVKVRGQRVELGEIENRLREcMPRATQMAV---------EVispagaaeqaktmVVAFLQLNDEARdallggnvpnd 6992
Cdd:cd17631    342 KKDMIISGGENVYPAEVEDVLYE-HPAVAEVAVigvpdekwgEA-------------VVAVVVPRPGAE----------- 396
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 6993 dnlsaqvVFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDR 7038
Cdd:cd17631    397 -------LDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
847-1236 3.70e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 60.83  E-value: 3.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  847 PPAVDRCIHDLFAEQARARPD-------ASAVCAWDGeLTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAM 919
Cdd:PRK12582    44 LGPYPRSIPHLLAKWAAEAPDrpwlaqrEPGHGQWRK-VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMT 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  920 LAVLKAGgafVPLDPGHPA--------SRHEEIFKQIGAQVVLtsSQHAMLFASSeRHQVT---VSKVSTSQLPT---VV 985
Cdd:PRK12582   123 LAAMQAG---VPAAPVSPAyslmshdhAKLKHLFDLVKPRVVF--AQSGAPFARA-LAALDlldVTVVHVTGPGEgiaSI 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  986 NFAK---SPVD-----------PGNTAYIIFTSGTTGIPKGVVLQHRAVTTS---------------------------C 1024
Cdd:PRK12582   197 AFADlaaTPPTaavaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANiamqeqlrprepdppppvsldwmpwnhT 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1025 LGHGEAFG---------YTDHARVLqfaSYTFDACIAEI--ITTLLYG------GCICVPSESDR--RNNLAKAISTMDV 1085
Cdd:PRK12582   277 MGGNANFNgllwgggtlYIDDGKPL---PGMFEETIRNLreISPTVYGnvpagyAMLAEAMEKDDalRRSFFKNLRLMAY 353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1086 NCALLTPSVARLLEPSAVPSLkrlvlqGEQVSFadwnrwpgsvqtINGYGPTECS-VCCNTYSGKQgfKSGIIGTSVAsl 1164
Cdd:PRK12582   354 GGATLSDDLYERMQALAVRTT------GHRIPF------------YTGYGATETApTTTGTHWDTE--RVGLIGLPLP-- 411
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 1165 swvvdaGNHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFiDDpawllEGYeghagrrgrlYKTGDLVR 1236
Cdd:PRK12582   412 ------GVELKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAF-DE-----EGF----------YRLGDAAR 461
PRK05850 PRK05850
acyl-CoA synthetase; Validated
7611-7779 3.79e-08

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 60.73  E-value: 3.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7611 DLFAEQARARPGAPAIC------AWDG---ELTYGELDVLSSNLAGHLVQLGVnPEDVVPLCFEKSMWTVVAMLAVLKAG 7681
Cdd:PRK05850     5 SLLRERASLQPDDAAFTfidyeqDPAGvaeTLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7682 GAFVPLDPDHPASRHEeifeQTGAqvVVASAQYSARWTSSSChVVTVSKALSSQ----LPAVV-------DSTNTS-VRP 7749
Cdd:PRK05850    84 LIAVPLSVPQGGAHDE----RVSA--VLRDTSPSVVLTTSAV-VDDVTEYVAPQpgqsAPPVIevdlldlDSPRGSdARP 156
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1820002560 7750 ENA---AYIIFTSGSTGVPKGVVLEHRAVATSC 7779
Cdd:PRK05850   157 RDLpstAYLQYTSGSTRTPAGVMVSHRNVIANF 189
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
5645-6139 4.00e-08

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 60.06  E-value: 4.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5645 DGELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAfvpldpdhpasrhedtfrhtgaqvvv 5724
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV-------------------------- 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5725 tsaqhsARWIGTNhqvvtVSAGSLGQLSTLVNPVGLpaIPENAVYImFTSGSTGIPKGVVLEHR---------------- 5788
Cdd:cd05940     55 ------AALINYN-----LRGESLAHCLNVSSAKHL--VVDAALYI-YTSGTTGLPKAAIISHRrawrggaffagsggal 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5789 --------------AVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCIC------VPSDSDRRNDLVK 5848
Cdd:cd05940    121 psdvlytclplyhsTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCryllnqPPKPTERKHKVRM 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5849 AISTMdvscalLTPSV-ARLLEPSSVPTLqmlvlqgeqVSFadwnrwpasvqtingYGPTECSICCNTYSGKQGF--KSG 5925
Cdd:cd05940    201 IFGNG------LRPDIwEEFKERFGVPRI---------AEF---------------YAATEGNSGFINFFGKPGAigRNP 250
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5926 IIGTSVASVSWV-VDPENHDRL---------APLGSIGELLVEGPILAR--GYLNDIQKTAA----VFIDDPAWllegyp 5989
Cdd:cd05940    251 SLLRKVAPLALVkYDLESGEPIrdaegrcikVPRGEPGLLISRINPLEPfdGYTDPAATEKKilrdVFKKGDAW------ 324
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5990 ghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVR--ECLPEARQLAVEVilpSGQKDHAMLAa 6067
Cdd:cd05940    325 ---------FNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGafPGVEEANVYGVQV---PGTDGRAGMA- 391
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 6068 fvqleegtqnALLDKEASGEDsmaqvvfLASVEEELAKRLPEHMVPtVFFSLL-HFPTTTSGKTDRKRLREIG 6139
Cdd:cd05940    392 ----------AIVLQPNEEFD-------LSALAAHLEKNLPGYARP-LFLRLQpEMEITGTFKQQKVDLRNEG 446
PRK03584 PRK03584
acetoacetate--CoA ligase;
858-1017 4.74e-08

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 60.58  E-value: 4.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  858 FAEQA--RARPDASAVCAW--DG---ELTYGELDELSSKLAAHLVQLGVKREDVV----PLCFEksmwTVVAMLAVLKAG 926
Cdd:PRK03584    88 YAENLlrHRRDDRPAIIFRgeDGprrELSWAELRRQVAALAAALRALGVGPGDRVaaylPNIPE----TVVAMLATASLG 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  927 GAFV---PlDPGHPA--SRheeiFKQIGAQVVLTSSQHamLFASSERHQVTVSKVSTSQLPT-----VVNFAKSPVDPGN 996
Cdd:PRK03584   164 AIWSscsP-DFGVQGvlDR----FGQIEPKVLIAVDGY--RYGGKAFDRRAKVAELRAALPSlehvvVVPYLGPAAAAAA 236
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560  997 TA----------------------------YIIFTSGTTGIPK-------GVVLQH 1017
Cdd:PRK03584   237 LPgallwedflapaeaaelefepvpfdhplWILYSSGTTGLPKcivhghgGILLEH 292
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
3467-3968 5.13e-08

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 60.36  E-value: 5.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3467 FTEQAKAR---PHAPAICAWDG----ELTYGELDALSSKLASHLVQLGVNPED----VVPLCFEksmwTVVAMLAVLKAG 3535
Cdd:cd05943     72 YAENLLRHadaDDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDrvagYLPNIPE----AVVAMLATASIG 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3536 GAFVPLDPDHPASRHEEIFEQTGAQVV--VASAQYSARWTSSSCHVVTVSKALSSQLPAV-VDSTNTSVRPENAA----- 3607
Cdd:cd05943    148 AIWSSCSPDFGVPGVLDRFGQIEPKVLfaVDAYTYNGKRHDVREKVAELVKGLPSLLAVVvVPYTVAAGQPDLSKiakal 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3608 -------------------------YIIFTSGSTGVPKGVVleHRAVATsCLGHGRAFGI-TNLS---RVLQFAS----- 3653
Cdd:cd05943    228 tledflatgaagelefeplpfdhplYILYSSGTTGLPKCIV--HGAGGT-LLQHLKEHILhCDLRpgdRLFYYTTcgwmm 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3654 YTFdaciaeIITTLLCGGCIC-------VPsDSDRRNSLAKA--ISTMDVNWAFLtpsvARLLDPGLIP-------SLKI 3717
Cdd:cd05943    305 WNW------LVSGLAVGATIVlydgspfYP-DTNALWDLADEegITVFGTSAKYL----DALEKAGLKPaethdlsSLRT 373
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3718 LAIGGE--QSSSADW--NRWPGSVQKIHVYGPTE-CCIFCTGYTTKQGF--EPSTIGTSVASVSWvvDPENHnrlAPLGS 3790
Cdd:cd05943    374 ILSTGSplKPESFDYvyDHIKPDVLLASISGGTDiISCFVGGNPLLPVYrgEIQCRGLGMAVEAF--DEEGK---PVWGE 448
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3791 MGELLMEGPILAR--GYLNDVD--KTEAAFIDDpawllegYPGhpgrqgrLYKTGDLVQYNADGNLVYLGRKDSQVKVRG 3866
Cdd:cd05943    449 KGELVCTKPFPSMpvGFWNDPDgsRYRAAYFAK-------YPG-------VWAHGDWIEITPRGGVVILGRSDGTLNPGG 514
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3867 QRVELGE----VEHH--VRECL---PEARQLAVEVILpsgqkdhamlaaFVQLEEGtqnalldkeaggedsmaqVVFLAS 3937
Cdd:cd05943    515 VRIGTAEiyrvVEKIpeVEDSLvvgQEWKDGDERVIL------------FVKLREG------------------VELDDE 564
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1820002560 3938 VEEELAKRL-----PEHmVPTVFFSLLHFPTTTSGK 3968
Cdd:cd05943    565 LRKRIRSTIrsalsPRH-VPAKIIAVPDIPRTLSGK 599
PLN02736 PLN02736
long-chain acyl-CoA synthetase
1924-2107 5.19e-08

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 60.11  E-value: 5.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1924 PPAIE-RCVHDLFTEQAKARPHAPA----ICAwDGE------LTYGELDALSSKLASHLVQLGVNPEDVVPLCF-EKSMW 1991
Cdd:PLN02736    38 PDHPEiGTLHDNFVYAVETFRDYKYlgtrIRV-DGTvgeykwMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFiNRPEW 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1992 TVV--AMLAVLKAGgafVPL----DPDhpASRHedIFRQTGAQVVVTSAQH------------SARWI------------ 2041
Cdd:PLN02736   117 LIVdhACSAYSYVS---VPLydtlGPD--AVKF--IVNHAEVAAIFCVPQTlntllsclseipSVRLIvvvggadeplps 189
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 2042 ---GTNHQVVTVSAGSLEQFSTLVNPVdlPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQA 2107
Cdd:PLN02736   190 lpsGTGVEIVTYSKLLAQGRSSPQPFR--PPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLS 256
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
878-1366 5.82e-08

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 59.50  E-value: 5.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  878 LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVP----LDPGHPASRHEEIFKQIGAQVV 953
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRVDRGGAVYAAVDE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  954 LTSSQHAMLfasserhqvtvskvstsqlptvvnfakspvdpgntayIIFTSGTTGIPKGVVLQHRavtTSCLGHGEAF-- 1031
Cdd:cd05974     81 NTHADDPML-------------------------------------LYFTSGTTSKPKLVEHTHR---SYPVGHLSTMyw 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1032 ---------------GYTDHARVLQFASYTFDACIaeiittLLYGgcicvPSESDRRNNLAkAISTMDVNCALLTPSVAR 1096
Cdd:cd05974    121 iglkpgdvhwnisspGWAKHAWSCFFAPWNAGATV------FLFN-----YARFDAKRVLA-ALVRYGVTTLCAPPTVWR 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1097 LL--EP--SAVPSLKRLVLQGE--------QVSFAdWNRwpgsvqTI-NGYGPTECSVCCNTYSGkQGFKSGIIGTSVAS 1163
Cdd:cd05974    189 MLiqQDlaSFDVKLREVVGAGEplnpevieQVRRA-WGL------TIrDGYGQTETTALVGNSPG-QPVKAGSMGRPLPG 260
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1164 LswvvdagnhnRLAPLGSIGELLVEGPILArgylnDIDKTEaafiddPAWLLEGYEGHAGR-----RGRLYKTGDLVRCD 1238
Cdd:cd05974    261 Y----------RVALLDPDGAPATEGEVAL-----DLGDTR------PVGLMKGYAGDPDKtahamRGGYYRTGDIAMRD 319
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1239 ADGNLVCLGRKDSQVKVRGQRVELGEIEhhvrECLPEARQLAVEVILPSGQKEH-ALLAAFIQLDKGnhnalfeekaSGE 1317
Cdd:cd05974    320 EDGYLTYVGRADDVFKSSDYRISPFELE----SVLIEHPAVAEAAVVPSPDPVRlSVPKAFIVLRAG----------YEP 385
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 1318 DSMAQVVFLTGVEEELAkrlPEHMVPTILFtvKAMPITTSGKIDRKRLQ 1366
Cdd:cd05974    386 SPETALEIFRFSRERLA---PYKRIRRLEF--AELPKTISGKIRRVELR 429
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
877-1025 5.85e-08

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 60.14  E-value: 5.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLVQLgVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD----PGHpASRHEEIFKQIGAQV 952
Cdd:PRK12476    68 ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFapelPGH-AERLDTALRDAEPTV 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  953 VLTSSqhamlfASSERHQVTVSKVSTSQLPTVV-----------NFAKSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVT 1021
Cdd:PRK12476   146 VLTTT------AAAEAVEGFLRNLPRLRRPRVIaidaipdsageSFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVG 219

                   ....
gi 1820002560 1022 TSCL 1025
Cdd:PRK12476   220 TNLV 223
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
3608-3971 6.08e-08

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 58.96  E-value: 6.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3608 YIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRNSLAK 3687
Cdd:cd17633      4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3688 aISTMDVNWAFLTPSVARLLDPGLIPSLKILAIggeqSSSADwnRWPGSVQKihvygpteccifctgyTTKQGFEPSTI- 3766
Cdd:cd17633     84 -INQYNATVIYLVPTMLQALARTLEPESKIKSI----FSSGQ--KLFESTKK----------------KLKNIFPKANLi 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3767 ---GTSVAS-VSWVVDPEnhnrLAPLGSMGELLMEGPILARGYLNDVD-----KTEAAFiddpawllEGYPGHPGRQ-GR 3836
Cdd:cd17633    141 efyGTSELSfITYNFNQE----SRPPNSVGRPFPNVEIEIRNADGGEIgkifvKSEMVF--------SGYVRGGFSNpDG 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3837 LYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREC----------LPEAR--QLAVEVILPSGQKDHAML 3904
Cdd:cd17633    209 WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIpgieeaivvgIPDARfgEIAVALYSGDKLTYKQLK 288
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 3905 AAfvqleegtqnalldkeaggedsmaqvvflasveeeLAKRLPEHMVPTVFFSLLHFPTTTSGKTDR 3971
Cdd:cd17633    289 RF-----------------------------------LKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
51-173 6.13e-08

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 59.92  E-value: 6.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   51 GYGPTECCIVCTGyTSEQDFTTGTIGTSIASVSW-VVDPKDHGRLApLGSV--GELLVEGPILARGYLSDPEKTAAVFIN 127
Cdd:cd05927    305 GYGQTECTAGATL-TLPGDTSVGHVGGPLPCAEVkLVDVPEMNYDA-KDPNprGEVCIRGPNVFSGYYKDPEKTAEALDE 382
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560  128 NpAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKL 173
Cdd:cd05927    383 D-GWL---------------HTGDIGEWLPNGTLKIIDRKKNIFKL 412
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
7617-8122 6.16e-08

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 59.62  E-value: 6.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7617 ARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVplcfeksmwTVV-----AML----AVLKAGGAFVPL 7687
Cdd:cd12118     14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTV---------AVLapntpAMYelhfGVPMAGAVLNAL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7688 DPDHPASRHEEIFEQTGAQVVVASAQYSARwtssschvvtvskalssQLPAVVDSTNTSVRPENAAYII---FTSGSTGV 7764
Cdd:cd12118     85 NTRLDAEEIAFILRHSEAKVLFVDREFEYE-----------------DLLAEGDPDFEWIPPADEWDPIalnYTSGTTGR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7765 PKGVVLEHRAVATSCLGHGRAFGITNLSRVL----QF--ASYTFDACIAEIittllCGGCICVpsdsdrRNSLAKAI--- 7835
Cdd:cd12118    148 PKGVVYHHRGAYLNALANILEWEMKQHPVYLwtlpMFhcNGWCFPWTVAAV-----GGTNVCL------RKVDAKAIydl 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7836 ---------------STMDVNWAfltPSVARLLD-------PGLIPSLKILAiggeqsssadwNRWPGSVQKIHVYGPTE 7893
Cdd:cd12118    217 iekhkvthfcgaptvLNMLANAP---PSDARPLPhrvhvmtAGAPPPAAVLA-----------KMEELGFDVTHVYGLTE 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7894 C---CIFCT--------------GYTTKQGfepstIGTSVASVSWVVDPENHNRLAPLG-SMGELLMEGPILARGYLNDV 7955
Cdd:cd12118    283 TygpATVCAwkpewdelpteeraRLKARQG-----VRYVGLEEVDVLDPETMKPVPRDGkTIGEIVFRGNIVMKGYLKNP 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7956 DKTEAAFIDdpAWllegypghpgrqgrlYKTGDLVQYNADGnlvYLGRKDSQVKV---RGQRVELGEVE----HHvrecl 8028
Cdd:cd12118    358 EATAEAFRG--GW---------------FHSGDLAVIHPDG---YIEIKDRSKDIiisGGENISSVEVEgvlyKH----- 412
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8029 PEARQLAVeVILPS---GQKNHAmlavFVQLGKGThiahleekaggedsmaqvvflTGTEEELAK----RLPKHMVP-TV 8100
Cdd:cd12118    413 PAVLEAAV-VARPDekwGEVPCA----FVELKEGA---------------------KVTEEEIIAfcreHLAGFMVPkTV 466
                          570       580
                   ....*....|....*....|..
gi 1820002560 8101 FFalLHFPMTTSGKADRKRLRE 8122
Cdd:cd12118    467 VF--GELPKTSTGKIQKFVLRD 486
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
7249-7473 6.20e-08

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 59.64  E-value: 6.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7249 VVVEEKIQWTESEALEEYLKEDKAVSMGL-GDPLAHYALVKEawGGKRWFVW-TIHHALYDGGS-LPLI---LHAVKQVY 7322
Cdd:cd20484     77 SFQEEDISSLKESEIIAYLREKAKEPFVLeNGPLMRVHLFSR--SEQEHFVLiTIHHIIFDGSSsLTLIhslLDAYQALL 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7323 SGAVLERQPS---FNAFIQ----YLGQQDLEATAAYWQTALSDCEAVL--FPPLPSTVTQPVADTTVEYQCPP-LSK--- 7389
Cdd:cd20484    155 QGKQPTLASSpasYYDFVAweqdMLAGAEGEEHRAYWKQQLSGTLPILelPADRPRSSAPSFEGQTYTRRLPSeLSNqik 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7390 ---ATLDTTTSTLIRAAWAIVTSCYTSSDDVVYGTTVTGRnaPIAGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQ 7466
Cdd:cd20484    235 sfaRSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGR--PEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLT 312

                   ....*..
gi 1820002560 7467 STDMIAH 7473
Cdd:cd20484    313 VLDGLDH 319
PRK09192 PRK09192
fatty acyl-AMP ligase;
3487-3638 6.89e-08

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 59.63  E-value: 6.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3487 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVvvASA 3566
Cdd:PRK09192    50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIAQLRGML--ASA 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3567 QYSA--------RWTSSSCHVVTVSKALSSQ---LPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLG 3635
Cdd:PRK09192   128 QPAAiitpdellPWVNEATHGNPLLHVLSHAwfkALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRA 207

                   ...
gi 1820002560 3636 HGR 3638
Cdd:PRK09192   208 ISH 210
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
862-1367 7.01e-08

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 59.62  E-value: 7.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  862 ARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVplcfeksmwTVV-----AML----AVLKAGGAFVPL 932
Cdd:cd12118     14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTV---------AVLapntpAMYelhfGVPMAGAVLNAL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  933 DPGHPASRHEEIFKQIGAQVVLTSSQHAM--LFASSERhqvtvskvstsqlptvvNF-AKSPVDPGNTAYIIFTSGTTGI 1009
Cdd:cd12118     85 NTRLDAEEIAFILRHSEAKVLFVDREFEYedLLAEGDP-----------------DFeWIPPADEWDPIALNYTSGTTGR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1010 PKGVVLQHRAVTTSCLGHGEAFGYTDHARVL----QF--ASYTFDACIAEIittllyGGC-ICVpsesdrRNNLAKAI-- 1080
Cdd:cd12118    148 PKGVVYHHRGAYLNALANILEWEMKQHPVYLwtlpMFhcNGWCFPWTVAAV------GGTnVCL------RKVDAKAIyd 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1081 ----------------STMDVNCAlltPSVARLLE------PSAVPSLKRLVLQGEQVSFadwnrwpgsvQTINGYGPTE 1138
Cdd:cd12118    216 liekhkvthfcgaptvLNMLANAP---PSDARPLPhrvhvmTAGAPPPAAVLAKMEELGF----------DVTHVYGLTE 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1139 C----SVCC-----NTYS--------GKQGfksgiIGTSVASLSWVVDAGNHNRLAPLG-SIGELLVEGPILARGYLNDI 1200
Cdd:cd12118    283 TygpaTVCAwkpewDELPteerarlkARQG-----VRYVGLEEVDVLDPETMKPVPRDGkTIGEIVFRGNIVMKGYLKNP 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1201 DKTEAAFiddpawllegyeghagrRGRLYKTGDLVRCDADGNLvclgrkdsQVKVR--------GQRVELGEIE----HH 1268
Cdd:cd12118    358 EATAEAF-----------------RGGWFHSGDLAVIHPDGYI--------EIKDRskdiiisgGENISSVEVEgvlyKH 412
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1269 vreclPEARQLAVeVILPSgQKEHALLAAFIQLDKGnhnalfeEKASGEDSMAQVvfltgveeelAKRLPEHMVP-TILF 1347
Cdd:cd12118    413 -----PAVLEAAV-VARPD-EKWGEVPCAFVELKEG-------AKVTEEEIIAFC----------REHLAGFMVPkTVVF 468
                          570       580
                   ....*....|....*....|
gi 1820002560 1348 TvkAMPITTSGKIDRKRLQD 1367
Cdd:cd12118    469 G--ELPKTSTGKIQKFVLRD 486
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
3446-3875 7.01e-08

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 59.68  E-value: 7.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3446 KKIWGWN--ADVPPAIE----RCVHDLFtEQAKAR-PHAPAICAWDGELTYGELDALSSKLASHLV-QLGVNPEDVVPLC 3517
Cdd:PRK08974     2 EKVWLNRypADVPAEINpdryQSLVDMF-EQAVARyADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3518 FEKSMWTVVAMLAVLKAGGAFVPLDP-------DHP---------------ASRHEEIFEQTGAQVVVASA---QYSARW 3572
Cdd:PRK08974    81 MPNLLQYPIALFGILRAGMIVVNVNPlytprelEHQlndsgakaivivsnfAHTLEKVVFKTPVKHVILTRmgdQLSTAK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3573 TSSSCHVVTVSKALSSQ--LPAVVDSTNT--------SVRP----ENAAYIIFTSGSTGVPKGVVLEHR----------A 3628
Cdd:PRK08974   161 GTLVNFVVKYIKRLVPKyhLPDAISFRSAlhkgrrmqYVKPelvpEDLAFLQYTGGTTGVAKGAMLTHRnmlanleqakA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3629 VATSCLGHGRAFGITNLSRVLQFAsYTFDaCIAEI---ITTLLcggcICVPSDSDRR-NSLAK----AIStmDVNWAF-- 3698
Cdd:PRK08974   241 AYGPLLHPGKELVVTALPLYHIFA-LTVN-CLLFIelgGQNLL----ITNPRDIPGFvKELKKypftAIT--GVNTLFna 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3699 -LTPSVARLLDpglIPSLKiLAIGGE---QSSSADwnRWPgSVQKIHV---YGPTECCIFCTGYTTKQGFEPSTIGTSVA 3771
Cdd:PRK08974   313 lLNNEEFQELD---FSSLK-LSVGGGmavQQAVAE--RWV-KLTGQYLlegYGLTECSPLVSVNPYDLDYYSGSIGLPVP 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3772 SVS-WVVDPENHNrlAPLGSMGELLMEGPILARGYLNDVDKTeAAFIDDpAWLlegypghpgrqgrlyKTGDLVQYNADG 3850
Cdd:PRK08974   386 STEiKLVDDDGNE--VPPGEPGELWVKGPQVMLGYWQRPEAT-DEVIKD-GWL---------------ATGDIAVMDEEG 446
                          490       500
                   ....*....|....*....|....*
gi 1820002560 3851 NLVYLGRKDSQVKVRGQRVELGEVE 3875
Cdd:PRK08974   447 FLRIVDRKKDMILVSGFNVYPNEIE 471
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
24-184 7.34e-08

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 59.38  E-value: 7.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   24 LRILVMGGEQVN-SADWDRWPSSVQTINGYGPTECC-IVCtgYTSEQDFTTGTIGTSIASVSWVVDPKDhgrlaPLGSVG 101
Cdd:cd05914    236 IKEFVIGGAKINpDVEEFLRTIGFPYTIGYGMTETApIIS--YSPPNRIRLGSAGKVIDGVEVRIDSPD-----PATGEG 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  102 ELLVEGPILARGYLSDPEKTAAVFINNpAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKL-RGQRVEL 180
Cdd:cd05914    309 EIIVRGPNVMKGYYKNPEATAEAFDKD-GWF---------------HTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYP 372

                   ....
gi 1820002560  181 GEVE 184
Cdd:cd05914    373 EEIE 376
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
1924-2314 7.43e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 59.67  E-value: 7.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1924 PPAIERCVHDLFTEQAKARPHAPAIC-------AWDGeLTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAM 1996
Cdd:PRK12582    44 LGPYPRSIPHLLAKWAAEAPDRPWLAqrepghgQWRK-VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMT 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1997 LAVLKAGGAFVPLDP-------DHPASRH-------EDIFRQTGAQVvvTSAQHSARWIGTNHQVVTVSAGSLE--QFST 2060
Cdd:PRK12582   123 LAAMQAGVPAAPVSPayslmshDHAKLKHlfdlvkpRVVFAQSGAPF--ARALAALDLLDVTVVHVTGPGEGIAsiAFAD 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2061 LV-NPVDLPAK-------PENAAYVMFTSGSTGTPKGVVLEHR---------AVVTS------------------CLGHG 2105
Cdd:PRK12582   201 LAaTPPTAAVAaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRmmcaniamqEQLRPrepdppppvsldwmpwnhTMGGN 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2106 QAF------GVTNLLRALQFTAYTFDVCIAEI--ITTLVHGGcicVP-------SDSERRDNLAKAITDmqvNWGYLTSS 2170
Cdd:PRK12582   281 ANFngllwgGGTLYIDDGKPLPGMFEETIRNLreISPTVYGN---VPagyamlaEAMEKDDALRRSFFK---NLRLMAYG 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2171 VARLLDPCL--VPSLKVLVLGGEQVNSTDWGKWPSSVQTINGYGPTEccvfctgytgiqgfQSGNIGTSIASVSWvvdpe 2248
Cdd:PRK12582   355 GATLSDDLYerMQALAVRTTGHRIPFYTGYGATETAPTTTGTHWDTE--------------RVGLIGLPLPGVEL----- 415
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 2249 nhgRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFiDDpawllEGYpghegrqgrlYKTGDLVRY 2314
Cdd:PRK12582   416 ---KLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAF-DE-----EGF----------YRLGDAARF 462
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
5647-6136 7.44e-08

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 59.70  E-value: 7.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5647 ELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDTFRHTGAQVVVTS 5726
Cdd:PRK08008    37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5727 A------QHSARWIGTNHQVVTVSAGSLGQLSTLVN--------PVGL----PAIPENAVYIMFTSGSTGIPKGVVLEHR 5788
Cdd:PRK08008   117 AqfypmyRQIQQEDATPLRHICLTRVALPADDGVSSftqlkaqqPATLcyapPLSTDDTAEILFTSGTTSRPKGVVITHY 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5789 ----AVVTSCW-GRGRA--------------FGITNLSRVL-------------------QFASY--TFDACMDEIITTL 5828
Cdd:PRK08008   197 nlrfAGYYSAWqCALRDddvyltvmpafhidCQCTAAMAAFsagatfvllekysarafwgQVCKYraTITECIPMMIRTL 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5829 MyggcICVPSDSDRRNDLVKAISTMDVSCAlltpsvarllepssvptlqmlvlqgEQVSFADwnRWpaSVQTINGYGPTE 5908
Cdd:PRK08008   277 M----VQPPSANDRQHCLREVMFYLNLSDQ-------------------------EKDAFEE--RF--GVRLLTSYGMTE 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5909 C--SICCNTYSGKQGFKSgiIGTsvASVSW---VVDPENHDrlAPLGSIGELLVEG---PILARGYLNDIQKTAAVFIDD 5980
Cdd:PRK08008   324 TivGIIGDRPGDKRRWPS--IGR--PGFCYeaeIRDDHNRP--LPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEAD 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5981 pAWLlegypghpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHhVRECLPEARQLAVeVILPSGQK 6060
Cdd:PRK08008   398 -GWL---------------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELEN-IIATHPKIQDIVV-VGIKDSIR 459
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6061 DHAmLAAFVQLEEGTQnalLDKEAsgedsmaqvvFLASVEEELAKrlpeHMVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:PRK08008   460 DEA-IKAFVVLNEGET---LSEEE----------FFAFCEQNMAK----FKVPSYLEIRKDLPRNCSGKIIKKNLK 517
PLN02574 PLN02574
4-coumarate--CoA ligase-like
44-184 7.44e-08

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 59.47  E-value: 7.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   44 SSVQTINGYGPTECCIVCT-GYTSEQDFTTGTIGTSIASVSWVVDPKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTA 122
Cdd:PLN02574   344 PHVDFIQGYGMTESTAVGTrGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQ 423
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560  123 AVfINNPAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVE 184
Cdd:PLN02574   424 ST-IDKDGWL---------------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLE 469
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
6832-7041 7.54e-08

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 59.38  E-value: 7.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6832 PDENREaypfVRPSNAALAplgSIGELLVEGPILARGYLNDADKTAAafVNDPAWLveghgkhpgrrgrlyKTGDLVYYN 6911
Cdd:TIGR01923  276 PLAGRE----IKIKVDNKE---GHGEIMVKGANLMKGYLYQGELTPA--FEQQGWF---------------NTGDIGELD 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6912 KDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcmprATQMAVEVISPAGAAEQAKtMVVAFLQLNDEardallggnvPN 6991
Cdd:TIGR01923  332 GEGFLYVLGRRDDLIISGGENIYPEEIETVLYQ----HPGIQEAVVVPKPDAEWGQ-VPVAYIVSESD----------IS 396
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6992 DdnlsaqvvfpAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:TIGR01923  397 Q----------AKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
3461-3977 7.75e-08

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 59.68  E-value: 7.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3461 RCVHDLFTEQAKARPHAPAICAWDGE------LTYGELDALSSKLASHLVQLGVNPEDVVPlCFEKSMWTVVAM-LAVLK 3533
Cdd:PRK13295    24 RTINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVS-CQLPNWWEFTVLyLACSR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3534 AGGAFVPLdpdHPASRHEEI---FEQTGAQVVVAS--------AQYSARWTSSSC---HVVTVSKA-------------- 3585
Cdd:PRK13295   103 IGAVLNPL---MPIFRERELsfmLKHAESKVLVVPktfrgfdhAAMARRLRPELPalrHVVVVGGDgadsfeallitpaw 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3586 -LSSQLPAVVDSTNTsvRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQ---FASYTFDACIA 3661
Cdd:PRK13295   180 eQEPDAPAILARLRP--GPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMaspMAHQTGFMYGL 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3662 EIITTLlcgGCICVPSDSDRRNSLAKAISTMDVNW-----AFLTPSV-ARLLDPGLIPSLKILAIGG--------EQSss 3727
Cdd:PRK13295   258 MMPVML---GATAVLQDIWDPARAAELIRTEGVTFtmastPFLTDLTrAVKESGRPVSSLRTFLCAGapipgalvERA-- 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3728 adWNRWPGSVqkIHVYGPTECCIFCtgyTTKQGFEPSTIGTSVA-SVSW----VVDPENHNrlAPLGSMGELLMEGPILA 3802
Cdd:PRK13295   333 --RAALGAKI--VSAWGMTENGAVT---LTKLDDPDERASTTDGcPLPGvevrVVDADGAP--LPAGQIGRLQVRGCSNF 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3803 RGYLNDVDKTEaafIDDPAWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGR-KDsqVKVRG-QRVELGEVE----H 3876
Cdd:PRK13295   404 GGYLKRPQLNG---TDADGW---------------FDTGDLARIDADGYIRISGRsKD--VIIRGgENIPVVEIEallyR 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3877 HvreclPEARQLAVeVILPS---GQKdhamLAAFVQLEEGtqnALLDKEaggedsmAQVVFLASveEELAKR-LPEHMVp 3952
Cdd:PRK13295   464 H-----PAIAQVAI-VAYPDerlGER----ACAFVVPRPG---QSLDFE-------EMVEFLKA--QKVAKQyIPERLV- 520
                          570       580
                   ....*....|....*....|....*
gi 1820002560 3953 tVFFSLlhfPTTTSGKTDRKRLREI 3977
Cdd:PRK13295   521 -VRDAL---PRTPSGKIQKFRLREM 541
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
6710-6804 8.05e-08

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 59.16  E-value: 8.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6710 EQALAR-PNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPA 6788
Cdd:cd17631      2 RRRARRhPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTP 81
                           90
                   ....*....|....*.
gi 1820002560 6789 SRHEDILRQTGAQVIL 6804
Cdd:cd17631     82 PEVAYILADSGAKVLF 97
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
2070-2438 8.14e-08

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 59.98  E-value: 8.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2070 KPENAAYVMFTSGSTGTPKGVVLEHRAVVTSClghGQAFGVTNLLRA-LQFTA----YTFDVcIAEIITTLVHGgcICV- 2143
Cdd:PRK06814   791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANR---AQVAARIDFSPEdKVFNAlpvfHSFGL-TGGLVLPLLSG--VKVf 864
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2144 --PSDSERR-------DNLAKAI--TDMQVNwGYltssvARLLDPCLVPSLKVLVLGGEQVNSTDWGKWPSS--VQTING 2210
Cdd:PRK06814   865 lyPSPLHYRiipeliyDTNATILfgTDTFLN-GY-----ARYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKfgIRILEG 938
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2211 YGPTECCVFCTGYTGIQgFQSGNIGTSIasvswvvdPENHGRLAPLGSI---GELLVEGPILARGYLnDVDKtqaafidd 2287
Cdd:PRK06814   939 YGVTETAPVIALNTPMH-NKAGTVGRLL--------PGIEYRLEPVPGIdegGRLFVRGPNVMLGYL-RAEN-------- 1000
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2288 pawllegyPG-HEGRQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEhhmrkclpeanQLAVEVVPPSGe 2366
Cdd:PRK06814  1001 --------PGvLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVE-----------ELAAELWPDAL- 1060
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 2367 rdHAMLAafirLDDETRNSPLI-IKYAEDNSTAQIvfltgIEEELSERLPQHMVPTVFFALVHFPTTTSGKTD 2438
Cdd:PRK06814  1061 --HAAVS----IPDARKGERIIlLTTASDATRAAF-----LAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
PRK06188 PRK06188
acyl-CoA synthetase; Validated
2-285 8.38e-08

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 59.23  E-value: 8.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPS-VARLLE--PSH---IPSLRILVMGGEQVNSADW----DRW-PSSVQTingYGPTECCIVCTgYTSEQDF 70
Cdd:PRK06188   255 RITATFLVPTmIYALLDhpDLRtrdLSSLETVYYGASPMSPVRLaeaiERFgPIFAQY---YGQTEAPMVIT-YLRKRDH 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   71 TTGTIG--TSIASVSWVVDPK---DHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINnpAWLlegHggyagrqgr 145
Cdd:PRK06188   331 DPDDPKrlTSCGRPTPGLRVAlldEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRD--GWL---H--------- 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  146 lykTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAV---------E-----VVLPLGQKNHA 211
Cdd:PRK06188   397 ---TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAE-HPAVAQVAVigvpdekwgEavtavVVLRPGAAVDA 472
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  212 T-LAAFIQLDKGTHNAllkekvggddsiarvvflagveeelakrlPKHMvptVFFALLhfPTTTSGKTDRKRLRE 285
Cdd:PRK06188   473 AeLQAHVKERKGSVHA-----------------------------PKQV---DFVDSL--PLTALGKPDKKALRA 513
PRK13382 PRK13382
bile acid CoA ligase;
1934-2444 8.44e-08

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 59.39  E-value: 8.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1934 LFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 2013
Cdd:PRK13382    48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2014 PASRHEDIFRQTGAQVVV----------------TSAQHSARWIGTNHQVvtvsagSLEQFSTLVNPVDLPAKPENAAYV 2077
Cdd:PRK13382   128 AGPALAEVVTREGVDTVIydeefsatvdraladcPQATRIVAWTDEDHDL------TVEVLIAAHAGQRPEPTGRKGRVI 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2078 MFTSGSTGTPKGV-------------VLEH---RA----VVTSCLGHgqAFGVTNLLRALQF-----TAYTFDvciAEII 2132
Cdd:PRK13382   202 LLTSGTTGTPKGArrsgpggigtlkaILDRtpwRAeeptVIVAPMFH--AWGFSQLVLAASLactivTRRRFD---PEAT 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2133 TTLVhggcicvpsDSERrdnlAKAITDMQVNWGYLTSSVARLLDPCLVPSLKVLVLGGEQVNstdwgkwPSSVQTI---- 2208
Cdd:PRK13382   277 LDLI---------DRHR----ATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMR-------PDVVIAFmdqf 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2209 -----NGYGPTECCVFCTG-----YTGIQGFQSGNIGTSIAsvswVVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVD 2278
Cdd:PRK13382   337 gdviyNNYNATEAGMIATAtpadlRAAPDTAGRPAEGTEIR----ILDQD--FREVPTGEVGTIFVRNDTQFDGYTSGST 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2279 KtqaAFiddpawllegypgHEGrqgrLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMrKCLPEANQLAV 2358
Cdd:PRK13382   411 K---DF-------------HDG----FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTL-ATHPDVAEAAV 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2359 EVVPPS--GERdhamLAAFIRLDDETRNSPLIIKyaednstaqivfltgieEELSERLPQHMVPTVFFALVHFPTTTSGK 2436
Cdd:PRK13382   470 IGVDDEqyGQR----LAAFVVLKPGASATPETLK-----------------QHVRDNLANYKVPRDIVVLDELPRGATGK 528

                   ....*...
gi 1820002560 2437 TDRKRLRE 2444
Cdd:PRK13382   529 ILRRELQA 536
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
8282-8514 8.73e-08

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 58.74  E-value: 8.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8282 AFNYPFI-DLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIPRHqdlpfsifevngalaeESQAIHIRDLDQT 8360
Cdd:cd19537     23 SFNVSFAcRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSS----------------PPRVQRVDTLDVW 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8361 SPLGLPtsF-----TLVRNASGMNRLIIRLSHAqydgVC----MPVIWASLASIYQQEPLLSTTgfHSYLAYVHNQRSAS 8431
Cdd:cd19537     87 KEINRP--FdlereDPIRVFISPDTLLVVMSHI----ICdlttLQLLLREVSAAYNGKLLPPVR--REYLDSTAWSRPAS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8432 ---INYWSRLLKGSHITNI--TSKLRPKLGK-------DTTIRSVKveRVIRTpqlpTGLTMASLVSSAWAVVLSHISGE 8499
Cdd:cd19537    159 pedLDFWSEYLSGLPLLNLprRTSSKSYRGTsrvfqlpGSLYRSLL--QFSTS----SGITLHQLALAAVALALQDLSDR 232
                          250
                   ....*....|....*
gi 1820002560 8500 EDVVYGLVVAGRNSD 8514
Cdd:cd19537    233 TDIVLGAPYLNRTSE 247
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
6851-7042 1.01e-07

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 58.89  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVE-GPI-LARGYLNDADKTAAAFvndpawlveghgkhpgrRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKV 6928
Cdd:cd05972    271 PPGEEGDIAIKlPPPgLFLGYVGDPEKTEASI-----------------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKS 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6929 RGQRVELGEIENRLREcMPRATQMAVeVISPagaAEQAKTMVVAFLQLNDEArdallggnvPNDDNLSAQVVfpakvdEK 7008
Cdd:cd05972    334 SGYRIGPFEVESALLE-HPAVAEAAV-VGSP---DPVRGEVVKAFVVLTSGY---------EPSEELAEELQ------GH 393
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1820002560 7009 LSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLR 7042
Cdd:cd05972    394 VKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
4550-5061 1.02e-07

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 59.11  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4550 QARARPDTPAIcAWDGE-------LTYGELDTLSSKLASHLVQLGVKPED-------MVPLcfeksmwTVVAMLA----- 4610
Cdd:cd05966     62 HLKERGDKVAI-IWEGDepdqsrtITYRELLREVCRFANVLKSLGVKKGDrvaiympMIPE-------LVIAMLAcarig 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4611 --------------------------VLKA-----GGAFVPLDP-------DHPASRHEHIFRQTGAQVVlasaqyatlW 4652
Cdd:cd05966    134 avhsvvfagfsaesladrindaqcklVITAdggyrGGKVIPLKEivdealeKCPSVEKVLVVKRTGGEVP---------M 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4653 TSlGRSVV---IVSEASTSQLPVVTKTADPsvnpgnaAYAIFTSGSTGIPKGVVlehkavvtsclghgqafgitdHTR-- 4727
Cdd:cd05966    205 TE-GRDLWwhdLMAKQSPECEPEWMDSEDP-------LFILYTSGSTGKPKGVV---------------------HTTgg 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4728 ----VLQFASYTFDA-------CIAEI--IT-------TLLCCGCICV-----PS--DSDRrnnLAKAINAMDVNWALLT 4780
Cdd:cd05966    256 yllyAATTFKYVFDYhpddiywCTADIgwITghsyivyGPLANGATTVmfegtPTypDPGR---YWDIVEKHKVTIFYTA 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4781 PSVARML-----DPCVVQSLKIL-VLG--GEQVNSADWDRWPKSIqtinayGPTECSICCT---TYSGkqGF-------- 4841
Cdd:cd05966    333 PTAIRALmkfgdEWVKKHDLSSLrVLGsvGEPINPEAWMWYYEVI------GKERCPIVDTwwqTETG--GImitplpga 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4842 ---KSGTIGTSIVSVSWVVDPENHNRLAPLGSiGELLVEG--PILARGYLNDMEKTEAAFiddpawlLEGYGGHsgrqgr 4916
Cdd:cd05966    405 tplKPGSATRPFFGIEPAILDEEGNEVEGEVE-GYLVIKRpwPGMARTIYGDHERYEDTY-------FSKFPGY------ 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4917 lYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE-----HH-VREClteakqlAVeVIVPE---GEGGYamlaAF 4987
Cdd:cd05966    471 -YFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVEsalvaHPaVAEA-------AV-VGRPHdikGEAIY----AF 537
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4988 VQLgddtyntlvkeKAGGDsltvqvvFLDRVEEELAKRV---------PEHMMLTTfftleAMPTTTSGKIDRKRLREIG 5058
Cdd:cd05966    538 VTL-----------KDGEE-------PSDELRKELRKHVrkeigpiatPDKIQFVP-----GLPKTRSGKIMRRILRKIA 594

                   ...
gi 1820002560 5059 ASF 5061
Cdd:cd05966    595 AGE 597
PRK07470 PRK07470
acyl-CoA synthetase; Validated
1935-2114 1.02e-07

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 59.28  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1935 FTEQAKAR-PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpdh 2013
Cdd:PRK07470    12 FLRQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN--- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2014 pasrhediFRQTGAQVVVTSAQHSARWI------------------GTNHQVVTVSAGSLEQFSTLVNPvDLPAKPENAA 2075
Cdd:PRK07470    89 --------FRQTPDEVAYLAEASGARAMichadfpehaaavraaspDLTHVVAIGGARAGLDYEALVAR-HLGARVANAA 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 2076 -------YVMFTSGSTGTPKGVVLEhravvtsclgHGQ-AFGVTNLL 2114
Cdd:PRK07470   160 vdhddpcWFFFTSGTTGRPKAAVLT----------HGQmAFVITNHL 196
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
7630-7773 1.05e-07

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 58.90  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7630 DGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpdhpasrheeiFEQTGAQVVv 7709
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN-----------YNLRGESLA- 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 7710 asaqysarwtssscHVVTVSKALSsqlpAVVDstntsvrpenAAYIIFTSGSTGVPKGVVLEHR 7773
Cdd:cd05940     69 --------------HCLNVSSAKH----LVVD----------AALYIYTSGTTGLPKAAIISHR 104
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
4680-4962 1.09e-07

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 59.29  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4680 SVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTrVLQ--FASYT----FDACIAEIITTLLCCGCI 4753
Cdd:cd05933    146 SQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPAT-VGQesVVSYLplshIAAQILDIWLPIKVGGQV 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4754 C-------------------------VP----------------SDSDRRNNLAKAINA-MDVNWALL-----TPSVARM 4786
Cdd:cd05933    225 YfaqpdalkgtlvktlrevrptafmgVPrvwekiqekmkavgakSGTLKRKIASWAKGVgLETNLKLMggespSPLFYRL 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4787 LDPCVVQSLKiLVLGGEQVNSADWDRWPKSIQTIN-----------AYGPTECSiCCTTYSGKQGFKSGTIGTSIVSVSW 4855
Cdd:cd05933    305 AKKLVFKKVR-KALGLDRCQKFFTGAAPISRETLEfflslnipimeLYGMSETS-GPHTISNPQAYRLLSCGKALPGCKT 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4856 VVDPENHNrlaplgSIGELLVEGPILARGYLNDMEKTEAAfIDDPAWLlegyggHSgrqgrlyktGDLVRYDADGNLVYL 4935
Cdd:cd05933    383 KIHNPDAD------GIGEICFWGRHVFMGYLNMEDKTEEA-IDEDGWL------HS---------GDLGKLDEDGFLYIT 440
                          330       340
                   ....*....|....*....|....*...
gi 1820002560 4936 GR-KDSQVKLRGQRVELGEVEHHVRECL 4962
Cdd:cd05933    441 GRiKELIITAGGENVPPVPIEDAVKKEL 468
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
4141-4407 1.14e-07

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 58.35  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4141 VLELRADVNEDAFRAAWELVVQLTAVLRTRIVQhSELGLLQVVVEE--RIQWTESESLEE---YPredkavsmgvgDRLA 4215
Cdd:cd19537     29 ACRLSGDVDRDRLASAWNTVLARHRILRSRYVP-RDGGLRRSYSSSppRVQRVDTLDVWKeinRP-----------FDLE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4216 RYALIkepydggkRWF------VWTMHHALYDGWSLPRILHAVKQAYSGVVLERQPSFNAFIQYLSQQDPEAAAAYWQTA 4289
Cdd:cd19537     97 REDPI--------RVFispdtlLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWSRPASPEDLDFWSEY 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4290 LVDCKAALFPtlPPTVTQPVADTTVEYQCPPPS-QSATDITTST------LARAAWAIVTSRYTSSDDVVFGATVTGRNA 4362
Cdd:cd19537    169 LSGLPLLNLP--RRTSSKSYRGTSRVFQLPGSLyRSLLQFSTSSgitlhqLALAAVALALQDLSDRTDIVLGAPYLNRTS 246
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 4363 PiaGGEAIVG----PtiatVPVRLRV--QRDQTVFAFLQGVQ---QQAtdmIAH 4407
Cdd:cd19537    247 E--EDMETVGlfleP----LPIRIRFpsSSDASAADFLRAVRrssQAA---LAH 291
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
3484-3978 1.19e-07

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 58.52  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3484 DGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpdhpasrheeiFEQTGAQVVv 3563
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN-----------YNLRGESLA- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3564 asaqysarwtssscHVVTVSKALSsqlpAVVDstntsvrpenAAYIIFTSGSTGVPKGVVLEH-RAV-ATSCLGH-GRAF 3640
Cdd:cd05940     69 --------------HCLNVSSAKH----LVVD----------AALYIYTSGTTGLPKAAIISHrRAWrGGAFFAGsGGAL 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3641 ----------------GITNLSRVL----------QF-ASYTFDACIAEIITTLLCGGCIC------VPSDSDRRNSLAK 3687
Cdd:cd05940    121 psdvlytclplyhstaLIVGWSACLasgatlvirkKFsASNFWDDIRKYQATIFQYIGELCryllnqPPKPTERKHKVRM 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3688 AISTmdvnwafltpsvarlldpGLIPSLkilaiggeqsssadWNRWPGSVQKIHV---YGPTECCIFCTGYTTKQ---GF 3761
Cdd:cd05940    201 IFGN------------------GLRPDI--------------WEEFKERFGVPRIaefYAATEGNSGFINFFGKPgaiGR 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3762 EPStIGTSVASVSWV-VDPENHNRL---------APLGSMGELLMEGPILAR--GYLNDVDKTEA----AFIDDPAWlle 3825
Cdd:cd05940    249 NPS-LLRKVAPLALVkYDLESGEPIrdaegrcikVPRGEPGLLISRINPLEPfdGYTDPAATEKKilrdVFKKGDAW--- 324
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3826 gypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVR--ECLPEARQLAVEVilpSGQKDHAM 3903
Cdd:cd05940    325 ------------FNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGafPGVEEANVYGVQV---PGTDGRAG 389
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 3904 LAafvqleegtqnALLDKEAGGEDsmaqvvfLASVEEELAKRLPEHMVPtVFFSLL-HFPTTTSGKTDRKRLREIG 3978
Cdd:cd05940    390 MA-----------AIVLQPNEEFD-------LSALAAHLEKNLPGYARP-LFLRLQpEMEITGTFKQQKVDLRNEG 446
PRK03584 PRK03584
acetoacetate--CoA ligase;
5628-5787 1.21e-07

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 59.04  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5628 FTEQA--KARPHAPAICAW--DG---ELTYGELDALSSKLAGHLTQLGVKPED----MVPLCFEksmwTVVAMLAVLKAG 5696
Cdd:PRK03584    88 YAENLlrHRRDDRPAIIFRgeDGprrELSWAELRRQVAALAAALRALGVGPGDrvaaYLPNIPE----TVVAMLATASLG 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5697 GAFVPLDPDHPASRHEDTFRHTGAQVVVTSAQHsaRWIGTNHQVVTVSAGSLGQLSTLVNPVGLP--------AIPENAV 5768
Cdd:PRK03584   164 AIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGY--RYGGKAFDRRAKVAELRAALPSLEHVVVVPylgpaaaaAALPGAL 241
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 5769 -------------------------YIMFTSGSTGIPK-------GVVLEH 5787
Cdd:PRK03584   242 lwedflapaeaaelefepvpfdhplWILYSSGTTGLPKcivhghgGILLEH 292
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
7067-7135 1.21e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 53.02  E-value: 1.21e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  7067 PSTEAERTMQQL----WARMLKVK-ADSIGLDDSFFRLGGDSIVAMKLVGE-ARRTGLQLSVADVFRHPRLVDLA 7135
Cdd:smart00823    5 PPAERRRLLLDLvreqVAAVLGHAaAEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALA 79
PRK07867 PRK07867
acyl-CoA synthetase; Validated
5680-6139 1.23e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 58.92  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5680 EKSMWTVVAMLAvlkaGGAFVPLDPDHPASRHEDTFRHTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLGQLSTLVNPVG 5759
Cdd:PRK07867    66 EFSLLLGAAALS----GIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRD 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5760 LPAIPENA-----VYIMFTSGSTGIPKGVVLEHRAVVTScwGRGRA--FGITN-----LSRVLqFASytfDACMDEIITT 5827
Cdd:PRK07867   142 AEPPFRVAdpddlFMLIFTSGTSGDPKAVRCTHRKVASA--GVMLAqrFGLGPddvcyVSMPL-FHS---NAVMAGWAVA 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5828 LMYGGCICVP---SDSD-----RR------NDLVKAISTMdvscaLLTPSvarllEPSSVP-TLQMLVlqGEQVSFADWN 5892
Cdd:PRK07867   216 LAAGASIALRrkfSASGflpdvRRygatyaNYVGKPLSYV-----LATPE-----RPDDADnPLRIVY--GNEGAPGDIA 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5893 RWPA--SVQTINGYGPTECSIccnTYSGKQGFKSGIIGTSVASVSwVVDPE-----------NHDRLAPLGSIGELL-VE 5958
Cdd:PRK07867   284 RFARrfGCVVVDGFGSTEGGV---AITRTPDTPPGALGPLPPGVA-IVDPDtgtecppaedaDGRLLNADEAIGELVnTA 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5959 GPILARGYLNDIQKTAAVFiddpawllegypghpgRQGRlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHH 6038
Cdd:PRK07867   360 GPGGFEGYYNDPEADAERM----------------RGGV-YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERI 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6039 VREcLPEARQLAVEVILPSGQKDHAMLAafVQLEEGtqnALLDKEASGEdsmaqvvFLASvEEELAKRlpehMVPTVFFS 6118
Cdd:PRK07867   423 LLR-YPDATEVAVYAVPDPVVGDQVMAA--LVLAPG---AKFDPDAFAE-------FLAA-QPDLGPK----QWPSYVRV 484
                          490       500
                   ....*....|....*....|.
gi 1820002560 6119 LLHFPTTTSGKTDRKRLREIG 6139
Cdd:PRK07867   485 CAELPRTATFKVLKRQLSAEG 505
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
7625-7986 1.34e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 58.76  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7625 AICAWDGE-LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdhpaSRH---EE-- 7698
Cdd:PRK08276     3 VIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI------NWHltaAEia 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7699 -IFEQTGAQVVVASAQYSArwtssschvvtVSKALSSQLPA------VVDSTNTSVRP-ENA---------------AYI 7755
Cdd:PRK08276    77 yIVDDSGAKVLIVSAALAD-----------TAAELAAELPAgvplllVVAGPVPGFRSyEEAlaaqpdtpiadetagADM 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7756 IFTSGSTGVPKGVV--LEHRAVATSCLGH----GRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRN 7829
Cdd:PRK08276   146 LYSSGTTGRPKGIKrpLPGLDPDEAPGMMlallGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEE 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7830 SLAkAISTMDVNWAFLTPSV-ARLL----------DpglIPSLKiLAIGGEQSSSADWNR----WPGSVqkIH-VYGPTE 7893
Cdd:PRK08276   226 ALA-LIERYRVTHSQLVPTMfVRMLklpeevraryD---VSSLR-VAIHAAAPCPVEVKRamidWWGPI--IHeYYASSE 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7894 CCIFcTGYTTKQGFE-PSTIGTSVASVSWVVDpENHNRLAPlGSMGELLMEGPILARGYLNDVDKTEAAFIDDpAWLLEG 7972
Cdd:PRK08276   299 GGGV-TVITSEDWLAhPGSVGKAVLGEVRILD-EDGNELPP-GEIGTVYFEMDGYPFEYHNDPEKTAAARNPH-GWVTVG 374
                          410
                   ....*....|....
gi 1820002560 7973 YPGHPGRQGRLYKT 7986
Cdd:PRK08276   375 DVGYLDEDGYLYLT 388
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
4000-4069 1.36e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 52.64  E-value: 1.36e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560  4000 PSTEAEQTMQQL----WAQVLSL-GADIIGLDDSFFRLGGDSIAAMKLVGE-ARRMGLHLSVADIFRHPKLADFAG 4069
Cdd:smart00823    5 PPAERRRLLLDLvreqVAAVLGHaAAEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALAE 80
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
6851-7043 1.39e-07

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 58.62  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFVNDpawlveGhgkhpgrrgrLYKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:COG1021    376 PPGEVGELLTRGPYTIRGYYRAPEHNARAFTPD------G----------FYRTGDLVRRTPDGYLVVEGRAKDQINRGG 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6931 QRVELGEIENRLRECmPRATQMAvevispagaaeqaktmVVAFlqlndeaRDALLGGN-----VPNDDNLSaqvvfPAKV 7005
Cdd:COG1021    440 EKIAAEEVENLLLAH-PAVHDAA----------------VVAM-------PDEYLGERscafvVPRGEPLT-----LAEL 490
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1820002560 7006 DEKLSNL-LPSYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:COG1021    491 RRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
855-1365 1.44e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 58.47  E-value: 1.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  855 HDLFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDP 934
Cdd:PRK13383    38 YTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  935 GhpasrheeiFKQIGAQVVLTSSQHAMLFASSE-RHQVTVSKVSTSQL-PTVVNFAKSPVDPGNTA---YIIFTSGTTGI 1009
Cdd:PRK13383   118 E---------FRSDALAAALRAHHISTVVADNEfAERIAGADDAVAVIdPATAGAEESGGRPAVAApgrIVLLTSGTTGK 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1010 PKGVvlqHRAVTTSClGHGEAFGYTDHARV-----LQFASYTFDAC-IAEIITTLLYGGCICVPSESDRRNNLAKAiSTM 1083
Cdd:PRK13383   189 PKGV---PRAPQLRS-AVGVWVTILDRTRLrtgsrISVAMPMFHGLgLGMLMLTIALGGTVLTHRHFDAEAALAQA-SLH 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1084 DVNCALLTPSV-ARLLE-PSAV------PSLKRLVLQGEQVSFADWNRWPGSVQTI--NGYGPTECSVCCNTYSGKQGFK 1153
Cdd:PRK13383   264 RADAFTAVPVVlARILElPPRVrarnplPQLRVVMSSGDRLDPTLGQRFMDTYGDIlyNGYGSTEVGIGALATPADLRDA 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1154 SGIIGTSVASLSWVVDAGNHNRLAPlgsigelLVEGPILARGYLNDidkteaafiddpawllEGYEGHAGRR--GRLYKT 1231
Cdd:PRK13383   344 PETVGKPVAGCPVRILDRNNRPVGP-------RVTGRIFVGGELAG----------------TRYTDGGGKAvvDGMTST 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1232 GDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVrECLPEARQLAVeVILPSGQKEHAlLAAFIQLDKGnhnalfe 1311
Cdd:PRK13383   401 GDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENAL-AAHPAVADNAV-IGVPDERFGHR-LAAFVVLHPG------- 470
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 1312 ekaSGEDSMAqvvfltgVEEELAKRLPEHMVPTILFTVKAMPITTSGKIDRKRL 1365
Cdd:PRK13383   471 ---SGVDAAQ-------LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
6706-6807 1.50e-07

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 58.74  E-value: 1.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6706 DLFTEQALARPNAPAVCAWDGE--LTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 6783
Cdd:PRK05852    20 DLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLD 99
                           90       100
                   ....*....|....*....|....
gi 1820002560 6784 PDHPASRHEDILRQTGAQVILASA 6807
Cdd:PRK05852   100 PALPIAEQRVRSQAAGARVVLIDA 123
PRK09192 PRK09192
fatty acyl-AMP ligase;
4567-4718 1.52e-07

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 58.48  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQvvLASA 4646
Cdd:PRK09192    50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIAQLRGM--LASA 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4647 QYATLWTSLGrSVVIVSEASTSQLPVVTKTAD------------PSVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCL 4714
Cdd:PRK09192   128 QPAAIITPDE-LLPWVNEATHGNPLLHVLSHAwfkalpeadvalPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLR 206

                   ....
gi 1820002560 4715 GHGQ 4718
Cdd:PRK09192   207 AISH 210
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
63-285 1.54e-07

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 58.74  E-value: 1.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   63 GYTSEQDFTTGTIGTSIASVSWVVDPkDHGRLAPlGSVGELLVEGPILARGYLSDPEKTAAVFINnpAWLleghggyagr 142
Cdd:PRK05852   345 GQTENPVVSTGLVGRSTGAQIRIVGS-DGLPLPA-GAVGEVWLRGTTVVRGYLGDPTITAANFTD--GWL---------- 410
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  143 qgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVElgevehhvreclPEAkqlaVEVVLPlGQKNHATLAAFiqldkG 222
Cdd:PRK05852   411 -----RTGDLGSLSAAGDLSIRGRIKELINRGGEKIS------------PER----VEGVLA-SHPNVMEAAVF-----G 463
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  223 THNALLKEKVGGddSIARVVFLAGVEEELA----KRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:PRK05852   464 VPDQLYGEAVAA--VIVPRESAPPTAEELVqfcrERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
PRK07787 PRK07787
acyl-CoA synthetase; Validated
10-184 1.56e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 58.46  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   10 PSVARLLEPShipslRILVMGGEQVNSADWDRWPSSV--QTINGYGPTECCIVcTGYTSEQDFTTGTIGTSIASV-SWVV 86
Cdd:PRK07787   234 PEAARALRGA-----RLLVSGSAALPVPVFDRLAALTghRPVERYGMTETLIT-LSTRADGERRPGWVGLPLAGVeTRLV 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   87 DpkDHGRLAPLG--SVGELLVEGPILARGYLSDPEKTAAVFINNpAWlleghggyagrqgrlYKTGDLVRYDADGNLVCL 164
Cdd:PRK07787   308 D--EDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTAD-GW---------------FRTGDVAVVDPDGMHRIV 369
                          170       180
                   ....*....|....*....|.
gi 1820002560  165 GRKDSQ-VKLRGQRVELGEVE 184
Cdd:PRK07787   370 GRESTDlIKSGGYRIGAGEIE 390
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
51-184 1.62e-07

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 58.31  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   51 GYGPTECCIVCTgYTSEQDFTTGTIGTSIASVSW-VVDPkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVfINNP 129
Cdd:cd17642    333 GYGLTETTSAIL-ITPEGDDKPGAVGKVVPFFYAkVVDL-DTGKTLGPNERGELCVKGPMIMKGYVNNPEATKAL-IDKD 409
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  130 AWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVE 184
Cdd:cd17642    410 GWL---------------HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELE 449
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
875-1076 1.73e-07

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 58.21  E-value: 1.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  875 DGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAG--GAFVPLDPGHPASRHeeifkqigaqV 952
Cdd:cd05939      1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGveTALINSNLRLESLLH----------C 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  953 VLTSSQHAMLFasseRHQVTVSKVSTSQLPTVVnfaksPVDPGNTAYIIFTSGTTGIPKGVV------------------ 1014
Cdd:cd05939     71 ITVSKAKALIF----NLLDPLLTQSSTEPPSQD-----DVNFRDKLFYIYTSGTTGLPKAAVivhsryyriaagayyafg 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1015 ------------LQHRAVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCIC------VPSESDRRNNL 1076
Cdd:cd05939    142 mrpedvvydclpLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICryllaqPPSEEEQKHNV 221
PRK03584 PRK03584
acetoacetate--CoA ligase;
7613-7772 1.77e-07

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 58.65  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7613 FAEQA--RARPGAPAICAW--DG---ELTYGELDVLSSNLAGHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAG 7681
Cdd:PRK03584    88 YAENLlrHRRDDRPAIIFRgeDGprrELSWAELRRQVAALAAALRALGVGPGDRVaaylPNIPE----TVVAMLATASLG 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7682 GAFVPLDPDHPASRHEEIFEQTGAQVVVASA--QYSARWTSSSCHVVTVSKALSSQLPAVV----DSTNTSVRPENAA-- 7753
Cdd:PRK03584   164 AIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyRYGGKAFDRRAKVAELRAALPSLEHVVVvpylGPAAAAAALPGALlw 243
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 7754 -----------------------YIIFTSGSTGVPK-------GVVLEH 7772
Cdd:PRK03584   244 edflapaeaaelefepvpfdhplWILYSSGTTGLPKcivhghgGILLEH 292
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
18-361 1.77e-07

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 58.50  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   18 PSHIPSLRILVMGGEQVNSADWDR---WPSSVQTINGYGPTEccivcTGYT----SEQDFTTGTIGTSIASVSWVVDPKD 90
Cdd:PRK06060   256 PDSFRSLRCVVSAGEALELGLAERlmeFFGGIPILDGIGSTE-----VGQTfvsnRVDEWRLGTLGRVLPPYEIRVVAPD 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   91 hGRLAPLGSVGELLVEGPILARGYLSDPEKtaavFINNPAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQ 170
Cdd:PRK06060   331 -GTTAGPGVEGDLWVRGPAIAKGYWNRPDS----PVANEGWL---------------DTRDRVCIDSDGWVTYRCRADDT 390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  171 VKLRGQRVELGEVEHHVRECLPEAKQLAVEVVLPLGQknhATLAAFIQLDKGThnallkekvGGDDSIARvvflaGVEEE 250
Cdd:PRK06060   391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGA---STLQAFLVATSGA---------TIDGSVMR-----DLHRG 453
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  251 LAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREIGASFTAQQLAEMRTSSQGPKR-----------QPSTEAERTMQQ 319
Cdd:PRK06060   454 LLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSGVRAQrddlsasnmtiAGGNDGGATLRE 533
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560  320 LWA-------------------RVLGiEPD--SIGLDDSFFRLGGDSIAAIKLVGE-ARRTGLQ 361
Cdd:PRK06060   534 RLValrqerqrlvvdavcaeaaKMLG-EPDpwSVDQDLAFSELGFDSQMTVTLCKRlAAVTGLR 596
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
19-155 1.77e-07

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 58.29  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   19 SHIPSLRILVMGGEQVNSADWD---RWPSSVQTINGYGPTECCIVCTGYTSEQDFTTGTIGTSIASVSWVVDPKDHGRLA 95
Cdd:PRK06334   296 SCLPSLRFVVIGGDAFKDSLYQealKTFPHIQLRQGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVPV 375
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   96 PLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAWLLEGHGGYAGRQGRLYKTGDLVRY 155
Cdd:PRK06334   376 SSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRF 435
PRK05850 PRK05850
acyl-CoA synthetase; Validated
1933-2101 1.85e-07

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 58.42  E-value: 1.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1933 DLFTEQAKARPHAPAIC------AWDG---ELTYGELDALSSKLASHLVQLGVnPEDVVPLCFEKSMWTVVAMLAVLKAG 2003
Cdd:PRK05850     5 SLLRERASLQPDDAAFTfidyeqDPAGvaeTLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2004 GAFVPLDPDHPASRHEDI---FRQTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLEQFSTL-----VNPVDLPAKPENAA 2075
Cdd:PRK05850    84 LIAVPLSVPQGGAHDERVsavLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLdldspRGSDARPRDLPSTA 163
                          170       180
                   ....*....|....*....|....*.
gi 1820002560 2076 YVMFTSGSTGTPKGVVLEHRAVVTSC 2101
Cdd:PRK05850   164 YLQYTSGSTRTPAGVMVSHRNVIANF 189
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
4680-4955 1.93e-07

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 58.29  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4680 SVNPGNAAYAIFTSGSTGIPKGVVLEHKAVVT---SCLghgQAFGITDHTRVLQFA----SYTFDACIaeiITTLLCCGC 4752
Cdd:PRK06334   179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLAnqrACL---KFFSPKEDDVMMSFLppfhAYGFNSCT---LFPLLSGVP 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4753 ICVPSDSDRRNNLAKAINAMDVNWALLTP-------SVARMLDPCVvQSLKILVLGGEQVNSADWDRWPKS---IQTINA 4822
Cdd:PRK06334   253 VVFAYNPLYPKKIVEMIDEAKVTFLGSTPvffdyilKTAKKQESCL-PSLRFVVIGGDAFKDSLYQEALKTfphIQLRQG 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4823 YGPTECSICCTTYSGKQGFKSGTIGTSIVSVSWVVDPENHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDPAW 4902
Cdd:PRK06334   332 YGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGETW 411
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 4903 llegygghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE 4955
Cdd:PRK06334   412 ---------------YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALE 449
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
85-285 1.95e-07

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 58.40  E-value: 1.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   85 VVDPkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNPAwllEGHGGYagrqgrlYKTGDLVRYdADGNLVCL 164
Cdd:cd05931    368 IVDP-ETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAA---TDEGGW-------LRTGDLGFL-HDGELYIT 435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  165 GRKDSQVKLRGQRVELGEVEHHVRECLPEAKQLAVevvlplgqknhatlAAF-IQLDKGTHNALLKEKVGGDDSIARVVF 243
Cdd:cd05931    436 GRLKDLIIVRGRNHYPQDIEATAEEAHPALRPGCV--------------AAFsVPDDGEERLVVVAEVERGADPADLAAI 501
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560  244 LAGVEEELAKRlpkHMVPTVFFALL---HFPTTTSGKTDRKRLRE 285
Cdd:cd05931    502 AAAIRAAVARE---HGVAPADVVLVrpgSIPRTSSGKIQRRACRA 543
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
992-1369 1.96e-07

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 58.21  E-value: 1.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  992 VDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDHARVLQ-FASYTFDACIAEIITTLLYGGCIC----- 1065
Cdd:cd05937     84 VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTcMPLYHGTAAFLGACNCLMSGGTLAlsrkf 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1066 ---------VPSESDR--------RNNLAKAISTMD----VNCAL---LTPSV-ARLLEPSAVPSLKRLVLQGEQVsFAD 1120
Cdd:cd05937    164 sasqfwkdvRDSGATIiqyvgelcRYLLSTPPSPYDrdhkVRVAWgngLRPDIwERFRERFNVPEIGEFYAATEGV-FAL 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1121 WNRwpgsvqtingygptecsvccntysGKQGFKSGIIGTSVASLSW------VVDAGNHN-------------RLAPLGS 1181
Cdd:cd05937    243 TNH------------------------NVGDFGAGAIGHHGLIRRWkfenqvVLVKMDPEtddpirdpktgfcVRAPVGE 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1182 IGELLVEGPILAR----GYLNDIDKTEAAFIDDpawllegyeghAGRRGRLY-KTGDLVRCDADGNLVCLGRKDSQVKVR 1256
Cdd:cd05937    299 PGEMLGRVPFKNReafqGYLHNEDATESKLVRD-----------VFRKGDIYfRTGDLLRQDADGRWYFLDRLGDTFRWK 367
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1257 GQRVELGEIEHHVRECLPEARQLAVEVILPsGQKEHALLAAfIQLdKGNHNALFEEKASGEDSMAQvvfltgveeelaKR 1336
Cdd:cd05937    368 SENVSTTEVADVLGAHPDIAEANVYGVKVP-GHDGRAGCAA-ITL-EESSAVPTEFTKSLLASLAR------------KN 432
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1820002560 1337 LPEHMVPTILFTVKAMPITTSGKIDRKRLQDIG 1369
Cdd:cd05937    433 LPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEG 465
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
999-1362 2.03e-07

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 57.03  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  999 YIIFTSGTTGIPKGVVLQHR--AVTTSCLGHGEAFGYTDhaRVLQFASYTFDACIAEIITTLLYGGCICVPSESDRRNNL 1076
Cdd:cd17633      4 YIGFTSGTTGLPKAYYRSERswIESFVCNEDLFNISGED--AILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1077 AKaISTMDVNCALLTPSVARLLEPSAVPSLK-RLVLQGEQVSFADW-----NRWPGSVqTINGYGPTECSVC---CNTYS 1147
Cdd:cd17633     82 RK-INQYNATVIYLVPTMLQALARTLEPESKiKSIFSSGQKLFESTkkklkNIFPKAN-LIEFYGTSELSFItynFNQES 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1148 GKQGfksgiigtSVASLSWVVDAGNHNrlAPLGSIGELLVEGPILARGYLndidktEAAFIDDPAWllegyeghagrrgr 1227
Cdd:cd17633    160 RPPN--------SVGRPFPNVEIEIRN--ADGGEIGKIFVKSEMVFSGYV------RGGFSNPDGW-------------- 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1228 lYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVREClpEARQLAVEVILPSgQKEHALLAAFIQLDKGNHN 1307
Cdd:cd17633    210 -MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAI--PGIEEAIVVGIPD-ARFGEIAVALYSGDKLTYK 285
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 1308 ALfeekasgedsmaqvvfltgvEEELAKRLPEHMVPTILFTVKAMPITTSGKIDR 1362
Cdd:cd17633    286 QL--------------------KRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
4566-5055 2.32e-07

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 57.77  E-value: 2.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4566 ELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLAS 4645
Cdd:PRK08008    37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4646 AQYATLWTSLGRS-------VVIVSEASTSQLPVVTKTADPSVNPGNAAYA-----------IFTSGSTGIPKGVVLEHK 4707
Cdd:PRK08008   117 AQFYPMYRQIQQEdatplrhICLTRVALPADDGVSSFTQLKAQQPATLCYApplstddtaeiLFTSGTTSRPKGVVITHY 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4708 AVVTSclGHGQAF--GITDHTRVLQ-FASYTFD-ACIAEIITTLLCCGCICVPSDSDR---------RNNLAKAInAMDV 4774
Cdd:PRK08008   197 NLRFA--GYYSAWqcALRDDDVYLTvMPAFHIDcQCTAAMAAFSAGATFVLLEKYSARafwgqvckyRATITECI-PMMI 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4775 NWALLTPSVARMLDPCVVQSLKILVLGgEQVNSADWDRWpkSIQTINAYGPTEC--SICCTTYSGKQGFKSgtIGTSIVS 4852
Cdd:PRK08008   274 RTLMVQPPSANDRQHCLREVMFYLNLS-DQEKDAFEERF--GVRLLTSYGMTETivGIIGDRPGDKRRWPS--IGRPGFC 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4853 VSWVVDPENHNRLAPlGSIGELLVEG---PILARGYLNDMEKTEAAFIDDpAWLlegygghsgrqgrlyKTGDLVRYDAD 4929
Cdd:PRK08008   349 YEAEIRDDHNRPLPA-GEIGEICIKGvpgKTIFKEYYLDPKATAKVLEAD-GWL---------------HTGDTGYVDEE 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4930 GNLVYLGRKDSQVKLRGQRVELGEVEHHVrecLTEAKQLAVEVI-VPEGEGGYAmLAAFVQLGDdtyntlvkekagGDSL 5008
Cdd:PRK08008   412 GFFYFVDRRCNMIKRGGENVSCVELENII---ATHPKIQDIVVVgIKDSIRDEA-IKAFVVLNE------------GETL 475
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560 5009 TVQVvFLDRVEEELAK-RVPEHMMLTTFFtleamPTTTSGKIDRKRLR 5055
Cdd:PRK08008   476 SEEE-FFAFCEQNMAKfKVPSYLEIRKDL-----PRNCSGKIIKKNLK 517
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
4136-4439 2.37e-07

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 57.66  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4136 YIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSELGLlQVVVEE-----RIQWTESESLEEYPREDKAVSMgv 4210
Cdd:cd19538     24 YNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPY-QLILEEdeatpKLEIKEVDEEELESEINEAVRY-- 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4211 gdrlaRYALIKEP--------YDGGKRWFVWTMHHALYDGWSLPRILHAVKQAYSGVVLERQPSFNAF-IQY----LSQQ 4277
Cdd:cd19538    101 -----PFDLSEEPpfratlfeLGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLpVQYadyaLWQQ 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4278 -------DPEAAAA----YWQTALvdckaALFPTLPPTVTqpvadttvEYQCPPPSQSATDITT-----------STLAR 4335
Cdd:cd19538    176 ellgdesDPDSLIArqlaYWKKQL-----AGLPDEIELPT--------DYPRPAESSYEGGTLTfeidselhqqlLQLAK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4336 -----------AAWAIVTSRYTSSDDVVFGATVTGRNApiAGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQATDM 4404
Cdd:cd19538    243 dnnvtlfmvlqAGFAALLTRLGAGTDIPIGSPVAGRND--DSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEA 320
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1820002560 4405 IAHEQTGLQRIAK-MSP---GARHACgFQTLLVVQPTDD 4439
Cdd:cd19538    321 YEHQDIPFERLVEaLNPtrsRSRHPL-FQIMLALQNTPQ 358
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
4568-5056 2.41e-07

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 57.88  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4568 TYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDhpaSRHEHIFRQTgaqvvlasaq 4647
Cdd:cd05908     17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIG---SNEEHKLKLN---------- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4648 yaTLWTSLGRSVVIVSEASTSQlpvvtktadpsvNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTR 4727
Cdd:cd05908     84 --KVWNTLKNPYLITEEEVLCE------------LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4728 VLQFASYTFDACIAEIITTLLCCGC----------ICVPSDSDRRNNLAKAINAMDVNWA------LLTPSVARMLDpcv 4791
Cdd:cd05908    150 ILSWMPLTHDMGLIAFHLAPLIAGMnqylmptrlfIRRPILWLKKASEHKATIVSSPNFGykyflkTLKPEKANDWD--- 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4792 VQSLKILVLGGEQVNSADWDRWPKSIQT--------INAYGPTECSICCTTYSGKQGFKSGTI----------------- 4846
Cdd:cd05908    227 LSSIRMILNGAEPIDYELCHEFLDHMSKyglkrnaiLPVYGLAEASVGASLPKAQSPFKTITLgrrhvthgepepevdkk 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4847 ---GTSIVSVSWVVDP------ENHNRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDDpAWLlegygghsgrqgrl 4917
Cdd:cd05908    307 dseCLTFVEVGKPIDEtdiricDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDD-GWL-------------- 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4918 yKTGDL--VRydaDGNLVYLGRKDSQVKLRGQRVELGEVEhhvreclteakQLAVEVIvPEGEGGYAMLAAFvqlgddty 4995
Cdd:cd05908    372 -KTGDLgfIR---NGRLVITGREKDIIFVNGQNVYPHDIE-----------RIAEELE-GVELGRVVACGVN-------- 427
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 4996 ntlvKEKAGGDSLTVQVVFLDRVEE--ELAKRVPEHM------MLTTFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:cd05908    428 ----NSNTRNEEIFCFIEHRKSEDDfyPLGKKIKKHLnkrggwQINEVLPIRRIPKTTSGKVKRYELAQ 492
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
21-279 2.43e-07

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 57.39  E-value: 2.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   21 IPSLRILVMGG----EQVNSADWDRWPSSVqTINGYGPTECCIVCTGYTSEQDFTTGTIgTSIASVSWVVDpkDHGRLAP 96
Cdd:cd05924    133 LSSLFAISSGGallsPEVKQGLLELVPNIT-LVDAFGSSETGFTGSGHSAGSGPETGPF-TRANPDTVVLD--DDGRVVP 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   97 LGS--VGELLVEGPIlARGYLSDPEKTAAVF--INNPAWLLeghggyagrqgrlykTGDLVRYDADGNLVCLGRKDSQVK 172
Cdd:cd05924    209 PGSggVGWIARRGHI-PLGYYGDEAKTAETFpeVDGVRYAV---------------PGDRATVEADGTVTLLGRGSVCIN 272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  173 LRGQRVELGEVEHHVReclpeaKQLAVEVVLPLGQKNH---ATLAAFIQLDKgthnallkekvGGDDSIARVVflAGVEE 249
Cdd:cd05924    273 TGGEKVFPEEVEEALK------SHPAVYDVLVVGRPDErwgQEVVAVVQLRE-----------GAGVDLEELR--EHCRT 333
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1820002560  250 ELAK-RLPKHM--VPTVffallhfPTTTSGKTD 279
Cdd:cd05924    334 RIARyKLPKQVvfVDEI-------ERSPAGKAD 359
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
7592-8021 2.48e-07

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 57.76  E-value: 2.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7592 QQLWAWN--ADVPPAIE----RCVHDLFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLV-QLGVNPEDVVPLCF 7664
Cdd:PRK08974     2 EKVWLNRypADVPAEINpdryQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7665 EKSMWTVVAMLAVLKAGGAFVPLDP-------DHP---------------ASRHEEIFEQTGAQVVVASA---QYSARWT 7719
Cdd:PRK08974    82 PNLLQYPIALFGILRAGMIVVNVNPlytprelEHQlndsgakaivivsnfAHTLEKVVFKTPVKHVILTRmgdQLSTAKG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7720 SSSCHVVTVSKALSSQ--LPAVVDSTNT--------SVRP----ENAAYIIFTSGSTGVPKGVVLEHR----------AV 7775
Cdd:PRK08974   162 TLVNFVVKYIKRLVPKyhLPDAISFRSAlhkgrrmqYVKPelvpEDLAFLQYTGGTTGVAKGAMLTHRnmlanleqakAA 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7776 ATSCLGHGRAFGITNLSRVLQFAsYTFDaCIAEI---ITTLLcggcICVPSDSDRR-NSLAK----AIStmDVNWAF--- 7844
Cdd:PRK08974   242 YGPLLHPGKELVVTALPLYHIFA-LTVN-CLLFIelgGQNLL----ITNPRDIPGFvKELKKypftAIT--GVNTLFnal 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7845 LTPSVARLLDpglIPSLKiLAIGGE---QSSSADwnRWPgSVQKIHV---YGPTECCIFCTGYTTKQGFEPSTIGTSVAS 7918
Cdd:PRK08974   314 LNNEEFQELD---FSSLK-LSVGGGmavQQAVAE--RWV-KLTGQYLlegYGLTECSPLVSVNPYDLDYYSGSIGLPVPS 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7919 VS-WVVDPENHNrlAPLGSMGELLMEGPILARGYLNDVDKTeAAFIDDpAWLlegypghpgrqgrlyKTGDLVQYNADGN 7997
Cdd:PRK08974   387 TEiKLVDDDGNE--VPPGEPGELWVKGPQVMLGYWQRPEAT-DEVIKD-GWL---------------ATGDIAVMDEEGF 447
                          490       500
                   ....*....|....*....|....
gi 1820002560 7998 LVYLGRKDSQVKVRGQRVELGEVE 8021
Cdd:PRK08974   448 LRIVDRKKDMILVSGFNVYPNEIE 471
PRK13382 PRK13382
bile acid CoA ligase;
857-1367 2.50e-07

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 57.85  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  857 LFAEQARARPDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGH 936
Cdd:PRK13382    48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  937 PASRHEEIFKQIGAQVVLTSSQHAMLFA---------------SSERHQVTVSKVSTSQLptvvnfAKSPVDPGNTA-YI 1000
Cdd:PRK13382   128 AGPALAEVVTREGVDTVIYDEEFSATVDraladcpqatrivawTDEDHDLTVEVLIAAHA------GQRPEPTGRKGrVI 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1001 IFTSGTTGIPKG------------------VVLQHRAVTTSCLGHGEAFGYTDharvLQFASY---------TFD--ACI 1051
Cdd:PRK13382   202 LLTSGTTGTPKGarrsgpggigtlkaildrTPWRAEEPTVIVAPMFHAWGFSQ----LVLAASlactivtrrRFDpeATL 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1052 AEIITTLLYGGCIcVPSESDRrnnlakaisTMDVncalltpsVARLLEPSAVPSLKRLVLQGE----QVSFADWNRWpGS 1127
Cdd:PRK13382   278 DLIDRHRATGLAV-VPVMFDR---------IMDL--------PAEVRNRYSGRSLRFAAASGSrmrpDVVIAFMDQF-GD 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1128 VqTINGYGPTECSVCC-----------NTySGKQGfksgiIGTSVAslswVVDAgNHNRLaPLGSIGELLVEGPILARGY 1196
Cdd:PRK13382   339 V-IYNNYNATEAGMIAtatpadlraapDT-AGRPA-----EGTEIR----ILDQ-DFREV-PTGEVGTIFVRNDTQFDGY 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1197 LNDIDKteaafiddpawllegyEGHAGrrgrLYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEhHVRECLPEA 1276
Cdd:PRK13382   406 TSGSTK----------------DFHDG----FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVE-KTLATHPDV 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1277 RQLAVEVILPS--GQKehalLAAFIQLDKGnhNALFEEKASGEdsmaqvvfltgVEEELAKrlpeHMVPTILFTVKAMPI 1354
Cdd:PRK13382   465 AEAAVIGVDDEqyGQR----LAAFVVLKPG--ASATPETLKQH-----------VRDNLAN----YKVPRDIVVLDELPR 523
                          570
                   ....*....|...
gi 1820002560 1355 TTSGKIDRKRLQD 1367
Cdd:PRK13382   524 GATGKILRRELQA 536
PRK07470 PRK07470
acyl-CoA synthetase; Validated
858-1232 2.67e-07

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 57.74  E-value: 2.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  858 FAEQARAR-PDASAVCAWDGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpgh 936
Cdd:PRK07470    12 FLRQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN--- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  937 pasrheeiFKQIGAQVVL---TSSQHAMLFASSERHQVTVSKVSTSQLPTVVNFAKSP---------------------V 992
Cdd:PRK07470    89 --------FRQTPDEVAYlaeASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARagldyealvarhlgarvanaaV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  993 DPGNTAYIIFTSGTTGIPKGVVLQHravttsclgHGEAF-----------GYTDHARVLQFASYTFDACIAEIITTLLYG 1061
Cdd:PRK07470   161 DHDDPCWFFFTSGTTGRPKAAVLTH---------GQMAFvitnhladlmpGTTEQDASLVVAPLSHGAGIHQLCQVARGA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1062 GCICVPSESDRRNNLAKAISTMDVNCALLTPSVARLL-EPSAV-----PSLKRLVLQGEQVSFADWNR-----WPGSVQT 1130
Cdd:PRK07470   232 ATVLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLvEHPAVdrydhSSLRYVIYAGAPMYRADQKRalaklGKVLVQY 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1131 ingYGPTECSVCC--------------NTYSGKQGFKSgiIGTSVASLSwvvDAGnhnRLAPLGSIGELLVEGPILARGY 1196
Cdd:PRK07470   312 ---FGLGEVTGNItvlppalhdaedgpDARIGTCGFER--TGMEVQIQD---DEG---RELPPGETGEICVIGPAVFAGY 380
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1820002560 1197 LNDIDKTEAAFIDDpaWLLEGYEGHAGRRGRLYKTG 1232
Cdd:PRK07470   381 YNNPEANAKAFRDG--WFRTGDLGHLDARGFLYITG 414
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
3476-3846 2.69e-07

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 57.90  E-value: 2.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3476 HAPAICAWD---GELTYGELD----ALSSKLASHlvqlgvnPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 3548
Cdd:PRK06334    32 MTTATVCWDeqlGKLSYNQVRkaviALATKVSKY-------PDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLR 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3549 RHEEIFEQTGAQVVVASAQY----------SARWTSSSCHVVTVSKALS----------SQLPA--VVDSTNTS-VRPEN 3605
Cdd:PRK06334   105 EVTACANLVGVTHVLTSKQLmqhlaqthgeDAEYPFSLIYMEEVRKELSfwekcrigiyMSIPFewLMRWFGVSdKDPED 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3606 AAYIIFTSGSTGVPKGVVLEHR---AVATSCLghgRAFGITN----LSRVLQFASYTFDACiaeIITTLLCGGCICVPSD 3678
Cdd:PRK06334   185 VAVILFTSGTEKLPKGVPLTHAnllANQRACL---KFFSPKEddvmMSFLPPFHAYGFNSC---TLFPLLSGVPVVFAYN 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3679 SDRRNSLAKAISTMDVNWAFLTP-------SVARLLDPGLiPSLKILAIGGE---QSSSADWNRWPGSVQKIHVYGPTEC 3748
Cdd:PRK06334   259 PLYPKKIVEMIDEAKVTFLGSTPvffdyilKTAKKQESCL-PSLRFVVIGGDafkDSLYQEALKTFPHIQLRQGYGTTEC 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3749 CIFCTGYTTKQGFEPSTIGTSVASVSWVVDPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPAWLLEGYP 3828
Cdd:PRK06334   338 SPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGETWYVTGDL 417
                          410
                   ....*....|....*...
gi 1820002560 3829 GHPGRQGRLYKTGDLVQY 3846
Cdd:PRK06334   418 GYVDRHGELFLKGRLSRF 435
PRK07867 PRK07867
acyl-CoA synthetase; Validated
6829-6980 2.79e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 57.77  E-value: 2.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6829 ILFPDENREAYPFVRPSNAALAPLGSIGELL-VEGPILARGYLNDADKTAAAfvndpawlveghgkhpgRRGRLYKTGDL 6907
Cdd:PRK07867   326 IVDPDTGTECPPAEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAER-----------------MRGGVYWSGDL 388
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 6908 VYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAGAAEQaktmVVAFLQLNDEA 6980
Cdd:PRK07867   389 AYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLR-YPDATEVAVYAVPDPVVGDQ----VMAALVLAPGA 456
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
23-190 2.95e-07

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 57.72  E-value: 2.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRWPSSVQT--INGYGPTECCIVCTGYTSEQDFTTGTIGTSIASvSWVVDPKDHGRLAPLGSV 100
Cdd:PRK07059   328 KLIVANGGGMAVQRPVAERWLEMTGCpiTEGYGLSETSPVATCNPVDATEFSGTIGLPLPS-TEVSIRDDDGNDLPLGEP 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  101 GELLVEGPILARGYLSDPEKTAAVFINNpawlleghgGYagrqgrlYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVEL 180
Cdd:PRK07059   407 GEICIRGPQVMAGYWNRPDETAKVMTAD---------GF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYP 470
                          170
                   ....*....|
gi 1820002560  181 GEVEHHVREC 190
Cdd:PRK07059   471 NEIEEVVASH 480
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
7633-8004 3.03e-07

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 57.61  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVN--PEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP----LDPDhpASRHeeIFEQTGAQ 7706
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPlydtLGPE--AIEY--ILNHAEIS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7707 VVVASAQYSarwtssschVVTVSKAL---SSQLPAVVDSTntsvrPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHG 7783
Cdd:cd05927     82 IVFCDAGVK---------VYSLEEFEklgKKNKVPPPPPK-----PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVF 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7784 RAFGITN--------LS---------RVLQFASYTFDACI--------------AEIITTLLCGgcicVPSDSDR----- 7827
Cdd:cd05927    148 KILEILNkinptdvyISylplahifeRVVEALFLYHGAKIgfysgdirlllddiKALKPTVFPG----VPRVLNRiydki 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7828 RNSLAK--AISTMDVNWAFLTpSVARLLDPGLIPSL--------KI-LAIGGEqsssadwNRW--------PGSVQK--- 7885
Cdd:cd05927    224 FNKVQAkgPLKRKLFNFALNY-KLAELRSGVVRASPfwdklvfnKIkQALGGN-------VRLmltgsaplSPEVLEflr 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7886 ----IHV---YGPTECCifctGYTTKQGFEPSTIGTSVASVSWV----VD-PE-NHNRLAPLGSmGELLMEGPILARGYL 7952
Cdd:cd05927    296 valgCPVlegYGQTECT----AGATLTLPGDTSVGHVGGPLPCAevklVDvPEmNYDAKDPNPR-GEVCIRGPNVFSGYY 370
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 7953 NDVDKTEAAFIDDpAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRK 8004
Cdd:cd05927    371 KDPEKTAEALDED-GWL---------------HTGDIGEWLPNGTLKIIDRK 406
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
451-705 3.18e-07

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 57.08  E-value: 3.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  451 LELRADVDEHAFRAAWEYVVQSIAVLRTRIVQHSELGLL-QVVVE------EKMQWTESESLEEYLNEDKAASMGLGD-R 522
Cdd:cd19532     30 YRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPmQGVLAssplrlEHVQISDEAEVEEEFERLKNHVYDLESgE 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  523 LARYALIKEScGGKRWFVWTIHHALYDGWSLPLVLDAVKQVYSGAALERQPSfnTFIQYVSQQ--DVKAAA-----AYWQ 595
Cdd:cd19532    110 TMRIVLLSLS-PTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPL--QYLDFAARQrqDYESGAldedlAYWK 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  596 TALADCEAVLfPPLP-STVT--QPVAD---TTVKYQCPPSpevTSSNI-TTSTLIR--------AAWAIIASRYTSSEDI 660
Cdd:cd19532    187 SEFSTLPEPL-PLLPfAKVKsrPPLTRydtHTAERRLDAA---LAARIkEASRKLRvtpfhfylAALQVLLARLLDVDDI 262
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560  661 VFGTTVTGRNAPitGVEAMVGPTIATVPLRVRPRKGQTVSAFLEN 705
Cdd:cd19532    263 CIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQTFADVLKE 305
PRK07787 PRK07787
acyl-CoA synthetase; Validated
6854-6942 3.20e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 57.31  E-value: 3.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6854 SIGELLVEGPILARGYLNDADKTAAAFVNDpAWlveghgkhpgrrgrlYKTGDLVYYNKDGNLVYIGRKDGQ-VKVRGQR 6932
Cdd:PRK07787   320 TVGELQVRGPTLFDGYLNRPDATAAAFTAD-GW---------------FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYR 383
                           90
                   ....*....|
gi 1820002560 6933 VELGEIENRL 6942
Cdd:PRK07787   384 IGAGEIETAL 393
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
5632-6001 3.28e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 57.39  E-value: 3.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPA-ICAWDGE-LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 5709
Cdd:PRK13391     7 AQTTPDKPAvIMASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5710 RHEDTFRHTGAQVVVTSAQH-------SARWIGTNHQVVTVSAGSLGQLSTLVNPV-GLPAIP----ENAVYIMFTSGST 5777
Cdd:PRK13391    87 EAAYIVDDSGARALITSAAKldvaralLKQCPGVRHRLVLDGDGELEGFVGYAEAVaGLPATPiadeSLGTDMLYSSGTT 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5778 GIPKGVV--LEHRAVVTS------CwgrGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVpsdsdrrndlvka 5849
Cdd:PRK13391   167 GRPKGIKrpLPEQPPDTPlpltafL---QRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIV------------- 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5850 ISTMDVSCALLTPSVARLLEPSSVPTL--QMLVLQGEQVSFADWNRW----------PASV--QTINGYGPtecsICCNT 5915
Cdd:PRK13391   231 MEHFDAEQYLALIEEYGVTHTQLVPTMfsRMLKLPEEVRDKYDLSSLevaihaaapcPPQVkeQMIDWWGP----IIHEY 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5916 YSGKQGfkSGIigTSVASVSWVVDP--------------ENHDRLAPLGSIGELLVEGPILARgYLNDIQKTAAVFIDDP 5981
Cdd:PRK13391   307 YAATEG--LGF--TACDSEEWLAHPgtvgramfgdlhilDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDG 381
                          410       420
                   ....*....|....*....|
gi 1820002560 5982 AWLLEGYPGHPGRQGRLYKT 6001
Cdd:PRK13391   382 TWSTVGDIGYVDEDGYLYLT 401
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
23-199 3.37e-07

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 56.74  E-value: 3.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRWPS--SVQTI-NGYGPTECcIVCTGYTSEQDFTT--GTIGTSIASVSwvvdpkdhgrlAPL 97
Cdd:cd17638    116 SLRAAVTGAATVPVELVRRMRSelGFETVlTAYGLTEA-GVATMCRPGDDAETvaTTCGRACPGFE-----------VRI 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   98 GSVGELLVEGPILARGYLSDPEKTAAVfINNPAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDSQVKLRGQR 177
Cdd:cd17638    184 ADDGEVLVRGYNVMQGYLDDPEATAEA-IDADGWL---------------HTGDVGELDERGYLRITDRLKDMYIVGGFN 247
                          170       180
                   ....*....|....*....|..
gi 1820002560  178 VELGEVEHHVREcLPEAKQLAV 199
Cdd:cd17638    248 VYPAEVEGALAE-HPGVAQVAV 268
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
1937-2444 3.42e-07

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 57.48  E-value: 3.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1937 EQAKARPHAPAICAWDG---EL--TYGELDALSSKLASHLVQL-GVNPEDVVPLCFEK-SMWTVVAmLAVLKAGGAFVPL 2009
Cdd:cd05928     19 EKAGKRPPNPALWWVNGkgdEVkwSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRvPEWWLVN-VACIRTGLVFIPG 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2010 DPDHPAsrhEDI---FRQTGAQVVVTSAQHSARWIGTNHQV------VTVSAGSLE---QFSTLVNPVD-----LPAKPE 2072
Cdd:cd05928     98 TIQLTA---KDIlyrLQASKAKCIVTSDELAPEVDSVASECpslktkLLVSEKSRDgwlNFKELLNEAStehhcVETGSQ 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2073 NAAYVMFTSGSTGTPKGVVLEHravvtSCLGHGQAFGvTNLLRALQFTAYTFDVC----IAEIITTLV----HGGCICVP 2144
Cdd:cd05928    175 EPMAIYFTSGTTGSPKMAEHSH-----SSLGLGLKVN-GRYWLDLTASDIMWNTSdtgwIKSAWSSLFepwiQGACVFVH 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2145 SDSE-RRDNLAKAITDMQVNWGYLTSSVARLL-----DPCLVPSLKVLVLGGEQVNSTDWGKWP--SSVQTINGYGPTEC 2216
Cdd:cd05928    249 HLPRfDPLVILKTLSSYPITTFCGAPTVYRMLvqqdlSSYKFPSLQHCVTGGEPLNPEVLEKWKaqTGLDIYEGYGQTET 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2217 CVFCTGYTGIQgFQSGNIGTsiASVSW---VVDpeNHGRLAPLGSIGELLVE-GPI----LARGYLNDVDKTQAAFiddp 2288
Cdd:cd05928    329 GLICANFKGMK-IKPGSMGK--ASPPYdvqIID--DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATI---- 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2289 awllegypghegrQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEhhmrKCLPEANQLAVEVV-----PP 2363
Cdd:cd05928    400 -------------RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVE----SALIEHPAVVESAVvsspdPI 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2364 SGErdhaMLAAFIRLddetrnspliikyaednsTAQivFLTGIEEELSERLPQHM----VPTVFFALVHF----PTTTSG 2435
Cdd:cd05928    463 RGE----VVKAFVVL------------------APQ--FLSHDPEQLTKELQQHVksvtAPYKYPRKVEFvqelPKTVTG 518

                   ....*....
gi 1820002560 2436 KTDRKRLRE 2444
Cdd:cd05928    519 KIQRNELRD 527
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
4564-4927 3.59e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 57.43  E-value: 3.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4564 DG---ELTYGELDTLSSKLASHLVQLGvKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL-DPDHPAsrheHIFRqtgA 4639
Cdd:PRK07769    50 DGvarDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPG----HVGR---L 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4640 QVVLASAQYATLWTSLG----------------RSVVIVSEAstsqLP--VVTKTADPSVNPGNAAYAIFTSGSTGIPKG 4701
Cdd:PRK07769   122 HAVLDDCTPSAILTTTDsaegvrkffrarpakeRPRVIAVDA----VPdeVGATWVPPEANEDTIAYLQYTSGSTRIPAG 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4702 VVLEHKAVVTSCLGHGQAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICV--PSDSDRR-----NNLAKAINAMDV 4774
Cdd:PRK07769   198 VQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFmsPAAFVRRpgrwiRELARKPGGTGG 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4775 NWALLtPSVA------RML-----DPCVVQSLKILVLGGEQVNSADWDRW----------PKSIQTinAYGPTECSICCT 4833
Cdd:PRK07769   278 TFSAA-PNFAfehaaaRGLpkdgePPLDLSNVKGLLNGSEPVSPASMRKFneafapyglpPTAIKP--SYGMAEATLFVS 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4834 T----------YSGKQGFKSGTI-------GTSIVSVS--------W--VVDPENHNRLaPLGSIGELLVEGPILARGYL 4886
Cdd:PRK07769   355 TtpmdeeptviYVDRDELNAGRFvevpadaPNAVAQVSagkvgvseWavIVDPETASEL-PDGQIGEIWLHGNNIGTGYW 433
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 4887 NDMEKTEAAF----------------IDDPAWLLEG-YGGHsgRQGRLYKTG---DLVRYD 4927
Cdd:PRK07769   434 GKPEETAATFqnilksrlseshaegaPDDALWVRTGdYGVY--FDGELYITGrvkDLVIID 492
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
5770-6137 3.60e-07

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 57.48  E-value: 3.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 IMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYT--FDACMDEIITTLMYGGCICVPS----DSdrr 5843
Cdd:cd05928    179 IYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTgwIKSAWSSLFEPWIQGACVFVHHlprfDP--- 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5844 NDLVKAISTMDVSCALLTPSVARLLEPSSV-----PTLQMLVLQGEQVSFADWNRWPA--SVQTINGYGPTECSICCNTY 5916
Cdd:cd05928    256 LVILKTLSSYPITTFCGAPTVYRMLVQQDLssykfPSLQHCVTGGEPLNPEVLEKWKAqtGLDIYEGYGQTETGLICANF 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5917 SGKQgFKSGIIGTSVASVSWVVDPENHDRLAPlGSIGELLVE-GPI----LARGYLNDIQKTAAVFiddpawllegypgh 5991
Cdd:cd05928    336 KGMK-IKPGSMGKASPPYDVQIIDDNGNVLPP-GTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATI-------------- 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5992 pgrQGRLYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHaMLAAFVQL 6071
Cdd:cd05928    400 ---RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIE-HPAVVESAV-VSSPDPIRGE-VVKAFVVL 473
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 6072 EEGtqnalldkeasgedsmaqvvFLASVEEELAKRLPEHM--------VPTVFFSLLHFPTTTSGKTDRKRLRE 6137
Cdd:cd05928    474 APQ--------------------FLSHDPEQLTKELQQHVksvtapykYPRKVEFVQELPKTVTGKIQRNELRD 527
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
875-1359 3.69e-07

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 56.98  E-value: 3.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  875 DGELTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAfvpldpghpasrheeifkqigaqvvl 954
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV-------------------------- 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  955 tssqhAMLFASSERHQVTVSKVSTSQLPTVVnfakspVDpgnTAYIIFTSGTTGIPKGVVLQHR---------------- 1018
Cdd:cd05940     55 -----AALINYNLRGESLAHCLNVSSAKHLV------VD---AALYIYTSGTTGLPKAAIISHRrawrggaffagsggal 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1019 --------------AVTTSCLGHGEAFGYTDHARVLQFASYTFDACIAEIITTLLYGGCIC------VPSESDRRNNLAK 1078
Cdd:cd05940    121 psdvlytclplyhsTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCryllnqPPKPTERKHKVRM 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1079 AISTMdvncalLTPSV-ARLLEPSAVPSLKRLVLQGE-QVSFADWNRWPGSVQTINGYGPtecsvccntysgkQGFKSGI 1156
Cdd:cd05940    201 IFGNG------LRPDIwEEFKERFGVPRIAEFYAATEgNSGFINFFGKPGAIGRNPSLLR-------------KVAPLAL 261
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1157 IGTSVASLSWVVDAGNHNRLAPLGSIGELLVEGPILAR--GYLnDIDKTEAAFIDDpawllegyeghAGRRG-RLYKTGD 1233
Cdd:cd05940    262 VKYDLESGEPIRDAEGRCIKVPRGEPGLLISRINPLEPfdGYT-DPAATEKKILRD-----------VFKKGdAWFNTGD 329
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1234 LVRCDADGNLVCLGRKDSQVKVRGQRVELGEIEHHVR--ECLPEARQLAVEVilpsgqkehallaafiqldkGNHNalfe 1311
Cdd:cd05940    330 LMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGafPGVEEANVYGVQV--------------------PGTD---- 385
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 1312 ekasGEDSMAQVVFLTGVEEEL-------AKRLPEHMVPTILFTVKAMPITTSGK 1359
Cdd:cd05940    386 ----GRAGMAAIVLQPNEEFDLsalaahlEKNLPGYARPLFLRLQPEMEITGTFK 436
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
5080-5148 3.95e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 51.48  E-value: 3.95e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  5080 PSTEAERTMQQL----WTRVLGIE-LNGIGLDDSFFRLGGDSIAAMKLVGE-ARRTGLQLSVADVFRHPRLVDLA 5148
Cdd:smart00823    5 PPAERRRLLLDLvreqVAAVLGHAaAEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALA 79
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
7607-8123 4.17e-07

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 56.99  E-value: 4.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7607 RCVHDLFAEQARARPGAPAICAWDGE------LTYGELDVLSSNLAGHLVQLGVNPEDVVPlCFEKSMWTVVAM-LAVLK 7679
Cdd:PRK13295    24 RTINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVS-CQLPNWWEFTVLyLACSR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7680 AGGAFVPLdpdHPASRHEEI---FEQTGAQVVVAS--------AQYSARWTSSSC---HVVTVSKA-------------- 7731
Cdd:PRK13295   103 IGAVLNPL---MPIFRERELsfmLKHAESKVLVVPktfrgfdhAAMARRLRPELPalrHVVVVGGDgadsfeallitpaw 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7732 -LSSQLPAVVDSTNTsvRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQ---FASYTFDACIA 7807
Cdd:PRK13295   180 eQEPDAPAILARLRP--GPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMaspMAHQTGFMYGL 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7808 EIITTLlcgGCICVPSDSDRRNSLAKAISTMDVNW-----AFLTPSV-ARLLDPGLIPSLKILAIGG--------EQSss 7873
Cdd:PRK13295   258 MMPVML---GATAVLQDIWDPARAAELIRTEGVTFtmastPFLTDLTrAVKESGRPVSSLRTFLCAGapipgalvERA-- 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7874 adWNRWPGSVqkIHVYGPTECCIFCtgyTTKQGFEPSTIGTSVA-SVSW----VVDPENHNrlAPLGSMGELLMEGPILA 7948
Cdd:PRK13295   333 --RAALGAKI--VSAWGMTENGAVT---LTKLDDPDERASTTDGcPLPGvevrVVDADGAP--LPAGQIGRLQVRGCSNF 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7949 RGYLNDVDKTEaafIDDPAWllegypghpgrqgrlYKTGDLVQYNADGNLVYLGR-KDsqVKVRG-QRVELGEVE----H 8022
Cdd:PRK13295   404 GGYLKRPQLNG---TDADGW---------------FDTGDLARIDADGYIRISGRsKD--VIIRGgENIPVVEIEallyR 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8023 HvreclPEARQLAVeVILPSGQKNHAMLAVFVQlgkgthiahleeKAGGEDSMAQVV-FLTgteeelAKRLPKHMVPTVF 8101
Cdd:PRK13295   464 H-----PAIAQVAI-VAYPDERLGERACAFVVP------------RPGQSLDFEEMVeFLK------AQKVAKQYIPERL 519
                          570       580
                   ....*....|....*....|..
gi 1820002560 8102 FALLHFPMTTSGKADRKRLREI 8123
Cdd:PRK13295   520 VVRDALPRTPSGKIQKFRLREM 541
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
6728-6809 4.35e-07

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 56.76  E-value: 4.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6728 LTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL----DPdhPASRHEdiLRQTGAQVI 6803
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLftafGP--KAIEHR--LRTSGARLV 76

                   ....*.
gi 1820002560 6804 LASAQN 6809
Cdd:cd05973     77 VTDAAN 82
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
5339-5533 4.47e-07

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 56.72  E-value: 4.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5339 GAVPERQPSFNAFIQYL--------GQQDLEA----ATLYWQTALADCKAALfpTLPPTVTQPVADT----TVEYQCPPP 5402
Cdd:cd19546    158 GRAPERAPLPLQFADYAlwerellaGEDDRDSligdQIAYWRDALAGAPDEL--ELPTDRPRPVLPSrragAVPLRLDAE 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5403 SQS-------ATDITTSTLVRAAWAIVTSRYTSSDDVVFGaTVTGRNAPIAGVEAMVGPTIATVPLRVCLQKDQTVSTLL 5475
Cdd:cd19546    236 VHArlmeaaeSAGATMFTVVQAALAMLLTRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELL 314
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 5476 ECLQQQSTDMIAHEQTGLQRIAKM----SPGARHACgFQTLLVVQptddvlgsDDMLGEWRS 5533
Cdd:cd19546    315 GRVREAVREARRHQDVPFERLAELlalpPSADRHPV-FQVALDVR--------DDDNDPWDA 367
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5765-6100 4.54e-07

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 56.24  E-value: 4.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5765 ENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGrGRAFG--------ITNLSRVLQFASYTFDAC-------MDEIITTLM 5829
Cdd:cd05924      3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMG-GADFGtgeftpseDAHKAAAAAAGTVMFPAPplmhgtgSWTAFGGLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5830 YGGCICVPSDSDRRNDLVKAI------STMDVSCALLTPSVARLLEPSSVPTLQMLVLQGeqvSFADWNRwpaSVQT--- 5900
Cdd:cd05924     82 GGQTVVLPDDRFDPEEVWRTIekhkvtSMTIVGDAMARPLIDALRDAGPYDLSSLFAISS---GGALLSP---EVKQgll 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5901 --------INGYGPTECSICCNTYSGKQGFKSGIIgTSVASVSWVVDPENHDRLAPLGSIGELLVEGPIlARGYLNDIQK 5972
Cdd:cd05924    156 elvpnitlVDAFGSSETGFTGSGHSAGSGPETGPF-TRANPDTVVLDDDGRVVPPGSGGVGWIARRGHI-PLGYYGDEAK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5973 TAAVF--IDDPAWLLegypghpgrqgrlykTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVReclpeaRQLA 6050
Cdd:cd05924    234 TAETFpeVDGVRYAV---------------PGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALK------SHPA 292
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 6051 VEVILPSGQKDH---AMLAAFVQLEEGTQNALLDKEASGEDSMA------QVVFLASVE 6100
Cdd:cd05924    293 VYDVLVVGRPDErwgQEVVAVVQLREGAGVDLEELREHCRTRIAryklpkQVVFVDEIE 351
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
6712-6807 4.56e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 56.89  E-value: 4.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6712 ALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQ-LGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASR 6790
Cdd:PRK08314    20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                           90
                   ....*....|....*..
gi 1820002560 6791 HEDILRQTGAQVILASA 6807
Cdd:PRK08314   100 LAHYVTDSGARVAIVGS 116
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
6842-7042 4.66e-07

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 56.13  E-value: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDpawlveghgkhpgrrgRLYKTGDLVYYNKDGNLVYIGR 6921
Cdd:cd05917    188 VDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD----------------GWLHTGDLAVMDEDGYCRIVGR 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 -KDgqVKVRG-QRVELGEIENRLrecmprATQMAVEVISPAGAA-EQAKTMVVAFLQLNDEARdallggnvPNDDNLSAQ 6998
Cdd:cd05917    252 iKD--MIIRGgENIYPREIEEFL------HTHPKVSDVQVVGVPdERYGEEVCAWIRLKEGAE--------LTEEDIKAY 315
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 6999 vvfpakVDEKLSNllpsYMMPEVYFAVPQLPMMISGKTDRKRLR 7042
Cdd:cd05917    316 ------CKGKIAH----YKVPRYVFFVDEFPLTVSGKIQKFKLR 349
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
5640-5783 4.91e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 56.84  E-value: 4.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5640 AICAWDGE-LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdhpaSRH----EDT 5714
Cdd:PRK08276     3 VIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI------NWHltaaEIA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5715 F--RHTGAQVVVTSAQHSArwigTNHQVVTVSAGSLGQLSTLVNPV-----------GLPAIP---ENAVYIM-FTSGST 5777
Cdd:PRK08276    77 YivDDSGAKVLIVSAALAD----TAAELAAELPAGVPLLLVVAGPVpgfrsyeealaAQPDTPiadETAGADMlYSSGTT 152

                   ....*.
gi 1820002560 5778 GIPKGV 5783
Cdd:PRK08276   153 GRPKGI 158
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
1625-1782 5.33e-07

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 56.66  E-value: 5.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1625 IHHAVYDGWSLPLILHAVKQVYS----GGVLQWQPsfnAFIQY----------LGQQD-----LEATVAYWQTALADCEA 1685
Cdd:cd19540    128 VHHIAADGWSMAPLARDLATAYAarraGRAPDWAP---LPVQYadyalwqrelLGDEDdpdslAARQLAYWRETLAGLPE 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1686 VLfpTLP-----PTVTQPVAdATVEYQCPP--------LSKATsDTTTSTLIRAAWAIVTSRYTTSDDVVFGTTVTGRNT 1752
Cdd:cd19540    205 EL--ELPtdrprPAVASYRG-GTVEFTIDAelharlaaLAREH-GATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGD 280
                          170       180       190
                   ....*....|....*....|....*....|
gi 1820002560 1753 PVtgVEAMVGPTIATVPVRLRVQRDQTvFA 1782
Cdd:cd19540    281 EA--LDDLVGMFVNTLVLRTDVSGDPT-FA 307
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
5628-5787 5.36e-07

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 56.90  E-value: 5.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5628 FTEQAKAR---PHAPAICAWDG----ELTYGELDALSSKLAGHLTQLGVKPED----MVPLCFEksmwTVVAMLAVLKAG 5696
Cdd:cd05943     72 YAENLLRHadaDDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDrvagYLPNIPE----AVVAMLATASIG 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5697 GA----------------FVPLDP--------------DHPasrHEDTFRH------TGAQVVV-----TSAQHSARWIG 5735
Cdd:cd05943    148 AIwsscspdfgvpgvldrFGQIEPkvlfavdaytyngkRHD---VREKVAElvkglpSLLAVVVvpytvAAGQPDLSKIA 224
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5736 TNHQVV-TVSAGSLGQLstlvNPVGLPaiPENAVYIMFTSGSTGIPK-------GVVLEH 5787
Cdd:cd05943    225 KALTLEdFLATGAAGEL----EFEPLP--FDHPLYILYSSGTTGLPKcivhgagGTLLQH 278
PRK03584 PRK03584
acetoacetate--CoA ligase;
1935-2094 5.43e-07

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 57.11  E-value: 5.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1935 FTEQA--KARPHAPAICAW--DG---ELTYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAG 2003
Cdd:PRK03584    88 YAENLlrHRRDDRPAIIFRgeDGprrELSWAELRRQVAALAAALRALGVGPGDRVaaylPNIPE----TVVAMLATASLG 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2004 GAFVPLDPDHPASRHEDIFRQTGAQVVVTSAQHsaRWIGTNHQVVTVSAGSLEQFSTL--------VNPVDLPAKPENAA 2075
Cdd:PRK03584   164 AIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGY--RYGGKAFDRRAKVAELRAALPSLehvvvvpyLGPAAAAAALPGAL 241
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 2076 -------------------------YVMFTSGSTGTPK-------GVVLEH 2094
Cdd:PRK03584   242 lwedflapaeaaelefepvpfdhplWILYSSGTTGLPKcivhghgGILLEH 292
PRK06178 PRK06178
acyl-CoA synthetase; Validated
90-184 5.54e-07

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 56.97  E-value: 5.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   90 DHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINnpAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRKDS 169
Cdd:PRK06178   404 ETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD--GWL---------------HTGDIGKIDEQGFLHYLGRRKE 466
                           90
                   ....*....|....*
gi 1820002560  170 QVKLRGQRVELGEVE 184
Cdd:PRK06178   467 MLKVNGMSVFPSEVE 481
PRK13382 PRK13382
bile acid CoA ligase;
3466-3976 5.78e-07

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 56.69  E-value: 5.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3466 LFTEQAKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 3545
Cdd:PRK13382    48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3546 PASRHEEIFEQTGAQVVV-------------ASAQYSAR---WTSSScHVVTVSKALSSQLPAVVDStntsvRPENAAYI 3609
Cdd:PRK13382   128 AGPALAEVVTREGVDTVIydeefsatvdralADCPQATRivaWTDED-HDLTVEVLIAAHAGQRPEP-----TGRKGRVI 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3610 IFTSGSTGVPKGV-------------VLEH---RA----VATSCLGHgrAFGITNLSRVLQFASYT-----FD-ACIAEI 3663
Cdd:PRK13382   202 LLTSGTTGTPKGArrsgpggigtlkaILDRtpwRAeeptVIVAPMFH--AWGFSQLVLAASLACTIvtrrrFDpEATLDL 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3664 ITTLLCGGCICVPSDSDRrnslakaisTMDVnwafltpsVARLLDPGLIPSLKILAIGGEQSSsadwnrwPGSVQKI--- 3740
Cdd:PRK13382   280 IDRHRATGLAVVPVMFDR---------IMDL--------PAEVRNRYSGRSLRFAAASGSRMR-------PDVVIAFmdq 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3741 ------HVYGPTECCIFCTGYTTKQGFEPSTIGT-SVASVSWVVDPEnHNRLaPLGSMGELLMEGPILARGYLNDVDKte 3813
Cdd:PRK13382   336 fgdviyNNYNATEAGMIATATPADLRAAPDTAGRpAEGTEIRILDQD-FREV-PTGEVGTIFVRNDTQFDGYTSGSTK-- 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3814 aAFIDdpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVEVI 3893
Cdd:PRK13382   412 -DFHD-------GF----------MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVE-KTLATHPDVAEAAVIGV 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3894 LPS--GQKdhamLAAFVQLEEGTQnalldkeaggedsmaqvVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDR 3971
Cdd:PRK13382   473 DDEqyGQR----LAAFVVLKPGAS-----------------ATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILR 531

                   ....*
gi 1820002560 3972 KRLRE 3976
Cdd:PRK13382   532 RELQA 536
PRK07867 PRK07867
acyl-CoA synthetase; Validated
1987-2373 5.87e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 56.61  E-value: 5.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1987 EKSMWTVVAMLAvlkaGGAFVPLDPDHPASRHEDIFRQTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLEQFSTLVNPVD 2066
Cdd:PRK07867    66 EFSLLLGAAALS----GIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRD 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2067 LPAKPENAA-----YVMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTnllralqftayTFDVC------------IA 2129
Cdd:PRK07867   142 AEPPFRVADpddlfMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLG-----------PDDVCyvsmplfhsnavMA 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2130 EIITTLVHGGCICVPsdseRRDNLAKAITDMQvNWG-----YLTSSVARLLDPCLVP-----SLKVlVLGGEQVnSTDWG 2199
Cdd:PRK07867   211 GWAVALAAGASIALR----RKFSASGFLPDVR-RYGatyanYVGKPLSYVLATPERPddadnPLRI-VYGNEGA-PGDIA 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2200 KWPS--SVQTINGYGPTECCVfctGYTGIQGFQSGNIGTSIASVSwVVDPE-----------NHGRLAPLGSIGELL-VE 2265
Cdd:PRK07867   284 RFARrfGCVVVDGFGSTEGGV---AITRTPDTPPGALGPLPPGVA-IVDPDtgtecppaedaDGRLLNADEAIGELVnTA 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2266 GPILARGYLNDVDKTQaafiddpawllegypghEGRQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHH 2345
Cdd:PRK07867   360 GPGGFEGYYNDPEADA-----------------ERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERI 422
                          410       420
                   ....*....|....*....|....*...
gi 1820002560 2346 MRKcLPEANQLAVEVVPPSGERDHAMLA 2373
Cdd:PRK07867   423 LLR-YPDATEVAVYAVPDPVVGDQVMAA 449
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
4681-5058 5.91e-07

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 56.67  E-value: 5.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4681 VNPGNAAYAIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQ-FASYTFDACIAEIITTLLCCGCICV-PSD 4758
Cdd:cd05937     84 VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTcMPLYHGTAAFLGACNCLMSGGTLALsRKF 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4759 SDRRnnLAKAINAMDVNWALLTPSVARML--------DpcvvQSLKILVLGGEQVNSADWDRWPK--SIQTINA-YGPTE 4827
Cdd:cd05937    164 SASQ--FWKDVRDSGATIIQYVGELCRYLlstppspyD----RDHKVRVAWGNGLRPDIWERFRErfNVPEIGEfYAATE 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4828 CSICCTTYsGKQGFKSGTIGTSIVSVSWV---------VDPENHNRL----------APLGSIGELLVEGPILAR----G 4884
Cdd:cd05937    238 GVFALTNH-NVGDFGAGAIGHHGLIRRWKfenqvvlvkMDPETDDPIrdpktgfcvrAPVGEPGEMLGRVPFKNReafqG 316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4885 YLNDMEKTEAAFIDDPAwllegygghsgRQGRLY-KTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVRECLT 4963
Cdd:cd05937    317 YLHNEDATESKLVRDVF-----------RKGDIYfRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPD 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4964 EAKQLAVEVIVP--EGEGGyamlAAFVQLGDDTYNTLVKEKAGGDSLtvqvvfldrveeeLAKRVPEHMMLTTFFTLEAM 5041
Cdd:cd05937    386 IAEANVYGVKVPghDGRAG----CAAITLEESSAVPTEFTKSLLASL-------------ARKNLPSYAVPLFLRLTEEV 448
                          410
                   ....*....|....*..
gi 1820002560 5042 PTTTSGKIDRKRLREIG 5058
Cdd:cd05937    449 ATTDNHKQQKGVLRDEG 465
PRK07788 PRK07788
acyl-CoA synthetase; Validated
6712-6804 6.16e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 56.47  E-value: 6.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6712 ALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 6791
Cdd:PRK07788    59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
                           90
                   ....*....|...
gi 1820002560 6792 EDILRQTGAQVIL 6804
Cdd:PRK07788   139 AEVAAREGVKALV 151
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
875-1038 6.40e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 56.66  E-value: 6.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  875 DG---ELTYGELDELSSKLAAHLVQLGvKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL----DPGHpASRHEEIFKQ 947
Cdd:PRK07769    50 DGvarDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGH-VGRLHAVLDD 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  948 IGAQVVLTSSQHA----MLFAS---SERHQVtvskVSTSQLPTVVNFAKSPVDPG--NTAYIIFTSGTTGIPKGVVLQHR 1018
Cdd:PRK07769   128 CTPSAILTTTDSAegvrKFFRArpaKERPRV----IAVDAVPDEVGATWVPPEANedTIAYLQYTSGSTRIPAGVQITHL 203
                          170       180
                   ....*....|....*....|
gi 1820002560 1019 AVTTSCLGHGEAFGYTDHAR 1038
Cdd:PRK07769   204 NLPTNVLQVIDALEGQEGDR 223
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
23-189 6.41e-07

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 56.52  E-value: 6.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMGGEQVNSADWDRW-----PSSVQT---INGYGPTECC------IVCTGYTSEQDFTTGTIGTSIASVSW-VVD 87
Cdd:cd05906    290 SLRYLVNAGEAVVAKTIRRLlrllePYGLPPdaiRPAFGMTETCsgviysRSFPTYDHSQALEFVSLGRPIPGVSMrIVD 369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   88 pkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNpAWlleghggyagrqgrlYKTGDLVrYDADGNLVCLGRK 167
Cdd:cd05906    370 --DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED-GW---------------FRTGDLG-FLDNGNLTITGRT 430
                          170       180
                   ....*....|....*....|..
gi 1820002560  168 DSQVKLRGQRVELGEVEHHVRE 189
Cdd:cd05906    431 KDTIIVNGVNYYSHEIEAAVEE 452
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
5766-6132 6.59e-07

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 55.49  E-value: 6.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5766 NAVYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNLSRVLQFASYTFDACMDEIITTLMYGGCICVPSDSDRRNd 5845
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKS- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5846 LVKAISTMDVSCALLTPSVARLLEPSSVPTLQM-LVLQGEQVSFADW-----NRWPASVqTINGYGPTECS-ICCNTYsg 5918
Cdd:cd17633     80 WIRKINQYNATVIYLVPTMLQALARTLEPESKIkSIFSSGQKLFESTkkklkNIFPKAN-LIEFYGTSELSfITYNFN-- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5919 KQGFKSGIIGTSVASVSwvVDPENHDRlaplGSIGELLVEGPILARGYLNdiqktaAVFIDDPAWllegypghpgrqgrl 5998
Cdd:cd17633    157 QESRPPNSVGRPFPNVE--IEIRNADG----GEIGKIFVKSEMVFSGYVR------GGFSNPDGW--------------- 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5999 YKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREC----------LPEAR--QLAVEVILPSGQKDHAMLA 6066
Cdd:cd17633    210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIpgieeaivvgIPDARfgEIAVALYSGDKLTYKQLKR 289
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6067 AfvqleegtqnalldkeasgedsmaqvvflasveeeLAKRLPEHMVPTVFFSLLHFPTTTSGKTDR 6132
Cdd:cd17633    290 F-----------------------------------LKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
6846-6971 6.83e-07

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 56.45  E-value: 6.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6846 NAALAPlGSIGELLVEGPILARGYLNDADKTAAAFVNDpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQ 6925
Cdd:cd05911    334 KDSLGP-NEPGEICVRGPQVMKGYYNNPEATKETFDED-GWL---------------HTGDIGYFDEDGYLYIVDRKKEL 396
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 6926 VKVRGQRVELGEIENRLREcMPRATQMAVEVISPAGAAEQAKTMVV 6971
Cdd:cd05911    397 IKYKGFQVAPAELEAVLLE-HPGVADAAVIGIPDEVSGELPRAYVV 441
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
5632-6137 7.38e-07

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 56.15  E-value: 7.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGELTYGELDALSSKLAGHLTQLGVKPEDMVplcfeksmwTVV-----AML----AVLKAGGAFVPL 5702
Cdd:cd12118     14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTV---------AVLapntpAMYelhfGVPMAGAVLNAL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5703 DPDHPASRHEDTFRHTGAQVVVTSAQHSARWIgtnhqvvtVSAGSlgqlstlVNPVGLPAIPE-NAVYIMFTSGSTGIPK 5781
Cdd:cd12118     85 NTRLDAEEIAFILRHSEAKVLFVDREFEYEDL--------LAEGD-------PDFEWIPPADEwDPIALNYTSGTTGRPK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5782 GVVLEHR--------AVVTS----------------C------WGRGrAFGITN--LSRVLqfASYTFDACMDEIITTlm 5829
Cdd:cd12118    150 GVVYHHRgaylnalaNILEWemkqhpvylwtlpmfhCngwcfpWTVA-AVGGTNvcLRKVD--AKAIYDLIEKHKVTH-- 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5830 YGGC------ICVPSDSDRRNdLVKAISTMdVSCALLTPSVARLLE-----------------PSSVPTLQmlvlqgeqv 5886
Cdd:cd12118    225 FCGAptvlnmLANAPPSDARP-LPHRVHVM-TAGAPPPAAVLAKMEelgfdvthvygltetygPATVCAWK--------- 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5887 sfADWNRWPASVQTingygptecsiccnTYSGKQGfksgiIGTSVASVSWVVDPENHDRLAPLG-SIGELLVEGPILARG 5965
Cdd:cd12118    294 --PEWDELPTEERA--------------RLKARQG-----VRYVGLEEVDVLDPETMKPVPRDGkTIGEIVFRGNIVMKG 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5966 YLNDIQKTAAVFIDdpAWllegypghpgrqgrlYKTGDLVRYDANGNLvclgrkdsQVKLR--------GQRVELGEVE- 6036
Cdd:cd12118    353 YLKNPEATAEAFRG--GW---------------FHSGDLAVIHPDGYI--------EIKDRskdiiisgGENISSVEVEg 407
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6037 ---HHvreclPEARQLAVeVILPSgQKDHAMLAAFVQLEEGtqnalldKEASGEDSMAQVvflasveeelAKRLPEHMVP 6113
Cdd:cd12118    408 vlyKH-----PAVLEAAV-VARPD-EKWGEVPCAFVELKEG-------AKVTEEEIIAFC----------REHLAGFMVP 463
                          570       580
                   ....*....|....*....|....*
gi 1820002560 6114 -TVFFSllHFPTTTSGKTDRKRLRE 6137
Cdd:cd12118    464 kTVVFG--ELPKTSTGKIQKFVLRD 486
PRK03584 PRK03584
acetoacetate--CoA ligase;
4547-4706 7.62e-07

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 56.34  E-value: 7.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4547 FAEQA--RARPDTPAICAW--DG---ELTYGELDTLSSKLASHLVQLGVKPED----MVPLCFEksmwTVVAMLAVLKAG 4615
Cdd:PRK03584    88 YAENLlrHRRDDRPAIIFRgeDGprrELSWAELRRQVAALAAALRALGVGPGDrvaaYLPNIPE----TVVAMLATASLG 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4616 GAFVPLDPDHPAS----RhehiFRQTGAQVVLASAQY-------------ATLWTSLG--RSVVIV----SEASTSQLPV 4672
Cdd:PRK03584   164 AIWSSCSPDFGVQgvldR----FGQIEPKVLIAVDGYryggkafdrrakvAELRAALPslEHVVVVpylgPAAAAAALPG 239
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 4673 VTKTADPSVNPGNAA------------YAIFTSGSTGIPK-------GVVLEH 4706
Cdd:PRK03584   240 ALLWEDFLAPAEAAElefepvpfdhplWILYSSGTTGLPKcivhghgGILLEH 292
PRK08315 PRK08315
AMP-binding domain protein; Validated
3456-3980 7.69e-07

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 56.36  E-value: 7.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3456 PPAIERCVHDLFTEQAKARPHAPAICAWDGEL--TYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmWTVVaML 3529
Cdd:PRK08315    11 VPLLEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVgiwaPNVPE---WVLT-QF 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3530 AVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYsarWTSS----------SCHVVTVSKALSSQLP-------- 3591
Cdd:PRK08315    87 ATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGF---KDSDyvamlyelapELATCEPGQLQSARLPelrrvifl 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3592 -----------------------AVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRV 3648
Cdd:PRK08315   164 gdekhpgmlnfdellalgravddAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRL 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3649 lqfasytfdaCI--------AEIITTLLC---GGCICVPSDS-DRRNSLAkAIS-----------TMdvnwaFLtpsvAR 3705
Cdd:PRK08315   244 ----------CIpvplyhcfGMVLGNLACvthGATMVYPGEGfDPLATLA-AVEeerctalygvpTM-----FI----AE 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3706 LLDPGL----IPSLK--ILAiggeqsssadwnrwpGS----------VQKIH------VYGPTECC--IFCTGYTTkqGF 3761
Cdd:PRK08315   304 LDHPDFarfdLSSLRtgIMA---------------GSpcpievmkrvIDKMHmsevtiAYGMTETSpvSTQTRTDD--PL 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3762 EP--STIGTSVASV-SWVVDPENhNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypgHpgrqgrly 3838
Cdd:PRK08315   367 EKrvTTVGRALPHLeVKIVDPET-GETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDADGWM------H-------- 430
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3839 kTGDLVQYNADGNLVYLGR-KDsqVKVRGqrvelG------EVE----HHvreclPEArqLAVEVI-LPSgQKDHAMLAA 3906
Cdd:PRK08315   431 -TGDLAVMDEEGYVNIVGRiKD--MIIRG-----GeniyprEIEeflyTH-----PKI--QDVQVVgVPD-EKYGEEVCA 494
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 3907 FVQLEEGTQnalLDKEAggedsmaqvvflasVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLREIGAS 3980
Cdd:PRK08315   495 WIILRPGAT---LTEED--------------VRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIE 551
PRK07470 PRK07470
acyl-CoA synthetase; Validated
3467-3644 8.62e-07

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 56.20  E-value: 8.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3467 FTEQAKAR-PHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP----L 3541
Cdd:PRK07470    12 FLRQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPtnfrQ 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3542 DPDHPASrheeIFEQTGAQVVVASAQYS--ARWTSSSC----HVVTVSKALSSQ-LPAVVDStNTSVRPENAA------- 3607
Cdd:PRK07470    92 TPDEVAY----LAEASGARAMICHADFPehAAAVRAASpdltHVVAIGGARAGLdYEALVAR-HLGARVANAAvdhddpc 166
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1820002560 3608 YIIFTSGSTGVPKGVVLEHravatsclgHGRAFGITN 3644
Cdd:PRK07470   167 WFFFTSGTTGRPKAAVLTH---------GQMAFVITN 194
PRK09192 PRK09192
fatty acyl-AMP ligase;
7633-7784 9.36e-07

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 56.17  E-value: 9.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7633 LTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVvvASA 7712
Cdd:PRK09192    50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIAQLRGML--ASA 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7713 QYSA--------RWTSSSCHVVTVSKALSSQ---LPAVVDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLG 7781
Cdd:PRK09192   128 QPAAiitpdellPWVNEATHGNPLLHVLSHAwfkALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRA 207

                   ...
gi 1820002560 7782 HGR 7784
Cdd:PRK09192   208 ISH 210
PRK03584 PRK03584
acetoacetate--CoA ligase;
3467-3626 1.00e-06

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 55.96  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3467 FTEQA--KARPHAPAICAW--DG---ELTYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmwTVVAMLAVLKAG 3535
Cdd:PRK03584    88 YAENLlrHRRDDRPAIIFRgeDGprrELSWAELRRQVAALAAALRALGVGPGDRVaaylPNIPE----TVVAMLATASLG 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3536 GAFVPLDPDHPASRHEEIFEQTGAQVVVASA--QYSARWTSSSCHVVTVSKALSSQLPAVV----DSTNTSVRPENAA-- 3607
Cdd:PRK03584   164 AIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyRYGGKAFDRRAKVAELRAALPSLEHVVVvpylGPAAAAAALPGALlw 243
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 3608 -----------------------YIIFTSGSTGVPK-------GVVLEH 3626
Cdd:PRK03584   244 edflapaeaaelefepvpfdhplWILYSSGTTGLPKcivhghgGILLEH 292
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
3486-3633 1.07e-06

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 55.82  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3486 ELTYGELDALSSKLASHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVA 3564
Cdd:cd05905     14 TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3565 S-AQYSARWTSSSCHVVTVSKALSSQLPAVVDSTNTS---------------VRPENAAYIIFTSGSTGVPKGVVLEHRA 3628
Cdd:cd05905     94 VeACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPkskrsklkkwgphppTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173

                   ....*
gi 1820002560 3629 VATSC 3633
Cdd:cd05905    174 LLAHC 178
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
3480-3976 1.08e-06

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 55.94  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3480 ICAWDG----ELTYGELDALSSKLASHLV-QLGVNPEDVV----PLCFEKsmwtVVAMLAVLKAGGAFVPLDPDHPASRH 3550
Cdd:PRK05620    28 VTTWGGaeqeQTTFAAIGARAAALAHALHdELGITGDQRVgsmmYNCAEH----LEVLFAVACMGAVFNPLNKQLMNDQI 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3551 EEIFEQTGAQVVVASAQYSARWTS--SSC----HVVTVS----KALSSQLP---------AVVDSTNT----SVRPEN-A 3606
Cdd:PRK05620   104 VHIINHAEDEVIVADPRLAEQLGEilKECpcvrAVVFIGpsdaDSAAAHMPegikvysyeALLDGRSTvydwPELDETtA 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3607 AYIIFTSGSTGVPKGVVLEHRAVATSCLG--HGRAFGITNlsrvlqfaSYTFDACI--------AEIITTLLCGGCICVP 3676
Cdd:PRK05620   184 AAICYSTGTTGAPKGVVYSHRSLYLQSLSlrTTDSLAVTH--------GESFLCCVpiyhvlswGVPLAAFMSGTPLVFP 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3677 SDSDRRNSLAKAISTMDVNWAFLTPS------VARLLDPGLIPSLKILAIGGEQSSSADWNRWPG--SVQKIHVYGPTEC 3748
Cdd:PRK05620   256 GPDLSAPTLAKIIATAMPRVAHGVPTlwiqlmVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEEryGVDVVHVWGMTET 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3749 CIFCT--------------GYTTKQGFEPSTIGTSVASVSWVVdpENHNRlaplgSMGELLMEGPILARGYLNDVDKTEa 3814
Cdd:PRK05620   336 SPVGTvarppsgvsgearwAYRVSQGRFPASLEYRIVNDGQVM--ESTDR-----NEGEIQVRGNWVTASYYHSPTEEG- 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3815 afiDDPAWLLEGYPGHPGRQ-----GRLyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLA 3889
Cdd:PRK05620   408 ---GGAASTFRGEDVEDANDrftadGWL-RTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAA-PEVVECA 482
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3890 VeVILPSgqkdhamlaafvqleegtqnalldkEAGGEDSMAQVVFLASVE------EELAKRL----PEHMVPTVFFSLL 3959
Cdd:PRK05620   483 V-IGYPD-------------------------DKWGERPLAVTVLAPGIEptretaERLRDQLrdrlPNWMLPEYWTFVD 536
                          570
                   ....*....|....*..
gi 1820002560 3960 HFPTTTSGKTDRKRLRE 3976
Cdd:PRK05620   537 EIDKTSVGKFDKKDLRQ 553
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4688-4955 1.15e-06

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 55.08  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4688 YAIFTSGSTGIPKGVVLEHKAVVTSCLGhGQAFG--------ITDHTRVLQFASYTFDAC-------IAEIITTLLCCGC 4752
Cdd:cd05924      7 YILYTGGTTGMPKGVMWRQEDIFRMLMG-GADFGtgeftpseDAHKAAAAAAGTVMFPAPplmhgtgSWTAFGGLLGGQT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4753 ICVPSDSDRRNNLAKAINAMDVNWALLTPSV-AR-MLD------PCVVQSLKILVLGG----EQVNSADWDRWPkSIQTI 4820
Cdd:cd05924     86 VVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAmARpLIDalrdagPYDLSSLFAISSGGallsPEVKQGLLELVP-NITLV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4821 NAYGPTECSICCTTYSGKQGFKSGTIgTSIVSVSWVVDPENHNRLAPLGSIGELLVEGPIlARGYLNDMEKTEAAF--ID 4898
Cdd:cd05924    165 DAFGSSETGFTGSGHSAGSGPETGPF-TRANPDTVVLDDDGRVVPPGSGGVGWIARRGHI-PLGYYGDEAKTAETFpeVD 242
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 4899 DPAWLLegygghsgrqgrlykTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVE 4955
Cdd:cd05924    243 GVRYAV---------------PGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVE 284
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
7745-7992 1.15e-06

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 55.59  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7745 TSVRPENAAYIIFTSGSTGVPKGVVLEHR---AVATSCLghgRAFGITN----LSRVLQFASYTFDACiaeIITTLLCGG 7817
Cdd:PRK06334   178 SDKDPEDVAVILFTSGTEKLPKGVPLTHAnllANQRACL---KFFSPKEddvmMSFLPPFHAYGFNSC---TLFPLLSGV 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7818 CICVPSDSDRRNSLAKAISTMDVNWAFLTP-------SVARLLDPGLiPSLKILAIGGE---QSSSADWNRWPGSVQKIH 7887
Cdd:PRK06334   252 PVVFAYNPLYPKKIVEMIDEAKVTFLGSTPvffdyilKTAKKQESCL-PSLRFVVIGGDafkDSLYQEALKTFPHIQLRQ 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7888 VYGPTECCIFCTGYTTKQGFEPSTIGTSVASVSWVVDPENHNRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDPA 7967
Cdd:PRK06334   331 GYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGET 410
                          250       260
                   ....*....|....*....|....*
gi 1820002560 7968 WLLEGYPGHPGRQGRLYKTGDLVQY 7992
Cdd:PRK06334   411 WYVTGDLGYVDRHGELFLKGRLSRF 435
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
4133-4392 1.18e-06

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 55.51  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4133 AGDYIMQTVLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHsELGLLQVVV---EERIQWTESESLEEypredkavsmG 4209
Cdd:cd19540     21 SAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPED-DGGPYQVVLpaaEARPDLTVVDVTED----------E 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4210 VGDRLARYAliKEPYD--------------GGKRW-FVWTMHHALYDGWSLPRILHAVKQAYSGVVLERQPSFNAF-IQY 4273
Cdd:cd19540     90 LAARLAEAA--RRGFDltaelplrarlfrlGPDEHvLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWAPLpVQY 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4274 ----LSQQ-------DPEAAAA----YWQTALVDCKAALfpTLP-----PTVTQPVADtTVEYQCPPPSQSA-------T 4326
Cdd:cd19540    168 adyaLWQRellgdedDPDSLAArqlaYWRETLAGLPEEL--ELPtdrprPAVASYRGG-TVEFTIDAELHARlaalareH 244
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 4327 DITTSTLARAAWAIVTSRYTSSDDVVFGATVTGRnapiaGGEA---IVGPTIATVPVRLRVQRDQTvFA 4392
Cdd:cd19540    245 GATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGR-----GDEAlddLVGMFVNTLVLRTDVSGDPT-FA 307
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
7751-8122 1.18e-06

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 55.94  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7751 NAAYIIFTSGSTGVPKGVVLEHRAVATSCLG--HGRAFGITNlsrvlqfaSYTFDACI--------AEIITTLLCGGCIC 7820
Cdd:PRK05620   182 TAAAICYSTGTTGAPKGVVYSHRSLYLQSLSlrTTDSLAVTH--------GESFLCCVpiyhvlswGVPLAAFMSGTPLV 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7821 VPSDSDRRNSLAKAISTMDVNWAFLTPS------VARLLDPGLIPSLKILAIGGEQSSSADWNRWPG--SVQKIHVYGPT 7892
Cdd:PRK05620   254 FPGPDLSAPTLAKIIATAMPRVAHGVPTlwiqlmVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEEryGVDVVHVWGMT 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7893 ECCIFCT--------------GYTTKQGFEPSTIGTSVASVSWVVdpENHNRlaplgSMGELLMEGPILARGYLNDVDKT 7958
Cdd:PRK05620   334 ETSPVGTvarppsgvsgearwAYRVSQGRFPASLEYRIVNDGQVM--ESTDR-----NEGEIQVRGNWVTASYYHSPTEE 406
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7959 EaafiDDPAWLLEGYPGHPGRQ-----GRLyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQ 8033
Cdd:PRK05620   407 G----GGAASTFRGEDVEDANDrftadGWL-RTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAA-PEVVE 480
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8034 LAVevilpsgqknhamlavfvqlgkgthIAHLEEKaGGEDSMAQVVFLTGTE------EELAKRL----PKHMVPTVFFA 8103
Cdd:PRK05620   481 CAV-------------------------IGYPDDK-WGERPLAVTVLAPGIEptretaERLRDQLrdrlPNWMLPEYWTF 534
                          410
                   ....*....|....*....
gi 1820002560 8104 LLHFPMTTSGKADRKRLRE 8122
Cdd:PRK05620   535 VDEIDKTSVGKFDKKDLRQ 553
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
859-1236 1.29e-06

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 55.52  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  859 AEQARARPDASAVCAWDGE-----LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 933
Cdd:cd05921      2 AHWARQAPDRTWLAEREGNggwrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  934 P-----GHPASRHEEIFKQIGAQVVLTSSqhAMLFASS-------------------ERHQVTVSKVSTSQLPTVVNFAK 989
Cdd:cd05921     82 PayslmSQDLAKLKHLFELLKPGLVFAQD--AAPFARAlaaifplgtplvvsrnavaGRGAISFAELAATPPTAAVDAAF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  990 SPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEAFGYTDH--ARVLQFA--SYTFDACIaeIITTLLYGGCIC 1065
Cdd:cd05921    160 AAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEepPVLVDWLpwNHTFGGNH--NFNLVLYNGGTL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1066 -------VP---SESDRrnNLAKAISTMDVNC----ALLTPSVAR--LLEPSAVPSLKRLVLQGEQVSFADWNRWPG-SV 1128
Cdd:cd05921    238 yiddgkpMPggfEETLR--NLREISPTVYFNVpagwEMLVAALEKdeALRRRFFKRLKLMFYAGAGLSQDVWDRLQAlAV 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1129 QTIN-------GYGPTECS-VCCNTYSGKQgfKSGIIGTSVaslswvvdAGNHNRLAPLGSIGELLVEGPILARGYLNDI 1200
Cdd:cd05921    316 ATVGeripmmaGLGATETApTATFTHWPTE--RSGLIGLPA--------PGTELKLVPSGGKYEVRVKGPNVTPGYWRQP 385
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1820002560 1201 DKTEAAFiDDpawllEGYeghagrrgrlYKTGDLVR 1236
Cdd:cd05921    386 ELTAQAF-DE-----EGF----------YCLGDAAK 405
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
6851-7043 1.35e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 55.39  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFVNDpaWlveghgkhpgrrgrlYKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:PRK05605   413 PDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--W---------------FRTGDVVVMEEDGFIRIVDRIKELIITGG 475
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6931 QRVELGEIENRLREcMPRATQMAVEVISPAGAAEqaktMVVAFLQLNDEArdallggnvpnddnlsaqVVFPAKVDEKLS 7010
Cdd:PRK05605   476 FNVYPAEVEEVLRE-HPGVEDAAVVGLPREDGSE----EVVAAVVLEPGA------------------ALDPEGLRAYCR 532
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1820002560 7011 NLLPSYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:PRK05605   533 EHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
4551-5056 1.38e-06

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 55.46  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4551 ARARPDTPAICAWDGELTYGELDTLSSKLASHLVQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHP-ASR 4629
Cdd:cd05929      2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPrAEA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4630 HEHIFRQTGAQVVLAsaqyATLWTSLGRSVVIVSEASTSQLPVVtktadPSVNPGNaaYAIFTSGSTGIPKGV------V 4703
Cdd:cd05929     82 CAIIEIKAAALVCGL----FTGGGALDGLEDYEAAEGGSPETPI-----EDEAAGW--KMLYSGGTTGRPKGIkrglpgG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4704 LEHKAVVTSCLGhgqAFGITDHTRVLQFASYTFDACIAEIITTLLCCGCICVPSDSDRRNNLaKAINAMDVNWALLTPSV 4783
Cdd:cd05929    151 PPDNDTLMAAAL---GFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFL-RLIERYRVTFAQFVPTM 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4784 -ARMLD-PCVVQ------SLKILVLGGE----QVNSADWDRWPKSIqtINAYGPTECS-ICCTtySGKQGFK-SGTIGTS 4849
Cdd:cd05929    227 fVRLLKlPEAVRnaydlsSLKRVIHAAApcppWVKEQWIDWGGPII--WEYYGGTEGQgLTII--NGEEWLThPGSVGRA 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4850 IVSVSWVVDpENHNRLAPlGSIGELLVEGPIlARGYLNDMEKTEAAfIDDPAWLlegygghsgrqgrlyKTGDLVRYDAD 4929
Cdd:cd05929    303 VLGKVHILD-EDGNEVPP-GEIGEVYFANGP-GFEYTNDPEKTAAA-RNEGGWS---------------TLGDVGYLDED 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4930 GNLVYLGRKDSQVKLRGQRVELGEVEHHVrecLTEAKQLAVEVI-VPEGEGGYAMLAAfVQLGDDTyntlVKEKAGGDSL 5008
Cdd:cd05929    364 GYLYLTDRRSDMIISGGVNIYPQEIENAL---IAHPKVLDAAVVgVPDEELGQRVHAV-VQPAPGA----DAGTALAEEL 435
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 5009 tvqVVFL-DRVEeelAKRVPEhmmltTFFTLEAMPTTTSGKIDRKRLRE 5056
Cdd:cd05929    436 ---IAFLrDRLS---RYKCPR-----SIEFVAELPRDDTGKLYRRLLRD 473
PLN02736 PLN02736
long-chain acyl-CoA synthetase
3456-3635 1.38e-06

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 55.49  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3456 PPAIE-RCVHDLFTEQAKARPHAPA----ICAwDGE------LTYGELDALSSKLASHLVQLGVNPEDVVPLCF-EKSMW 3523
Cdd:PLN02736    38 PDHPEiGTLHDNFVYAVETFRDYKYlgtrIRV-DGTvgeykwMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFiNRPEW 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3524 TVV--AMLAVLKAGgafVPL----DPDhpASR----HEE---IF--------------EQTGAQVVV----ASAQYSARW 3572
Cdd:PLN02736   117 LIVdhACSAYSYVS---VPLydtlGPD--AVKfivnHAEvaaIFcvpqtlntllsclsEIPSVRLIVvvggADEPLPSLP 191
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 3573 TSSSCHVVTVSKALS---SQLPAVVDStntsvRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLG 3635
Cdd:PLN02736   192 SGTGVEIVTYSKLLAqgrSSPQPFRPP-----KPEDVATICYTSGTTGTPKGVVLTHGNLIANVAG 252
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
6301-6477 1.47e-06

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 54.95  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6301 QSVLeLRV--DVDEDAFRAAWEHVVQLTAALRTRIVQHS----------ELGLLQVVVEEKIQWTESKRLEEyLREDKAV 6368
Cdd:cd19534     24 QSVL-LRVpqGLDPDALRQALRALVEHHDALRMRFRREDggwqqrirgdVEELFRLEVVDLSSLAQAAAIEA-LAAEAQS 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6369 SMGLGD-PLARYAIIKEAWGGKRwFVWTIHHALYDG--WslpRVL-----QAVKQAYNG--AVLETQPSFNAFIQ----Y 6434
Cdd:cd19534    102 SLDLEEgPLLAAALFDGTDGGDR-LLLVIHHLVVDGvsW---RILledleAAYEQALAGepIPLPSKTSFQTWAEllaeY 177
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 6435 LSQQDLEATAAYWQTALADceatLFPPLPSSVKQLVADTTVEH 6477
Cdd:cd19534    178 AQSPALLEELAYWRELPAA----DYWGLPKDPEQTYGDARTVS 216
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
5632-6025 1.48e-06

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 55.52  E-value: 1.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5632 AKARPHAPAICAWDGE-----LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 5706
Cdd:cd05921      5 ARQAPDRTWLAEREGNggwrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5707 PASRHE-DTFRH-----TGAQVVVTSAQHSARWIGTNHQVVTVSAGSLGQL---------STLVNPVGL------PAI-P 5764
Cdd:cd05921     85 SLMSQDlAKLKHlfellKPGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVagrgaisfaELAATPPTAavdaafAAVgP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5765 ENAVYIMFTSGSTGIPKGVVLEHR------AVVTSCWGRGR--------------------AFGIT-------------- 5804
Cdd:cd05921    165 DTVAKFLFTSGSTGLPKAVINTQRmlcanqAMLEQTYPFFGeeppvlvdwlpwnhtfggnhNFNLVlynggtlyiddgkp 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5805 ----------NLSRVLQFASYTFDACMDEIITTLmyggcicvPSDSDRRNDLVKAISTMDVSCALLTPSVARLLEPSSVP 5874
Cdd:cd05921    245 mpggfeetlrNLREISPTVYFNVPAGWEMLVAAL--------EKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALAVA 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5875 TLqmlvlqGEQVSFAdwnrwpasvqtiNGYGPTECS-ICCNTYSGKQgfKSGIIGTSVasvswvvdPENHDRLAPLGSIG 5953
Cdd:cd05921    317 TV------GERIPMM------------AGLGATETApTATFTHWPTE--RSGLIGLPA--------PGTELKLVPSGGKY 368
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 5954 ELLVEGPILARGYLNDIQKTAAVFiDDpawllEGYpghpgrqgrlYKTGDLVRY----DANGNLVCLGRKDSQVKL 6025
Cdd:cd05921    369 EVRVKGPNVTPGYWRQPELTAQAF-DE-----EGF----------YCLGDAAKLadpdDPAKGLVFDGRVAEDFKL 428
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
7748-8123 1.49e-06

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 55.49  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7748 RPENAAYIIFTSGSTGVPKGVVLEH----------RAVA--------TSCLGHGRAFGITnlsrvlqfasytfdaciAEI 7809
Cdd:PRK08043   363 QPEDAALILFTSGSEGHPKGVVHSHksllanveqiKTIAdftpndrfMSALPLFHSFGLT-----------------VGL 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7810 ITTLLCGGCICV-PSD----------SDRRNSLAKAISTMDVNWafltpsvARLLDPGLIPSLKILAIGGEQSSSADWNR 7878
Cdd:PRK08043   426 FTPLLTGAEVFLyPSPlhyrivpelvYDRNCTVLFGTSTFLGNY-------ARFANPYDFARLRYVVAGAEKLQESTKQL 498
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7879 WPGS--VQKIHVYGPTECCIfCTGYTTKQGFEPSTIGTsvasvswvVDPENHNRLAPLGSM---GELLMEGPILARGYLN 7953
Cdd:PRK08043   499 WQDKfgLRILEGYGVTECAP-VVSINVPMAAKPGTVGR--------ILPGMDARLLSVPGIeqgGRLQLKGPNIMNGYLR 569
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7954 dvdkteaafIDDPAwLLEGyPGHPGRQGRL----YKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvreclp 8029
Cdd:PRK08043   570 ---------VEKPG-VLEV-PTAENARGEMergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE-------- 630
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8030 earQLAVEVilpSGQKNHAMLAVfvqlgkgthiahlEEKAGGEdsmAQVVFLTGTE---EELAKR-----LPKHMVPTVF 8101
Cdd:PRK08043   631 ---QLALGV---SPDKQHATAIK-------------SDASKGE---ALVLFTTDSEltrEKLQQYarehgVPELAVPRDI 688
                          410       420
                   ....*....|....*....|..
gi 1820002560 8102 FALLHFPMTTSGKADRKRLREI 8123
Cdd:PRK08043   689 RYLKQLPLLGSGKPDFVTLKSM 710
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
2063-2343 1.52e-06

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 55.51  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2063 NPVD--LPaKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSclghgqAFGVTNLLRALQ----FTAYTFDVCIAEII--TT 2134
Cdd:PLN02387   240 NPVDpdLP-SPNDIAVIMYTSGSTGLPKGVMMTHGNIVAT------VAGVMTVVPKLGkndvYLAYLPLAHILELAaeSV 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2135 LVHGGC---------------------------------ICVPSDSER-RD----------NLAKAITD-------MQVN 2163
Cdd:PLN02387   313 MAAVGAaigygspltltdtsnkikkgtkgdasalkptlmTAVPAILDRvRDgvrkkvdakgGLAKKLFDiaykrrlAAIE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2164 ------WGyltssVARLLDPCLVPSLKVLVLGGeQVNSTDWGKWPSSVQT---IN---------GYGPTECCVFCTgYTG 2225
Cdd:PLN02387   393 gswfgaWG-----LEKLLWDALVFKKIRAVLGG-RIRFMLSGGAPLSGDTqrfINiclgapigqGYGLTETCAGAT-FSE 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2226 IQGFQSGNIG-----TSIASVSWvvdpENHGRL---APLGSiGELLVEGPILARGYLNDVDKTQAAFIDDPawllegypg 2297
Cdd:PLN02387   466 WDDTSVGRVGpplpcCYVKLVSW----EEGGYLisdKPMPR-GEIVIGGPSVTLGYFKNQEKTDEVYKVDE--------- 531
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 2298 hegRQGRLYKTGDLVRYSSDGNLVCLGRKDSQVKVR-GQRVELGEVE 2343
Cdd:PLN02387   532 ---RGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVE 575
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
6715-6808 1.53e-06

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 55.45  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6715 RPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDI 6794
Cdd:cd05959     17 RGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYY 96
                           90
                   ....*....|....
gi 1820002560 6795 LRQTGAQVILASAQ 6808
Cdd:cd05959     97 LEDSRARVVVVSGE 110
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
6850-7044 1.53e-06

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 55.35  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6850 APLGSIGELLVEGPILARGYLNDADKTAAAFVNdpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVR 6929
Cdd:PRK03640   327 VPPFEEGEIVVKGPNVTKGYLNREDATRETFQD--GWF---------------KTGDIGYLDEEGFLYVLDRRSDLIISG 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6930 GQRVELGEIENRLREcMPratqmAVEVISPAGAAEQAKTMV-VAFLqlndeardaLLGGNVPNDDnLSAQvvfpakVDEK 7008
Cdd:PRK03640   390 GENIYPAEIEEVLLS-HP-----GVAEAGVVGVPDDKWGQVpVAFV---------VKSGEVTEEE-LRHF------CEEK 447
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1820002560 7009 LSnllpSYMMPEVYFAVPQLPMMISGKTDRKRLREI 7044
Cdd:PRK03640   448 LA----KYKVPKRFYFVEELPRNASGKLLRHELKQL 479
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
6720-6807 1.66e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 55.29  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6720 AVCAWDGE-LTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDILRQT 6798
Cdd:PRK08276     3 VIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82

                   ....*....
gi 1820002560 6799 GAQVILASA 6807
Cdd:PRK08276    83 GAKVLIVSA 91
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
1954-2443 1.74e-06

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 55.07  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1954 ELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQTGAQVVVTS 2033
Cdd:PRK08008    37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2034 AQHSARW--------IGTNHQVVTVSAGSLEQ----FSTLVN--PVDL----PAKPENAAYVMFTSGSTGTPKGVVLEHr 2095
Cdd:PRK08008   117 AQFYPMYrqiqqedaTPLRHICLTRVALPADDgvssFTQLKAqqPATLcyapPLSTDDTAEILFTSGTTSRPKGVVITH- 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2096 avvtsclghgqafgvTNLLRALQFTAY---------------TFDV---CIAEIITTLVHGGCICVPSDSERRdnLAKAI 2157
Cdd:PRK08008   196 ---------------YNLRFAGYYSAWqcalrdddvyltvmpAFHIdcqCTAAMAAFSAGATFVLLEKYSARA--FWGQV 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2158 TDMQVNwgyLTSSVARLL-------------DPCLVPSLKVLVLGGEQVNS--TDWGkwpssVQTINGYGPTECCVFCTG 2222
Cdd:PRK08008   259 CKYRAT---ITECIPMMIrtlmvqppsandrQHCLREVMFYLNLSDQEKDAfeERFG-----VRLLTSYGMTETIVGIIG 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2223 YTGIQGFQSGNIG-TSIASVSWVVDpeNHGRLAPLGSIGELLVE---GPILARGYLNDVDKTQAAFIDDpAWLlegypgh 2298
Cdd:PRK08008   331 DRPGDKRRWPSIGrPGFCYEAEIRD--DHNRPLPAGEIGEICIKgvpGKTIFKEYYLDPKATAKVLEAD-GWL------- 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2299 egrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMrKCLPEANQLAVEVVPPSgERDHAmLAAFIRL 2378
Cdd:PRK08008   401 --------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENII-ATHPKIQDIVVVGIKDS-IRDEA-IKAFVVL 469
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 2379 DDETRNSpliikyaednstaqivfltgiEEELSERLPQHM----VPTVFFALVHFPTTTSGKTDRKRLR 2443
Cdd:PRK08008   470 NEGETLS---------------------EEEFFAFCEQNMakfkVPSYLEIRKDLPRNCSGKIIKKNLK 517
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
85-159 1.88e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 54.97  E-value: 1.88e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560   85 VVDPkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINnpawlLEGHggyagrqgRLYKTGDLVRYDADG 159
Cdd:PRK08314   370 VIDP-ETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE-----IDGK--------RFFRTGDLGRMDEEG 430
PRK05850 PRK05850
acyl-CoA synthetase; Validated
5626-5794 1.96e-06

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 54.95  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5626 DLFTEQAKARPHAPAIC------AWDG---ELTYGELDALSSKLAGHLTQLGVkPEDMVPLCFEKSMWTVVAMLAVLKAG 5696
Cdd:PRK05850     5 SLLRERASLQPDDAAFTfidyeqDPAGvaeTLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5697 GAFVPLDPDHPASRHEDT---FRHTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLGQLSTL---------VNPVGLPAIp 5764
Cdd:PRK05850    84 LIAVPLSVPQGGAHDERVsavLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLdldsprgsdARPRDLPST- 162
                          170       180       190
                   ....*....|....*....|....*....|
gi 1820002560 5765 enaVYIMFTSGSTGIPKGVVLEHRAVVTSC 5794
Cdd:PRK05850   163 ---AYLQYTSGSTRTPAGVMVSHRNVIANF 189
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
6799-7038 1.98e-06

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 54.19  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6799 GAQVILASAQNTTLFQSSNQT----VVTVNRSSYILFPDENREA------YP----FVRPSNAALAPLGSIGELLVEGPI 6864
Cdd:cd17635    126 GSRAIAADVRFIEATGLTNTAqvygLSETGTALCLPTDDDSIEInavgrpYPgvdvYLAATDGIAGPSASFGTIWIKSPA 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6865 LARGYLNDADKTAAAFVNDpaWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIEnRLRE 6944
Cdd:cd17635    206 NMLGYWNNPERTAEVLIDG--WV---------------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVE-RIAE 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6945 CMPRATQMAVEVISPAGAAEQAKTMVVAFlQLNDEARdallggnvpnddnLSAQVvfpakvdEKLSNLLPSYMMPEVYFA 7024
Cdd:cd17635    268 GVSGVQECACYEISDEEFGELVGLAVVAS-AELDENA-------------IRALK-------HTIRRELEPYARPSTIVI 326
                          250
                   ....*....|....
gi 1820002560 7025 VPQLPMMISGKTDR 7038
Cdd:cd17635    327 VTDIPRTQSGKVKR 340
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
6704-6807 1.98e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 54.81  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6704 VHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLD 6783
Cdd:PRK06187     8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
                           90       100
                   ....*....|....*....|....
gi 1820002560 6784 PDHPASRHEDILRQTGAQVILASA 6807
Cdd:PRK06187    88 IRLKPEEIAYILNDAEDRVVLVDS 111
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5773-6136 2.12e-06

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 54.41  E-value: 2.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5773 TSGSTGIPKGVVLEHRAVVTSCW--GRGRAFGITNlsrVLQFASYTF--DACMDEIITTLMYGGCICVPSDSDRRN---- 5844
Cdd:cd05944     10 TGGTTGTPKLAQHTHSNEVYNAWmlALNSLFDPDD---VLLCGLPLFhvNGSVVTLLTPLASGAHVVLAGPAGYRNpglf 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5845 -DLVKAISTMDVSCALLTPSV--ARLLEP--SSVPTLQMLVLQGEQVSFADWNRWPAS--VQTINGYGPTE--CSICCNT 5915
Cdd:cd05944     87 dNFWKLVERYRITSLSTVPTVyaALLQVPvnADISSLRFAMSGAAPLPVELRARFEDAtgLPVVEGYGLTEatCLVAVNP 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5916 YSGKQgfKSGIIGTSV--ASVSWVV-DPENHD--RLAPlGSIGELLVEGPILARGYLNDIQKTAAvFIDDpAWLlegypg 5990
Cdd:cd05944    167 PDGPK--RPGSVGLRLpyARVRIKVlDGVGRLlrDCAP-DEVGEICVAGPGVFGGYLYTEGNKNA-FVAD-GWL------ 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5991 hpgrqgrlyKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECLpeARQLAVEVILPSGQKD-HA--MLAA 6067
Cdd:cd05944    236 ---------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIE----EAL--LRHPAVAFAGAVGQPDaHAgeLPVA 300
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6068 FVQLEEGTqnalldkeasgedsmaqVVFLASVEEELAKRLPEH-MVPTVFFSLLHFPTTTSGKTDRKRLR 6136
Cdd:cd05944    301 YVQLKPGA-----------------VVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALR 353
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
6850-7042 2.28e-06

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 54.41  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6850 APLGSIGELLVEGPIlarGYLNDADKTAAAFVNDpAWLVeghgkhpgrrgrlykTGDLVYYNKDGNLVYIGRKDGQVKVR 6929
Cdd:cd05958    286 VPDGTIGRLAVRGPT---GCRYLADKRQRTYVQG-GWNI---------------TGDTYSRDPDGYFRHQGRSDDMIVSG 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6930 GQRVELGEIENRLrecmprATQMAVEVISPAGAAEQAKTMVV-AFLqlndeardALLGGNVPnddnlSAQVVfpAKVDEK 7008
Cdd:cd05958    347 GYNIAPPEVEDVL------LQHPAVAECAVVGHPDESRGVVVkAFV--------VLRPGVIP-----GPVLA--RELQDH 405
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1820002560 7009 LSNLLPSYMMP-EVYFaVPQLPMMISGKTDRKRLR 7042
Cdd:cd05958    406 AKAHIAPYKYPrAIEF-VTELPRTATGKLQRFALR 439
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
877-1040 2.43e-06

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 54.66  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  877 ELTYGELDELSSKLAAHLV-QLGVKREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPGHPASRHEEIFKQIGAQVVLT 955
Cdd:cd05905     14 TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  956 SSQHAMLFASSERHQVT---------------VSKVSTSQLPTVVNFAKSP-VDPGNTAYIIFTSGTTGIPKGVVLQHRA 1019
Cdd:cd05905     94 VEACLKGLPKKLLKSKTaaeiakkkgwpkildFVKIPKSKRSKLKKWGPHPpTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173
                          170       180
                   ....*....|....*....|.
gi 1820002560 1020 VTTSCLGHGEAFGYTdHARVL 1040
Cdd:cd05905    174 LLAHCRALKEACELY-ESRPL 193
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
6868-7043 2.46e-06

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 54.78  E-value: 2.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6868 GYLNDADKTAAAFvndpawlveghgkhpgrRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMP 6947
Cdd:cd05928    387 GYVDNPEKTAATI-----------------RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIE-HP 448
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6948 RATQMAVeVISPAGA-AEQAKTMVVAFLQLNDEARDALLggnvpnddnlsaqvvfpAKVDEKLSNLLPSYMMPEVYFAVP 7026
Cdd:cd05928    449 AVVESAV-VSSPDPIrGEVVKAFVVLAPQFLSHDPEQLT-----------------KELQQHVKSVTAPYKYPRKVEFVQ 510
                          170
                   ....*....|....*..
gi 1820002560 7027 QLPMMISGKTDRKRLRE 7043
Cdd:cd05928    511 ELPKTVTGKIQRNELRD 527
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
6716-6806 2.75e-06

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 54.24  E-value: 2.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6716 PNAPAVCAWDG--ELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHED 6793
Cdd:cd05926      1 PDAPALVVPGStpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90
                   ....*....|...
gi 1820002560 6794 ILRQTGAQVILAS 6806
Cdd:cd05926     81 YLADLGSKLVLTP 93
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
6704-6793 2.91e-06

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 54.42  E-value: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6704 VHDLFTEQALARPNAPAVcAWDGE------LTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGG 6777
Cdd:cd05968     63 VEQLLDKWLADTRTRPAL-RWEGEdgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
                           90       100
                   ....*....|....*....|
gi 1820002560 6778 AFVPL----DPDHPASRHED 6793
Cdd:cd05968    142 IVVPIfsgfGKEAAATRLQD 161
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
6820-6944 3.24e-06

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 54.29  E-value: 3.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6820 VVTVNRSSYIL-------FPDEnreAYPFVRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDpAWLveghg 6892
Cdd:cd17640    252 VVSARRLKCNVrgsvgrpLPGT---EIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSD-GWF----- 322
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 6893 khpgrrgrlyKTGDLVYYNKDGNLVYIGR-KDGQVKVRGQRVELGEIENRLRE 6944
Cdd:cd17640    323 ----------NTGDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIEEALMR 365
PRK08316 PRK08316
acyl-CoA synthetase; Validated
67-285 3.68e-06

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 54.17  E-value: 3.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   67 EQDFTTGTIGTSIASV-SWVVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinnpawlleghggyagrQGR 145
Cdd:PRK08316   335 EHLRRPGSAGRPVLNVeTRVVD--DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-----------------RGG 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  146 LYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECL---PEAKQLAVeVVLPlgqknHATlaaFIqldkg 222
Cdd:PRK08316   396 WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVE----EALythPAVAEVAV-IGLP-----DPK---WI----- 457
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560  223 thnallkEKVggddsIARVVFLAGV---EEEL----AKRLPKHMVP-TVFF--ALlhfPTTTSGKTDRKRLRE 285
Cdd:PRK08316   458 -------EAV-----TAVVVPKAGAtvtEDELiahcRARLAGFKVPkRVIFvdEL---PRNPSGKILKRELRE 515
PRK07798 PRK07798
acyl-CoA synthetase; Validated
6706-6780 3.76e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 54.12  E-value: 3.76e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 6706 DLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFV 6780
Cdd:PRK07798     7 DLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV 81
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
4564-4994 3.78e-06

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 54.22  E-value: 3.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4564 DGELTYGELDTLSSKLASHLV-QLGVKPEDMVPLCFEKSMWTVVAMLAVLKAG--GAFVPldpdhPASRHE---HIFRQT 4637
Cdd:cd05938      3 GETYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLN-----TNIRSKsllHCFRCC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4638 GAQVVLASAQyatLWTSL----------GRSVVIVSEASTSQ--------------LPVVTKTADPSVNPGNAAYaIFTS 4693
Cdd:cd05938     78 GAKVLVVAPE---LQEAVeevlpalradGVSVWYLSHTSNTEgvislldkvdaasdEPVPASLRAHVTIKSPALY-IYTS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4694 GSTGIPKGVVLEHKAVVTSC-------------------LGHGQAFGITDH-------TRVL--QF-ASYTFDACIAEII 4744
Cdd:cd05938    154 GTTGLPKAARISHLRVLQCSgflslcgvtaddviyitlpLYHSSGFLLGIGgcielgaTCVLkpKFsASQFWDDCRKHNV 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4745 TTLLCCGCIC------VPSDSDRRNNLAKAInamdvnwalltpsvarmldpcvvqslkilvlgGEQVNSADWDRWPK--- 4815
Cdd:cd05938    234 TVIQYIGELLrylcnqPQSPNDRDHKVRLAI--------------------------------GNGLRADVWREFLRrfg 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4816 SIQTINAYGPTECSICCTTYSGKQGfksgtigtSIVSVSW--------------------VVDPENHNRLAPLGSIGeLL 4875
Cdd:cd05938    282 PIRIREFYGSTEGNIGFFNYTGKIG--------AVGRVSYlykllfpfelikfdvekeepVRDAQGFCIPVAKGEPG-LL 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4876 VeGPILAR----GYLNDMEKTEAAFIDDPAwllegygghsgRQGRLY-KTGDLVRYDADGNLVYLGRKDSQVKLRGQRVE 4950
Cdd:cd05938    353 V-AKITQQspflGYAGDKEQTEKKLLRDVF-----------KKGDVYfNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVA 420
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 4951 LGEVEHHVR--ECLTEAKQLAVEviVPEGEGGYAMLAafVQLGDDT 4994
Cdd:cd05938    421 TTEVADVLGllDFLQEVNVYGVT--VPGHEGRIGMAA--VKLKPGH 462
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
5648-6137 3.82e-06

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 53.73  E-value: 3.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5648 LTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVP----LDPDHPASRHEdtfRHTGAQVV 5723
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRVD---RGGAVYAA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5724 VTSAQHSarwigtnhqvvtvsagslgqlstlvnpvglpaipENAVYIMFTSGSTGIPKGVVLEHRA-----VVTSCW-GR 5797
Cdd:cd05974     78 VDENTHA----------------------------------DDPMLLYFTSGTTSKPKLVEHTHRSypvghLSTMYWiGL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5798 GRAFGITNLSR--------------------VLQFASYTFDA--CMDEI----ITTLmyggciCVPSDSDR---RNDLVK 5848
Cdd:cd05974    124 KPGDVHWNISSpgwakhawscffapwnagatVFLFNYARFDAkrVLAALvrygVTTL------CAPPTVWRmliQQDLAS 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5849 AISTMDVSCALLTPsvarlLEPSSVptlqmlvlqgEQVSFAdWNRwpasvqTI-NGYGPTECSICCNTYSGkQGFKSGII 5927
Cdd:cd05974    198 FDVKLREVVGAGEP-----LNPEVI----------EQVRRA-WGL------TIrDGYGQTETTALVGNSPG-QPVKAGSM 254
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5928 GTsvasvswvvdPENHDRLAPLGSIGELLVEGPIlargylndiqktaAVFIDD--PAWLLEGYPGHPGR-----QGRLYK 6000
Cdd:cd05974    255 GR----------PLPGYRVALLDPDGAPATEGEV-------------ALDLGDtrPVGLMKGYAGDPDKtahamRGGYYR 311
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6001 TGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECLPEARQLAVEVILPSgqKDHAMLA---AFVQLEEGTQN 6077
Cdd:cd05974    312 TGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE----SVLIEHPAVAEAAVVPS--PDPVRLSvpkAFIVLRAGYEP 385
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6078 AlldkeasgeDSMAQVVFLASvEEELAkrlPEHMVPTVFFSLLhfPTTTSGKTDRKRLRE 6137
Cdd:cd05974    386 S---------PETALEIFRFS-RERLA---PYKRIRRLEFAEL--PKTISGKIRRVELRR 430
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
4567-4955 3.90e-06

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 54.35  E-value: 3.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGELDTLSSKLASHLVQLGVKPEDMVPL--------------CFEKSMwTVVAMLAVLkAGGAFVpldpdhpasrheH 4632
Cdd:PLN02387   107 ITYGQVFERVCNFASGLVALGHNKEERVAIfadtraewlialqgCFRQNI-TVVTIYASL-GEEALC------------H 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4633 IFRQTGAQVVLA-SAQYATL------WTSLGRSVVIVSEASTSQLPVV------------------TKTADPSV-NPGNA 4686
Cdd:PLN02387   173 SLNETEVTTVICdSKQLKKLidissqLETVKRVIYMDDEGVDSDSSLSgssnwtvssfseveklgkENPVDPDLpSPNDI 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4687 AYAIFTSGSTGIPKGVVLEHKAVVT----------------------------------------SCLGHGQAFGITDHT 4726
Cdd:PLN02387   253 AVIMYTSGSTGLPKGVMMTHGNIVAtvagvmtvvpklgkndvylaylplahilelaaesvmaavgAAIGYGSPLTLTDTS 332
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4727 RVLQFASYTfDAciAEIITTLLccgcICVPSDSDR-RNNLAKAINA-----------------MDVN------WALltps 4782
Cdd:PLN02387   333 NKIKKGTKG-DA--SALKPTLM----TAVPAILDRvRDGVRKKVDAkgglakklfdiaykrrlAAIEgswfgaWGL---- 401
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4783 vARML-DPCVVQSLKIlVLGGeQVN---------SADWDRWpksiqtIN---------AYGPTEcsICC-TTYSGKQGFK 4842
Cdd:PLN02387   402 -EKLLwDALVFKKIRA-VLGG-RIRfmlsggaplSGDTQRF------INiclgapigqGYGLTE--TCAgATFSEWDDTS 470
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4843 SGTIG-----TSIVSVSWvvdPENHNRLA--PLGSiGELLVEGPILARGYLNDMEKTEAAFIDDPawllegygghsgRQG 4915
Cdd:PLN02387   471 VGRVGpplpcCYVKLVSW---EEGGYLISdkPMPR-GEIVIGGPSVTLGYFKNQEKTDEVYKVDE------------RGM 534
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 4916 RLYKTGDLVRYDADGNLVYLGRKDSQVKLR-GQRVELGEVE 4955
Cdd:PLN02387   535 RWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVE 575
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
7209-7480 3.95e-06

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 53.61  E-value: 3.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7209 LELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGLL-QVVVE------EKIQW-TESEALEEY--LKE-----DKAV 7273
Cdd:cd19532     30 YRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPmQGVLAssplrlEHVQIsDEAEVEEEFerLKNhvydlESGE 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7274 SMGLgdplahyALVKeaWGGKR-WFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSfnafiQYLG-----QQDLEA 7347
Cdd:cd19532    110 TMRI-------VLLS--LSPTEhYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPL-----QYLDfaarqRQDYES 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7348 TA-----AYWQTALSDCEAVLfPPLP-STVT--QPVADTTVEYqcpplSKATLDTTTSTLIR---------------AAW 7404
Cdd:cd19532    176 GAldedlAYWKSEFSTLPEPL-PLLPfAKVKsrPPLTRYDTHT-----AERRLDAALAARIKeasrklrvtpfhfylAAL 249
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 7405 AIVTSCYTSSDDVVYGTTVTGRNAPiaGVEAMVGPTIATVPVRLRVQRDQTvfaFLQGLQQQSTDMiaheQTGLQH 7480
Cdd:cd19532    250 QVLLARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQT---FADVLKETRDKA----YAALAH 316
PLN03102 PLN03102
acyl-activating enzyme; Provisional
3611-3985 4.00e-06

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 53.87  E-value: 4.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3611 FTSGSTGVPKGVVLEHRAVATSCLGH--GRAFGITNLS----RVLQFASYTFDACIAEIITTLLCGGCICVPSdsdrrns 3684
Cdd:PLN03102   193 YTSGTTADPKGVVISHRGAYLSTLSAiiGWEMGTCPVYlwtlPMFHCNGWTFTWGTAARGGTSVCMRHVTAPE------- 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3685 LAKAISTMDVNWAFLTPSVARLLDPG-------LIPSLKILAIGGEQSSSADWNRWPGSVQKIHVYGPTECC---IFC-- 3752
Cdd:PLN03102   266 IYKNIEMHNVTHMCCVPTVFNILLKGnsldlspRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATgpvLFCew 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3753 ----TGYTTKQGFE-PSTIGTSVASVSwVVDPENHNRLAPL----GSMGELLMEGPILARGYLNDVDKTEAAFidDPAWL 3823
Cdd:PLN03102   346 qdewNRLPENQQMElKARQGVSILGLA-DVDVKNKETQESVprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF--KHGWL 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3824 legypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVeVILPsgqkdHAM 3903
Cdd:PLN03102   423 ---------------NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE-NVLYKYPKVLETAV-VAMP-----HPT 480
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3904 LA----AFVQLEEGTQNALLDKEAggedsmaqvvfLASVEEELAK----RLPEHMVP--TVFFSLLhfPTTTSGKTDRKR 3973
Cdd:PLN03102   481 WGetpcAFVVLEKGETTKEDRVDK-----------LVTRERDLIEycreNLPHFMCPrkVVFLQEL--PKNGNGKILKPK 547
                          410
                   ....*....|..
gi 1820002560 3974 LREIGASFTAQQ 3985
Cdd:PLN03102   548 LRDIAKGLVVED 559
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
3471-3976 4.21e-06

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 53.92  E-value: 4.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3471 AKARPHAPAICAWDGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 3550
Cdd:cd05929      2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3551 EEIFE-QTGAQVVVASAQYSARWtssschvvtvskALSSQLPAVVDSTNTSVRPE-NAAYIIFTSGSTGVPKGVVLEHRA 3628
Cdd:cd05929     82 CAIIEiKAAALVCGLFTGGGALD------------GLEDYEAAEGGSPETPIEDEaAGWKMLYSGGTTGRPKGIKRGLPG 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3629 V-------ATSCLGHGRAFGITNLSRVLQFASYTFDACiaeiITTLLCGGCICVPSDSDRRNSLaKAISTMDVNWAFLTP 3701
Cdd:cd05929    150 GppdndtlMAAALGFGPGADSVYLSPAPLYHAAPFRWS----MTALFMGGTLVLMEKFDPEEFL-RLIERYRVTFAQFVP 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3702 SV-ARLLD-PGLIP------SLKILAIGGEQSS---SADWNRWPGsvQKIH-VYGPTEccifCTGYTTKQGFE----PST 3765
Cdd:cd05929    225 TMfVRLLKlPEAVRnaydlsSLKRVIHAAAPCPpwvKEQWIDWGG--PIIWeYYGGTE----GQGLTIINGEEwlthPGS 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3766 IGTSVASVSWVVDpENHNRLAPlGSMGELLMEGPIlARGYLNDVDKTEAAfIDDPAWLlegypghpgrqgrlyKTGDLVQ 3845
Cdd:cd05929    299 VGRAVLGKVHILD-EDGNEVPP-GEIGEVYFANGP-GFEYTNDPEKTAAA-RNEGGWS---------------TLGDVGY 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3846 YNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREClPEARQLAVeVILPS---GQKDHAMlaafVQLEEGTQnalldke 3922
Cdd:cd05929    360 LDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH-PKVLDAAV-VGVPDeelGQRVHAV----VQPAPGAD------- 426
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 3923 aggedsmAQVVFLASVEEELAKRLPEHMVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:cd05929    427 -------AGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
6842-7041 4.30e-06

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 53.64  E-value: 4.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPawlveghgkhpGRRgrLYKTGDLVYYNKDGNLVYIGR 6921
Cdd:cd05935    265 IDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK-----------GRR--FFRTGDLGYMDEEGYFFFVDR 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 KDGQVKVRGQRVELGEIENRLREcMPRATQMAVEVISPAGAAEQAKTMVVaflqLNDEARdallgGNVPNDDnlsaqvvf 7001
Cdd:cd05935    332 VKRMINVSGFKVWPAEVEAKLYK-HPAI*EVCVISVPDERVGEEVKAFIV----LRPEYR-----GKVTEED-------- 393
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1820002560 7002 pakVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd05935    394 ---IIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
PRK05850 PRK05850
acyl-CoA synthetase; Validated
3465-3633 4.34e-06

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 53.79  E-value: 4.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3465 DLFTEQAKARPHAPAIC------AWDG---ELTYGELDALSSKLASHLVQLGVnPEDVVPLCFEKSMWTVVAMLAVLKAG 3535
Cdd:PRK05850     5 SLLRERASLQPDDAAFTfidyeqDPAGvaeTLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3536 GAFVPLDPDHPASRHEeifeQTGAqvVVASAQYSARWTSSSChVVTVSKALSSQ----LPAVV-------DSTNTS-VRP 3603
Cdd:PRK05850    84 LIAVPLSVPQGGAHDE----RVSA--VLRDTSPSVVLTTSAV-VDDVTEYVAPQpgqsAPPVIevdlldlDSPRGSdARP 156
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1820002560 3604 ENA---AYIIFTSGSTGVPKGVVLEHRAVATSC 3633
Cdd:PRK05850   157 RDLpstAYLQYTSGSTRTPAGVMVSHRNVIANF 189
PRK07867 PRK07867
acyl-CoA synthetase; Validated
3519-3978 4.38e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 53.92  E-value: 4.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3519 EKSMWTVVAMLAvlkaGGAFVPLDPDHPASRHEEIFEQTGAQVVVASAQYSARWTSSSC---HVVTVSKALSSQL--PAV 3593
Cdd:PRK07867    66 EFSLLLGAAALS----GIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPgvrVINVDSPAWADELaaHRD 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3594 VDSTNTSVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITN-----LSRVLqFASytfDACIAEIITTLL 3668
Cdd:PRK07867   142 AEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPddvcyVSMPL-FHS---NAVMAGWAVALA 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3669 CGGCICVP---SDSD-----RR------NSLAKAIStmdvnWAFLTPSVARLLDPglipSLKILAigGEQSSSADWNRWP 3734
Cdd:PRK07867   218 AGASIALRrkfSASGflpdvRRygatyaNYVGKPLS-----YVLATPERPDDADN----PLRIVY--GNEGAPGDIARFA 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3735 G--SVQKIHVYGPTECCIfctGYTTKQGFEPSTIGTSVASVSwVVDPE-----------NHNRLAPLGSMGELL-MEGPI 3800
Cdd:PRK07867   287 RrfGCVVVDGFGSTEGGV---AITRTPDTPPGALGPLPPGVA-IVDPDtgtecppaedaDGRLLNADEAIGELVnTAGPG 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3801 LARGYLNDVDKTEAAFiddpawllegypghpgRQGRlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVRE 3880
Cdd:PRK07867   363 GFEGYYNDPEADAERM----------------RGGV-YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLR 425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3881 cLPEARQLAVEVILPSGQKDHAMLAafVQLEEGtqnALLDKEAGGEdsmaqvvFLASvEEELAKRlpehMVPTVFFSLLH 3960
Cdd:PRK07867   426 -YPDATEVAVYAVPDPVVGDQVMAA--LVLAPG---AKFDPDAFAE-------FLAA-QPDLGPK----QWPSYVRVCAE 487
                          490
                   ....*....|....*...
gi 1820002560 3961 FPTTTSGKTDRKRLREIG 3978
Cdd:PRK07867   488 LPRTATFKVLKRQLSAEG 505
PLN02574 PLN02574
4-coumarate--CoA ligase-like
6845-6942 4.54e-06

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 53.69  E-value: 4.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6845 SNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDG 6924
Cdd:PLN02574   391 STGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKD-GWL---------------RTGDIAYFDEDGYLYIVDRLKE 454
                           90
                   ....*....|....*...
gi 1820002560 6925 QVKVRGQRVELGEIENRL 6942
Cdd:PLN02574   455 IIKYKGFQIAPADLEAVL 472
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
3602-3970 4.74e-06

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 54.20  E-value: 4.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3602 RPENAAYIIFTSGSTGVPKGVVLEHR------AVATSCLGHGRAFGITNLSRVlqFASYTFdacIAEIITTLLCGgcICV 3675
Cdd:PRK06814   791 DPDDPAVILFTSGSEGTPKGVVLSHRnllanrAQVAARIDFSPEDKVFNALPV--FHSFGL---TGGLVLPLLSG--VKV 863
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3676 ---PSDSDRR-------NSLAKAISTMDVnwaFLTpSVARLLDPGLIPSLKILAIGGEQSSSADWNRWpgsVQK--IHV- 3742
Cdd:PRK06814   864 flyPSPLHYRiipeliyDTNATILFGTDT---FLN-GYARYAHPYDFRSLRYVFAGAEKVKEETRQTW---MEKfgIRIl 936
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3743 --YGPTECC--IFCtgyTTKQGFEPSTIGTSVASVSWVVDPenhnrLAPLGSMGELLMEGPILARGYLndvdKTEAAFID 3818
Cdd:PRK06814   937 egYGVTETApvIAL---NTPMHNKAGTVGRLLPGIEYRLEP-----VPGIDEGGRLFVRGPNVMLGYL----RAENPGVL 1004
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3819 DPawLLEGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVRECLPEARQLAVEVilPSGQ 3898
Cdd:PRK06814  1005 EP--PADGW----------YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSI--PDAR 1070
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 3899 KdhamlaafvqleeGTQNALLDKEAGGEdsmaQVVFLASVEeelAKRLPEHMVPTVFFSLLHFPTTTSGKTD 3970
Cdd:PRK06814  1071 K-------------GERIILLTTASDAT----RAAFLAHAK---AAGASELMVPAEIITIDEIPLLGTGKID 1122
PRK13382 PRK13382
bile acid CoA ligase;
7612-8122 4.76e-06

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 53.61  E-value: 4.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7612 LFAEQARARPGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 7691
Cdd:PRK13382    48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7692 PASRHEEIFEQTGAQVVV-------------ASAQYSAR---WTSSScHVVTVSKALSSQLPAVVDStntsvRPENAAYI 7755
Cdd:PRK13382   128 AGPALAEVVTREGVDTVIydeefsatvdralADCPQATRivaWTDED-HDLTVEVLIAAHAGQRPEP-----TGRKGRVI 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7756 IFTSGSTGVPKGV-------------VLEH---RA----VATSCLGHgrAFGITNLSRVLQFASYT-----FD-ACIAEI 7809
Cdd:PRK13382   202 LLTSGTTGTPKGArrsgpggigtlkaILDRtpwRAeeptVIVAPMFH--AWGFSQLVLAASLACTIvtrrrFDpEATLDL 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7810 ITTLLCGGCICVPSDSDRrnslakaisTMDVnwafltpsVARLLDPGLIPSLKILAIGGEQSSsadwnrwPGSVQKI--- 7886
Cdd:PRK13382   280 IDRHRATGLAVVPVMFDR---------IMDL--------PAEVRNRYSGRSLRFAAASGSRMR-------PDVVIAFmdq 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7887 ------HVYGPTECCIFCTGYTTKQGFEPSTIGT-SVASVSWVVDPEnHNRLaPLGSMGELLMEGPILARGYLNDVDKte 7959
Cdd:PRK13382   336 fgdviyNNYNATEAGMIATATPADLRAAPDTAGRpAEGTEIRILDQD-FREV-PTGEVGTIFVRNDTQFDGYTSGSTK-- 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7960 aAFIDdpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhHVRECLPEARQLAVEVI 8039
Cdd:PRK13382   412 -DFHD-------GF----------MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVE-KTLATHPDVAEAAVIGV 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8040 LPS--GQKnhamLAVFVQLGKGThiAHLEEKAggedsmaqvvfltgtEEELAKRLPKHMVPTVFFALLHFPMTTSGKADR 8117
Cdd:PRK13382   473 DDEqyGQR----LAAFVVLKPGA--SATPETL---------------KQHVRDNLANYKVPRDIVVLDELPRGATGKILR 531

                   ....*
gi 1820002560 8118 KRLRE 8122
Cdd:PRK13382   532 RELQA 536
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
6727-6808 5.02e-06

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 53.25  E-value: 5.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6727 ELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDILRQTGAQVILAS 6806
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80

                   ..
gi 1820002560 6807 AQ 6808
Cdd:cd05935     81 SE 82
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
2571-2695 6.07e-06

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 53.13  E-value: 6.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2571 LDPsGRSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFqRQTGGRWQQYISEHDSSSLIV----NHIHTRDTTE 2646
Cdd:cd19531     17 LEP-GSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTF-VEVDGEPVQVILPPLPLPLPVvdlsGLPEAEREAE 94
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 2647 IVEALRQ-SRGSLDIERGPVLAAVLCDAGERQS-LFVAIHHLVVDLVSWRI 2695
Cdd:cd19531     95 AQRLAREeARRPFDLARGPLLRATLLRLGEDEHvLLLTMHHIVSDGWSMGV 145
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
2583-2865 6.18e-06

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 53.15  E-value: 6.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2583 FFLELRNRVQPQLLVTALTALVQRHSMLRARFQRQTGGRWQQYISEHDSSSLIVNHIHTRDTT-----EIVEALRQSRG- 2656
Cdd:cd19539     28 GAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVRDLSDPDSDrerrlEELLRERESRGf 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2657 SLDIERgPVLAAVLCDAGERQSLFVAIHHLVVDLVSWRILLE------ELEDLLLGQTLPPALST--PFQAWH------- 2721
Cdd:cd19539    108 DLDEEP-PIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARdlaalyAARRKGPAAPLPELRQQykEYAAWQrealaap 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2722 --AAQAKYIEEHVPPSAVAQVELD---PDQLSYWGvspdDVLSsyaiseeFVLDRKTTSTLLGSCNDAFSTrPLELMVAA 2796
Cdd:cd19539    187 raAELLDFWRRRLRGAEPTALPTDrprPAGFPYPG----ADLR-------FELDAELVAALRELAKRARSS-LFMVLLAA 254
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 2797 LSYSFATiFSDRKPAAIFNEIHGReawdSSIDLTRTVGWFTSMCP--VQAANGAGLLDAIRET-KDCIRSFQ 2865
Cdd:cd19539    255 YCVLLRR-YTGQTDIVVGTPVAGR----NHPRFESTVGFFVNLLPlrVDVSDCATFRDLIARVrKALVDAQR 321
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
6712-6812 6.23e-06

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 53.34  E-value: 6.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6712 ALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 6791
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                           90       100
                   ....*....|....*....|.
gi 1820002560 6792 EDILRQTGAQVILASAQNTTL 6812
Cdd:PRK09029    93 EELLPSLTLDFALVLEGENTF 113
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
2-285 6.27e-06

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 52.72  E-value: 6.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPS-VARLLE----PSHIPSLRILVMGGEQVNSADWDR-----WPssvqTINGYGPTEccivcTGYTSeqdfT 71
Cdd:cd17630     86 GVTHVSLVPTqLQRLLDsgqgPAALKSLRAVLLGGAPIPPELLERaadrgIP----LYTTYGMTE-----TASQV----A 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   72 TGTIGTSIASVSWVVDPKDHGRLAPlgsVGELLVEGPILARGYLSDPEKTAAvfiNNPAWlleghggyagrqgrlYKTGD 151
Cdd:cd17630    153 TKRPDGFGRGGVGVLLPGRELRIVE---DGEIWVGGASLAMGYLRGQLVPEF---NEDGW---------------FTTKD 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  152 LVRYDADGNLVCLGRKDSQVKLRGQRVELGEVE------HHVREClpeakqlaveVVLP-----LGQKnhatLAAFIQLD 220
Cdd:cd17630    212 LGELHADGRLTVLGRADNMIISGGENIQPEEIEaalaahPAVRDA----------FVVGvpdeeLGQR----PVAVIVGR 277
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  221 KGTHNALLkekvggddsiarvvflagvEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:cd17630    278 GPADPAEL-------------------RAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
PRK03584 PRK03584
acetoacetate--CoA ligase;
6708-6771 6.48e-06

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 53.26  E-value: 6.48e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 6708 FTEQAL--ARPNAPAVCAW--DG---ELTYGELEALSTKLAGHLVQLGVKPEDVV----PLCFEksmwTVVAMLA 6771
Cdd:PRK03584    88 YAENLLrhRRDDRPAIIFRgeDGprrELSWAELRRQVAALAAALRALGVGPGDRVaaylPNIPE----TVVAMLA 158
PRK07529 PRK07529
AMP-binding domain protein; Validated
3464-3976 6.80e-06

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 53.42  E-value: 6.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3464 HDLFTEQAKARPHAPAIC------AWDG--ELTYGELDALSSKLASHLVQLGVNPEDVV----PLCFEksmwTVVAMLAV 3531
Cdd:PRK07529    28 YELLSRAAARHPDAPALSflldadPLDRpeTWTYAELLADVTRTANLLHSLGVGPGDVVafllPNLPE----THFALWGG 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3532 LKAGGAFvP----LDPDHPAsrheEIFEQTGAQVVVA-----------SAQYSARWTSSSCHVVTVskALSSQLPAVVDS 3596
Cdd:PRK07529   104 EAAGIAN-PinplLEPEQIA----ELLRAAGAKVLVTlgpfpgtdiwqKVAEVLAALPELRTVVEV--DLARYLPGPKRL 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3597 TNTSVRPENAAYII----------------------------F-TSGSTGVPKGVVLEHRAVATSCLGHGRAFGITnLSR 3647
Cdd:PRK07529   177 AVPLIRRKAHARILdfdaelarqpgdrlfsgrpigpddvaayFhTGGTTGMPKLAQHTHGNEVANAWLGALLLGLG-PGD 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3648 VLQFASYTF--DACIAEIITTLLCGGCICVPSDSDRRN-----SLAKAISTMDVNWAFLTPSV-ARLL----DPGLIPSL 3715
Cdd:PRK07529   256 TVFCGLPLFhvNALLVTGLAPLARGAHVVLATPQGYRGpgviaNFWKIVERYRINFLSGVPTVyAALLqvpvDGHDISSL 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3716 KILAIGGEQSSSADWNRWPGS--VQKIHVYGPTEC-CIFCTGYTTKQgFEPSTIG-----TSVASVswVVDPENHN-RLA 3786
Cdd:PRK07529   336 RYALCGAAPLPVEVFRRFEAAtgVRIVEGYGLTEAtCVSSVNPPDGE-RRIGSVGlrlpyQRVRVV--ILDDAGRYlRDC 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3787 PLGSMGELLMEGPILARGYLNDvDKTEAAFIDDpAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGR-KDsqVKVR 3865
Cdd:PRK07529   413 AVDEVGVLCIAGPNVFSGYLEA-AHNKGLWLED-GWL---------------NTGDLGRIDADGYFWLTGRaKD--LIIR 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3866 -GQRVELGEVE----HHvreclpEARQLAVEVilpsGQKD-HA--MLAAFVQLEEGTQnalldkeaggedsmaqvVFLAS 3937
Cdd:PRK07529   474 gGHNIDPAAIEeallRH------PAVALAAAV----GRPDaHAgeLPVAYVQLKPGAS-----------------ATEAE 526
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 1820002560 3938 VEEELAKRLPEH-MVPTVFFSLLHFPTTTSGKTDRKRLRE 3976
Cdd:PRK07529   527 LLAFARDHIAERaAVPKHVRILDALPKTAVGKIFKPALRR 566
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
6851-7051 7.04e-06

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 53.22  E-value: 7.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLV---EGPILARGYLNDADKTAAAFVNdpAWlveghgkhpgrrgrlYKTGDLVYYNKDGNLVYIGRKDGQVK 6927
Cdd:PRK06155   365 PDGEPGELLLradEPFAFATGYFGMPEKTVEAWRN--LW---------------FHTGDRVVRDADGWFRFVDRIKDAIR 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6928 VRGQRVELGEIENRLREcmpratqmaveviSPAGAAeqaktmvVAFLQLNDEardalLGGnvpnDDNLSAQVVFPAKVDE 7007
Cdd:PRK06155   428 RRGENISSFEVEQVLLS-------------HPAVAA-------AAVFPVPSE-----LGE----DEVMAAVVLRDGTALE 478
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 7008 KLSnlLPSYMMPEV-YFAVP-------QLPMMISGKTDRKRLREIGasFTAQ 7051
Cdd:PRK06155   479 PVA--LVRHCEPRLaYFAVPryvefvaALPKTENGKVQKFVLREQG--VTAD 526
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
3602-3977 7.57e-06

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 53.18  E-value: 7.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3602 RPENAAYIIFTSGSTGVPKGVVLEH----------RAVA--------TSCLGHGRAFGITnlsrvlqfasytfdaciAEI 3663
Cdd:PRK08043   363 QPEDAALILFTSGSEGHPKGVVHSHksllanveqiKTIAdftpndrfMSALPLFHSFGLT-----------------VGL 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3664 ITTLLCGGCICV-PSD----------SDRRNSLAKAISTMDVNWafltpsvARLLDPGLIPSLKILAIGGEQSSSADWNR 3732
Cdd:PRK08043   426 FTPLLTGAEVFLyPSPlhyrivpelvYDRNCTVLFGTSTFLGNY-------ARFANPYDFARLRYVVAGAEKLQESTKQL 498
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3733 WPGS--VQKIHVYGPTECCIfCTGYTTKQGFEPSTIGTsvasvswvVDPENHNRLAPLGSM---GELLMEGPILARGYLN 3807
Cdd:PRK08043   499 WQDKfgLRILEGYGVTECAP-VVSINVPMAAKPGTVGR--------ILPGMDARLLSVPGIeqgGRLQLKGPNIMNGYLR 569
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3808 dvdkteaafIDDPAwLLEGyPGHPGRQGRL----YKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVRECLP 3883
Cdd:PRK08043   570 ---------VEKPG-VLEV-PTAENARGEMergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSP 638
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3884 EARQLAveVILPSGQKDHAmLAAFvqleegTQNALLDKEAggedsmaqvvfLASVEEELAkrLPEHMVPTVFFSLLHFPT 3963
Cdd:PRK08043   639 DKQHAT--AIKSDASKGEA-LVLF------TTDSELTREK-----------LQQYAREHG--VPELAVPRDIRYLKQLPL 696
                          410
                   ....*....|....
gi 1820002560 3964 TTSGKTDRKRLREI 3977
Cdd:PRK08043   697 LGSGKPDFVTLKSM 710
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1626-1782 7.81e-06

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 52.84  E-value: 7.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1626 HHAVYDGWSLPLILHAVKQVYSGGVLQWQPSfnafiQYL---GQQ-------DLEATVAYWQTALADCEAV--LFPtLPP 1693
Cdd:cd19532    130 HHIAMDGVSFQIFLRDLERAYNGQPLLPPPL-----QYLdfaARQrqdyesgALDEDLAYWKSEFSTLPEPlpLLP-FAK 203
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1694 TVTQPVADA----TVEYQcppLSKATSDT--TTSTLIR--------AAWAIVTSRYTTSDDVVFGTTVTGRNTPvtGVEA 1759
Cdd:cd19532    204 VKSRPPLTRydthTAERR---LDAALAARikEASRKLRvtpfhfylAALQVLLARLLDVDDICIGIADANRTDE--DFME 278
                          170       180
                   ....*....|....*....|...
gi 1820002560 1760 MVGPTIATVPVRLRVQRDQTvFA 1782
Cdd:cd19532    279 TIGFFLNLLPLRFRRDPSQT-FA 300
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
1952-2157 8.78e-06

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 52.74  E-value: 8.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1952 DGELTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDpdhpasrhediFRQTGAQVVv 2031
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN-----------YNLRGESLA- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2032 tsaqHSARWIGTNHQVVTvsagsleqfstlvnpvdlpakpenAAYVMFTSGSTGTPKGVVLEHR---------------- 2095
Cdd:cd05940     69 ----HCLNVSSAKHLVVD------------------------AALYIYTSGTTGLPKAAIISHRrawrggaffagsggal 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2096 --------------AVVTSCLGHGQAFGVTNLLRAlQFTAYTF-DVCIAEIITTLVHGGCIC------VPSDSERRDNLA 2154
Cdd:cd05940    121 psdvlytclplyhsTALIVGWSACLASGATLVIRK-KFSASNFwDDIRKYQATIFQYIGELCryllnqPPKPTERKHKVR 199

                   ...
gi 1820002560 2155 KAI 2157
Cdd:cd05940    200 MIF 202
PLN02736 PLN02736
long-chain acyl-CoA synthetase
847-1228 8.85e-06

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 53.18  E-value: 8.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  847 PPAVD-RCIHDLFAEQARARPD----ASAVCAwDGE------LTYGELDELSSKLAAHLVQLGVKREDVVPLCF-EKSMW 914
Cdd:PLN02736    38 PDHPEiGTLHDNFVYAVETFRDykylGTRIRV-DGTvgeykwMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFiNRPEW 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  915 TVV--AMLAVLKAGgafVPLdpghpasrheeiFKQIGAQVVLTSSQHAML---FASSERHQVTVSKVS------------ 977
Cdd:PLN02736   117 LIVdhACSAYSYVS---VPL------------YDTLGPDAVKFIVNHAEVaaiFCVPQTLNTLLSCLSeipsvrlivvvg 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  978 --TSQLPT--------VVNFAK------------SPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLGHGEA--FGY 1033
Cdd:PLN02736   182 gaDEPLPSlpsgtgveIVTYSKllaqgrsspqpfRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLStkFYP 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1034 TDharvlQFASYTFDACIAE---IITTLLYGgcicVPSESDRRNNLakaiSTMDvNCALLTP----SVARL--------- 1097
Cdd:PLN02736   262 SD-----VHISYLPLAHIYErvnQIVMLHYG----VAVGFYQGDNL----KLMD-DLAALRPtifcSVPRLynriydgit 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1098 ------------LEPSAVPSLKRLVLQGEQVSfADWNR---------WPGSVQTI------------------------N 1132
Cdd:PLN02736   328 navkesgglkerLFNAAYNAKKQALENGKNPS-PMWDRlvfnkikakLGGRVRFMssgasplspdvmeflricfggrvlE 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1133 GYGPTECSvcCNTYSGKQG-FKSGIIGTSVAS----LSWVVDAGNHNRLAPLGSiGELLVEGPILARGYLNDIDKTEAAf 1207
Cdd:PLN02736   407 GYGMTETS--CVISGMDEGdNLSGHVGSPNPAcevkLVDVPEMNYTSEDQPYPR-GEICVRGPIIFKGYYKDEVQTREV- 482
                          490       500
                   ....*....|....*....|.
gi 1820002560 1208 IDDPAWLLEGYEGHAGRRGRL 1228
Cdd:PLN02736   483 IDEDGWLHTGDIGLWLPGGRL 503
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
4566-4958 8.95e-06

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 52.74  E-value: 8.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4566 ELTYGELDTLSSKLASHLV-QLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLA 4644
Cdd:cd05905     14 TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4645 S-AQYATLWTSLGRSV---------------VIVSEASTSQLPVVTKTADPSVNPGNAAYAIFTSGSTGIPKGVVLEHKA 4708
Cdd:cd05905     94 VeACLKGLPKKLLKSKtaaeiakkkgwpkilDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4709 VVTSCLGHGQA---------FGITDHTRVLQFasytFDACIAEI---ITTLLCcgcicvpSDSDRRNNLA---------K 4767
Cdd:cd05905    174 LLAHCRALKEAcelyesrplVTVLDFKSGLGL----WHGCLLSVysgHHTILI-------PPELMKTNPLlwlqtlsqyK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4768 AINAM----DVNWALLTPSV---ARMLDPCVVQSLK-ILVLGGEQVNSADWDRWPKSIQTINaYGPTECS---------- 4829
Cdd:cd05905    243 VRDAYvklrTLHWCLKDLSStlaSLKNRDVNLSSLRmCMVPCENRPRISSCDSFLKLFQTLG-LSPRAVStefgtrvnpf 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4830 ICCTTYSG---------KQGFKSGTI----------------GTSIVSVSW-VVDPENHNRLAPlGSIGELLVEGPILAR 4883
Cdd:cd05905    322 ICWQGTSGpepsrvyldMRALRHGVVrlderdkpnslplqdsGKVLPGAQVaIVNPETKGLCKD-GEIGEIWVNSPANAS 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4884 GY--LNDMekTEAAFIDDPAWLL-EGYGGHS----GRQGRLYKTGDLVRYDADGNLVY-LGRKDSQVKLRGQRvelgeve 4955
Cdd:cd05905    401 GYflLDGE--TNDTFKVFPSTRLsTGITNNSyartGLLGFLRPTKCTDLNVEEHDLLFvVGSIDETLEVRGLR------- 471

                   ...
gi 1820002560 4956 HHV 4958
Cdd:cd05905    472 HHP 474
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
3149-3322 9.35e-06

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 52.36  E-value: 9.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3149 LCLDINHAIIDAHSRGILMHDLQEAYDANLNPQSTS-------FRDFASYIKQQSQEEAGR----YWAEYLDGVEPCFF- 3216
Cdd:cd19531    129 LLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPlpplpiqYADYAVWQREWLQGEVLErqlaYWREQLAGAPPVLEl 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3217 ------PSLGDSGGANtipRTVEVPSIDSSAVHMFCKIWEVTPATIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPihNV 3290
Cdd:cd19531    209 ptdrprPAVQSFRGAR---VRFTLPAELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRA--EL 283
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1820002560 3291 NSIFGPLISILPCRIHLHKQLTVLEALKTVQE 3322
Cdd:cd19531    284 EGLIGFFVNTLVLRTDLSGDPTFRELLARVRE 315
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
90-284 9.60e-06

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 52.76  E-value: 9.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   90 DHGRLAPLGSVGELLVE---GPILARGYLSDPEKTAAVFINNpAWLLEGHGGYAgrqgrlyktgdlvryDADGNLVCLGR 166
Cdd:PRK08008   356 DHNRPLPAGEIGEICIKgvpGKTIFKEYYLDPKATAKVLEAD-GWLHTGDTGYV---------------DEEGFFYFVDR 419
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  167 KDSQVKLRGQRVELGEVEhHVRECLPEAKQLAVevvlpLGQKNH---ATLAAFIQLDKGThnallkekvggddSIARVVF 243
Cdd:PRK08008   420 RCNMIKRGGENVSCVELE-NIIATHPKIQDIVV-----VGIKDSirdEAIKAFVVLNEGE-------------TLSEEEF 480
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1820002560  244 LAGVEEELAkrlpKHMVPTVFFALLHFPTTTSGKTDRKRLR 284
Cdd:PRK08008   481 FAFCEQNMA----KFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
8-298 9.65e-06

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 52.88  E-value: 9.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    8 LTPSVARLLEP--------SHIPSLRILVMGGEQVNSADWdRW------PSSVQTINGYGPTE------CCIVCTGyTSE 67
Cdd:cd05968    335 LSPTLIRALKPrgdapvnaHDLSSLRVLGSTGEPWNPEPW-NWlfetvgKGRNPIINYSGGTEisggilGNVLIKP-IKP 412
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   68 QDFTTGTIGTSIAsvswVVDpkDHGRLAPlGSVGELLVEGPI--LARGYLSDPEKTaavfinnpawllegHGGYAGRQGR 145
Cdd:cd05968    413 SSFNGPVPGMKAD----VLD--ESGKPAR-PEVGELVLLAPWpgMTRGFWRDEDRY--------------LETYWSRFDN 471
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  146 LYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVE------HHVREClpeakqLAVEVVLPL-GQKNHatlaAFIQ 218
Cdd:cd05968    472 VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIEsvlnahPAVLES------AAIGVPHPVkGEAIV----CFVV 541
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  219 LDKGthnallkekvggddsiarVVFLAGVEEELAKRLPKHM----VPTVFFALLHFPTTTSGKTDRKRLReigASFTAQQ 294
Cdd:cd05968    542 LKPG------------------VTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVIR---AAYLGKE 600

                   ....
gi 1820002560  295 LAEM 298
Cdd:cd05968    601 LGDL 604
PRK05857 PRK05857
fatty acid--CoA ligase;
7-198 9.93e-06

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 52.70  E-value: 9.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    7 LLTPSVARL-LEPSHIPSLRILVMGGEQVNSADWdRW--PSSVQTINGYGPTE--CCIVC--TGYTSEQDFTTGTIGTSI 79
Cdd:PRK05857   270 LLSKLVSELkSANATVPSLRLVGYGGSRAIAADV-RFieATGVRTAQVYGLSEtgCTALClpTDDGSIVKIEAGAVGRPY 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   80 ASVSWVVDPKDHG-----RLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINnpAWLleghggyagrqgrlyKTGDLVR 154
Cdd:PRK05857   349 PGVDVYLAATDGIgptapGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID--GWV---------------NTGDLLE 411
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1820002560  155 YDADGNLVCLGRKDSQVKLRGQRVELGEVEhHVRECLPEAKQLA 198
Cdd:PRK05857   412 RREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGVSGVREAA 454
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
3476-3975 9.97e-06

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 52.82  E-value: 9.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3476 HAPAICAWdgELTYGELDALSSKLASHLVQLgVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL-DPDHPAsrHEEIF 3554
Cdd:PRK12476    60 HSAAGCAV--ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPG--HAERL 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3555 EqtgaqVVVASAQYSARWTSSSC-----------------HVVTVSkalssqlpAVVDSTNTSVRP-----ENAAYIIFT 3612
Cdd:PRK12476   135 D-----TALRDAEPTVVLTTTAAaeavegflrnlprlrrpRVIAID--------AIPDSAGESFVPveldtDDVSHLQYT 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3613 SGSTGVPKGVVLEHRAVATSCLghGRAFGITNLSRVLQFASYT---FDACIAEIITTLLCGGCICV--PSDSDRR----- 3682
Cdd:PRK12476   202 SGSTRPPVGVEITHRAVGTNLV--QMILSIDLLDRNTHGVSWLplyHDMGLSMIGFPAVYGGHSTLmsPTAFVRRpqrwi 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3683 NSLAKAISTMDV-----NWAFLTPSVARLLDPG--LIPSLKILAIGGEQSSSADWNRW---------PGSVQKIHvYGPT 3746
Cdd:PRK12476   280 KALSEGSRTGRVvtaapNFAYEWAAQRGLPAEGddIDLSNVVLIIGSEPVSIDAVTTFnkafapyglPRTAFKPS-YGIA 358
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3747 ECCIFCTgyTTKQGFEPSTI-------------------GTSVASVS--------W--VVDPENHNRLaPLGSMGELLME 3797
Cdd:PRK12476   359 EATLFVA--TIAPDAEPSVVyldreqlgagravrvaadaPNAVAHVScgqvarsqWavIVDPDTGAEL-PDGEVGEIWLH 435
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3798 GPILARGYLNDVDKTEAAFIDD-PAWLLEGypGHPGR---QGRLYKTGDLVQYnADGNLVYLGRKDSQVKVRGQRVELGE 3873
Cdd:PRK12476   436 GDNIGRGYWGRPEETERTFGAKlQSRLAEG--SHADGaadDGTWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQD 512
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3874 VEHHVRECLPEARQLAVevilpsgqkdhamlAAF-VQLEEGTQNALLDKEAGGEDSMAQVVFLASVEEELAKRlpeHMVP 3952
Cdd:PRK12476   513 IEATVAEASPMVRRGYV--------------TAFtVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRR---HGLA 575
                          570       580
                   ....*....|....*....|....*.
gi 1820002560 3953 TVFFSLLH---FPTTTSGKTDRKRLR 3975
Cdd:PRK12476   576 VADVRLVPagaIPRTTSGKLARRACR 601
PRK07787 PRK07787
acyl-CoA synthetase; Validated
6718-6807 1.02e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 52.68  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6718 APAVCAWDGELTYGELEALSTKLAGhlvqlGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEDILRQ 6797
Cdd:PRK07787    16 ADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILAD 90
                           90
                   ....*....|
gi 1820002560 6798 TGAQVILASA 6807
Cdd:PRK07787    91 SGAQAWLGPA 100
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
7208-7473 1.03e-05

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 52.19  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7208 VLELRADVDEDVFCAAWEHVVQSTAALRTRIVQhSELGLLQVVVEE--KIQWTESEALEEYL-KEDKavsmglgdpLAHY 7284
Cdd:cd19537     29 ACRLSGDVDRDRLASAWNTVLARHRILRSRYVP-RDGGLRRSYSSSppRVQRVDTLDVWKEInRPFD---------LERE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7285 ALVkeawggkRWF------VWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSfnafiQYLG-----QQDLEATAAYWQ 7353
Cdd:cd19537     99 DPI-------RVFispdtlLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRR-----EYLDstawsRPASPEDLDFWS 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7354 TALSDCEAVLFPPLPSTVTqpVADTTVEYQCPP-LSKATLDTTTST------LIRAAWAIVTSCYTSSDDVVYGTTVTGR 7426
Cdd:cd19537    167 EYLSGLPLLNLPRRTSSKS--YRGTSRVFQLPGsLYRSLLQFSTSSgitlhqLALAAVALALQDLSDRTDIVLGAPYLNR 244
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 7427 NAPiaGVEAMVG----PtiatVPVRLRV--QRDQTVFAFLQGLQQQSTDMIAH 7473
Cdd:cd19537    245 TSE--EDMETVGlfleP----LPIRIRFpsSSDASAADFLRAVRRSSQAALAH 291
PRK06145 PRK06145
acyl-CoA synthetase; Validated
6851-7043 1.03e-05

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 52.58  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFVNDpaWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:PRK06145   341 PPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--WF---------------RSGDVGYLDEEGFLYLTDRKKDMIISGG 403
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6931 QRVELGEIENRLREcMPRATQMAVEVISPAGAAEQAKTMVVAflqlndeardallggnvpnddNLSAQVVFPAkVDEKLS 7010
Cdd:PRK06145   404 ENIASSEVERVIYE-LPEVAEAAVIGVHDDRWGERITAVVVL---------------------NPGATLTLEA-LDRHCR 460
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1820002560 7011 NLLPSYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:PRK06145   461 QRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
13-279 1.05e-05

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 53.05  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   13 ARLLEPSHIPSLRILVMGGEQVNSADWDRWPSS--VQTINGYGPTECCIVCTGYTSEQdFTTGTIGTSIasvswvvdPKD 90
Cdd:PRK06814   898 ARYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKfgIRILEGYGVTETAPVIALNTPMH-NKAGTVGRLL--------PGI 968
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   91 HGRLAPLGSV---GELLVEGPILARGYLsDPEktaavfinNPAWLLEGHGGYagrqgrlYKTGDLVRYDADGNLVCLGRK 167
Cdd:PRK06814   969 EYRLEPVPGIdegGRLFVRGPNVMLGYL-RAE--------NPGVLEPPADGW-------YDTGDIVTIDEEGFITIKGRA 1032
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  168 DSQVKLRGQRVELGEVEHHVRECLPEAKQLAVEVvlPLGQknhatlaafiqldKGTHNALLKEKVGgddsIARVVFLAGV 247
Cdd:PRK06814  1033 KRFAKIAGEMISLAAVEELAAELWPDALHAAVSI--PDAR-------------KGERIILLTTASD----ATRAAFLAHA 1093
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1820002560  248 EeelAKRLPKHMVPTVFFALLHFPTTTSGKTD 279
Cdd:PRK06814  1094 K---AAGASELMVPAEIITIDEIPLLGTGKID 1122
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
6848-7043 1.06e-05

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 52.35  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6848 ALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDpaWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVK 6927
Cdd:cd05912    258 DGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENG--WF---------------KTGDIGYLDEEGFLYVLDRRSDLII 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6928 VRGQRVELGEIENRLrecmpratqMAVEVISPAGaaeqaktmVVAflQLNDEardallGGNVPNDDNLSAQVVFPAKVDE 7007
Cdd:cd05912    321 SGGENIYPAEIEEVL---------LSHPAIKEAG--------VVG--IPDDK------WGQVPVAFVVSERPISEEELIA 375
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1820002560 7008 KLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:cd05912    376 YCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
6856-7043 1.13e-05

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 51.56  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6856 GELLVEGPILARGYLNDADKTAaafVNDPAWlveghgkhpgrrgrlYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVEL 6935
Cdd:cd17630    179 GEIWVGGASLAMGYLRGQLVPE---FNEDGW---------------FTTKDLGELHADGRLTVLGRADNMIISGGENIQP 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6936 GEIENRLrecmprATQMAVEVISPAGAA-EQAKTMVVAFLQLNDEARdallggnvpnddnlsaqvvfPAKVDEKLSNLLP 7014
Cdd:cd17630    241 EEIEAAL------AAHPAVRDAFVVGVPdEELGQRPVAVIVGRGPAD--------------------PAELRAWLKDKLA 294
                          170       180
                   ....*....|....*....|....*....
gi 1820002560 7015 SYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:cd17630    295 RFKLPKRIYPVPELPRTGGGKVDRRALRA 323
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
6851-7044 1.15e-05

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 52.12  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEG--PILARGYLNDADKTAAAFVNdpAWlveghgkhpgrrgrlYKTGDLVYYNKDGNLVYIGRKDGQVKV 6928
Cdd:cd05969    282 PPGTKGILALKPgwPSMFRGIWNDEERYKNSFID--GW---------------YLTGDLAYRDEDGYFWFVGRADDIIKT 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6929 RGQRVELGEIENRLREcmpratQMAVEVISPAGAAEQAK-TMVVAFLQLNDeardallgGNVPNDDnLSAQVVFPAKVDe 7007
Cdd:cd05969    345 SGHRVGPFEVESALME------HPAVAEAGVIGKPDPLRgEIIKAFISLKE--------GFEPSDE-LKEEIINFVRQK- 408
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1820002560 7008 klsnlLPSYMMP-EVYFaVPQLPMMISGKTDRKRLREI 7044
Cdd:cd05969    409 -----LGAHVAPrEIEF-VDNLPKTRSGKIMRRVLKAK 440
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
6841-6919 1.23e-05

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 52.24  E-value: 1.23e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 6841 FVRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLvYI 6919
Cdd:cd05904    344 IVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKE-GWL---------------HTGDLCYIDEDGYL-FI 405
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
6729-6817 1.25e-05

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 52.44  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6729 TYGELEALSTKLAGHLVQLGVKPEDVVplCFEKSMWT--VVAMLAVLKAGGAFVPLDpdhPASRHEDI---LRQTGAQVI 6803
Cdd:PRK06087    51 TYSALDHAASRLANWLLAKGIEPGDRV--AFQLPGWCefTIIYLACLKVGAVSVPLL---PSWREAELvwvLNKCQAKMF 125
                           90
                   ....*....|....
gi 1820002560 6804 LASaqntTLFQSSN 6817
Cdd:PRK06087   126 FAP----TLFKQTR 135
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
3469-3976 1.34e-05

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 52.08  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3469 EQAKARPHAPAICAWDG---EL--TYGELDALSSKLASHLVQL-GVNPEDVVPLCFEK-SMWTVVAmLAVLKAGGAFVPL 3541
Cdd:cd05928     19 EKAGKRPPNPALWWVNGkgdEVkwSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRvPEWWLVN-VACIRTGLVFIPG 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3542 DPDHPASRHEEIFEQTGAQVVVASAQYSARWTS--SSCHVVTvSKALSS-----------QLPAVVDSTNTSVR--PENA 3606
Cdd:cd05928     98 TIQLTAKDILYRLQASKAKCIVTSDELAPEVDSvaSECPSLK-TKLLVSeksrdgwlnfkELLNEASTEHHCVEtgSQEP 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3607 AYIIFTSGSTGVPKgvVLEHravATSCLGHGRAFG---ITNL--SRVLQFASYT--FDACIAEIITTLLCGGCICVPS-- 3677
Cdd:cd05928    177 MAIYFTSGTTGSPK--MAEH---SHSSLGLGLKVNgryWLDLtaSDIMWNTSDTgwIKSAWSSLFEPWIQGACVFVHHlp 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3678 --DSdrrNSLAKAISTMDVNWAFLTPSVARLLDPGLI-----PSLKILAIGGEQSSSADWNRWPG--SVQKIHVYGPTEC 3748
Cdd:cd05928    252 rfDP---LVILKTLSSYPITTFCGAPTVYRMLVQQDLssykfPSLQHCVTGGEPLNPEVLEKWKAqtGLDIYEGYGQTET 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3749 CIFCTGYTTKQgFEPSTIGTSVASVSWVVDPENHNRLAPlGSMGELLME-GPI----LARGYLNDVDKTEAAFiddpawl 3823
Cdd:cd05928    329 GLICANFKGMK-IKPGSMGKASPPYDVQIIDDNGNVLPP-GTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATI------- 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3824 legypghpgrQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKDHaM 3903
Cdd:cd05928    400 ----------RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIE-HPAVVESAV-VSSPDPIRGE-V 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3904 LAAFVQLEEGtqnalldkeaggedsmaqvvFLASVEEELAKRLPEHM--------VPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd05928    467 VKAFVVLAPQ--------------------FLSHDPEQLTKELQQHVksvtapykYPRKVEFVQELPKTVTGKIQRNELR 526

                   .
gi 1820002560 3976 E 3976
Cdd:cd05928    527 D 527
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
6694-6803 1.36e-05

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 52.33  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6694 AELPLAVDRCVHDLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVL 6773
Cdd:PRK07059    15 AEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
                           90       100       110
                   ....*....|....*....|....*....|
gi 1820002560 6774 KAGGAFVPLDPDHPASRHEDILRQTGAQVI 6803
Cdd:PRK07059    95 RAGYVVVNVNPLYTPRELEHQLKDSGAEAI 124
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
9-284 1.37e-05

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 52.14  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    9 TPSVARLLEPSHIP-------SLRILVMGGEQVNSA--DWDRWPSSVQTINGYGPTEC-CIVCTGYTSEQDFTTGTIGTS 78
Cdd:cd05973    185 SPTAYRLLMAAGAEvparpkgRLRRVSSAGEPLTPEviRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVHAGSAGRA 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   79 IASVSWVVdPKDHGRLAPLGSVGELLVE---GPILA-RGYLSDPEKTAAvfinnpawlleghggyagrqGRLYKTGDLVR 154
Cdd:cd05973    265 MPGWRVAV-LDDDGDELGPGEPGRLAIDianSPLMWfRGYQLPDTPAID--------------------GGYYLTGDTVE 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  155 YDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAVeVVLPLGQKNHaTLAAFIQLDKGTHNAllkekvgg 234
Cdd:cd05973    324 FDPDGSFSFIGRADDVITMSGYRIGPFDVESALIE-HPAVAEAAV-IGVPDPERTE-VVKAFVVLRGGHEGT-------- 392
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  235 ddsiarvvflAGVEEELA----KRLPKHMVP-TVFFaLLHFPTTTSGKTDRKRLR 284
Cdd:cd05973    393 ----------PALADELQlhvkKRLSAHAYPrTIHF-VDELPKTPSGKIQRFLLR 436
PRK08316 PRK08316
acyl-CoA synthetase; Validated
6706-6807 1.47e-05

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 52.24  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6706 DLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP---- 6781
Cdd:PRK08316    15 DILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPvnfm 94
                           90       100
                   ....*....|....*....|....*.
gi 1820002560 6782 LDPDHPASrhedILRQTGAQVILASA 6807
Cdd:PRK08316    95 LTGEELAY----ILDHSGARAFLVDP 116
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
51-199 1.64e-05

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 51.15  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   51 GYGPTECcivcTGYTSEQDFTTGTIGTSIASVSWV----VDPKdhGRLAPLGSVGELLVEGPILARGYLSDPEKTAAvfi 126
Cdd:cd17636    142 GYGQTEV----MGLATFAALGGGAIGGAGRPSPLVqvriLDED--GREVPDGEVGEIVARGPTVMAGYWNRPEVNAR--- 212
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560  127 nnpawlleghggyagRQ-GRLYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEAKQLAV 199
Cdd:cd17636    213 ---------------RTrGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQ-HPAVADAAV 270
PRK07470 PRK07470
acyl-CoA synthetase; Validated
7613-7790 1.77e-05

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 51.97  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7613 FAEQARAR-PGAPAICAWDGELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP----L 7687
Cdd:PRK07470    12 FLRQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPtnfrQ 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7688 DPDHPASrheeIFEQTGAQVVVASAQYS--ARWTSSSC----HVVTVSKALSSQ-LPAVVDStNTSVRPENAA------- 7753
Cdd:PRK07470    92 TPDEVAY----LAEASGARAMICHADFPehAAAVRAASpdltHVVAIGGARAGLdYEALVAR-HLGARVANAAvdhddpc 166
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1820002560 7754 YIIFTSGSTGVPKGVVLEHravatsclgHGRAFGITN 7790
Cdd:PRK07470   167 WFFFTSGTTGRPKAAVLTH---------GQMAFVITN 194
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
99-285 1.89e-05

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 51.53  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   99 SVGELLVEGPILARGYLSDPEKTAAVFinnpawllegHGGYagrqgrlYKTGDLVRYDADGNLvclgrkdsQVKLR---- 174
Cdd:cd12118    338 TIGEIVFRGNIVMKGYLKNPEATAEAF----------RGGW-------FHSGDLAVIHPDGYI--------EIKDRskdi 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  175 ----GQRVELGEVE----HHvreclPEAKQLAVeVVLP---LGQknhaTLAAFIQLDKGthnallkEKVGGDDSIARVvf 243
Cdd:cd12118    393 iisgGENISSVEVEgvlyKH-----PAVLEAAV-VARPdekWGE----VPCAFVELKEG-------AKVTEEEIIAFC-- 453
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1820002560  244 lagveeelAKRLPKHMVP-TVFFalLHFPTTTSGKTDRKRLRE 285
Cdd:cd12118    454 --------REHLAGFMVPkTVVF--GELPKTSTGKIQKFVLRD 486
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
6157-6229 1.93e-05

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 46.47  E-value: 1.93e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560  6157 PKRQPSTEAEQTMQKLWAQVLGIE-LNGIGLDDSFFRLGGDSIAAMKLVGE-ARRIGLQLSVADIFRYARLVDLA 6229
Cdd:smart00823    5 PPAERRRLLLDLVREQVAAVLGHAaAEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALA 79
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
6712-6823 2.06e-05

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 51.47  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6712 ALARPNAPA-VCAWDG-ELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdHPAS 6789
Cdd:cd05904     15 ASAHPSRPAlIDAATGrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA---NPLS 91
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1820002560 6790 RHEDILRQ---TGAQVILASAQNTTLFQSSNQTVVTV 6823
Cdd:cd05904     92 TPAEIAKQvkdSGAKLAFTTAELAEKLASLALPVVLL 128
PRK07529 PRK07529
AMP-binding domain protein; Validated
7586-8005 2.07e-05

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 51.88  E-value: 2.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7586 TTPEDRQQLWA--WNADVPPAierCVHDLFAEQARARPGAPAIC------AWDG--ELTYGEL--DVL-SSNLaghLVQL 7652
Cdd:PRK07529     5 ATLADIEAIEAvpLAARDLPA---STYELLSRAAARHPDAPALSflldadPLDRpeTWTYAELlaDVTrTANL---LHSL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7653 GVNPEDVV----PLCFEksmwTVVAMLAVLKAGGAFvP----LDPDHPAsrheEIFEQTGAQVVVA-----------SAQ 7713
Cdd:PRK07529    79 GVGPGDVVafllPNLPE----THFALWGGEAAGIAN-PinplLEPEQIA----ELLRAAGAKVLVTlgpfpgtdiwqKVA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7714 YSARWTSSSCHVVTVskALSSQLPAVVDSTNTSVRPENAAYII----------------------------F-TSGSTGV 7764
Cdd:PRK07529   150 EVLAALPELRTVVEV--DLARYLPGPKRLAVPLIRRKAHARILdfdaelarqpgdrlfsgrpigpddvaayFhTGGTTGM 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7765 PKGVVLEHRAVATSCLGHGRAFGITnLSRVLQFASYTF--DACIAEIITTLLCGGCICVPSDSDRRN-----SLAKAIST 7837
Cdd:PRK07529   228 PKLAQHTHGNEVANAWLGALLLGLG-PGDTVFCGLPLFhvNALLVTGLAPLARGAHVVLATPQGYRGpgviaNFWKIVER 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7838 MDVNWAFLTPSV-ARLL----DPGLIPSLKILAIGGEQSSSADWNRWPGS--VQKIHVYGPTEC-CIFCTGYTTKQgFEP 7909
Cdd:PRK07529   307 YRINFLSGVPTVyAALLqvpvDGHDISSLRYALCGAAPLPVEVFRRFEAAtgVRIVEGYGLTEAtCVSSVNPPDGE-RRI 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7910 STIG-----TSVASVswVVDPENHN-RLAPLGSMGELLMEGPILARGYLNDvDKTEAAFIDDpAWLlegypghpgrqgrl 7983
Cdd:PRK07529   386 GSVGlrlpyQRVRVV--ILDDAGRYlRDCAVDEVGVLCIAGPNVFSGYLEA-AHNKGLWLED-GWL-------------- 447
                          490       500
                   ....*....|....*....|...
gi 1820002560 7984 yKTGDLVQYNADGNLVYLGR-KD 8005
Cdd:PRK07529   448 -NTGDLGRIDADGYFWLTGRaKD 469
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
7206-7403 2.21e-05

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 51.48  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7206 QSV-LELRADVDEDVFCAAWEHVVQSTAALRTRIVQHS----------ELGLLQVVVEEKIQWTESEALEEyLKEDKAVS 7274
Cdd:cd19534     24 QSVlLRVPQGLDPDALRQALRALVEHHDALRMRFRREDggwqqrirgdVEELFRLEVVDLSSLAQAAAIEA-LAAEAQSS 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7275 MGLGD-PLAHYALVKEAWGGKRwFVWTIHHALYDGGSLPLIL----HAVKQVYSG--AVLERQPSFNAFIQ----YLGQQ 7343
Cdd:cd19534    103 LDLEEgPLLAAALFDGTDGGDR-LLLVIHHLVVDGVSWRILLedleAAYEQALAGepIPLPSKTSFQTWAEllaeYAQSP 181
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 7344 DLEATAAYWQTALSDceavLFPPLPSTVTQPVADTTVEyqcpplsKATLD-TTTSTLIRAA 7403
Cdd:cd19534    182 ALLEELAYWRELPAA----DYWGLPKDPEQTYGDARTV-------SFTLDeEETEALLQEA 231
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
6856-6945 2.30e-05

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 51.45  E-value: 2.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6856 GELLVEGPILARGYLNDADKTAAAFvNDPAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVR-GQRVE 6934
Cdd:cd17639    331 GEILIRGPNVFKGYYKNPEKTKEAF-DGDGWF---------------HTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIA 394
                           90
                   ....*....|.
gi 1820002560 6935 LGEIENRLREC 6945
Cdd:cd17639    395 LEKLESIYRSN 405
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
6850-7042 2.31e-05

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 51.61  E-value: 2.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6850 APLGSIGELLVEG---PILARGYLNDADKTAAAFVNDpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQV 6926
Cdd:PRK08008   361 LPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEAD-GWL---------------HTGDTGYVDEEGFFYFVDRRCNMI 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6927 KVRGQRVELGEIENRLrECMPRATQMAVEVIsPAGAAEQAktmVVAFLQLNDEARdallggnvpnddnLSAQVVFpAKVD 7006
Cdd:PRK08008   425 KRGGENVSCVELENII-ATHPKIQDIVVVGI-KDSIRDEA---IKAFVVLNEGET-------------LSEEEFF-AFCE 485
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1820002560 7007 EKLSNL-LPSYMmpEVyfaVPQLPMMISGKTDRKRLR 7042
Cdd:PRK08008   486 QNMAKFkVPSYL--EI---RKDLPRNCSGKIIKKNLK 517
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
2561-2689 2.61e-05

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 51.05  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2561 LTPIQH--LYLTL-DPSGRSSFDQcFFLELRNRVQPQLLVTALTALVQRHSMLRARFQRQTGGRWQQYIseHDSSSLIVN 2637
Cdd:cd19543      4 LSPMQEgmLFHSLlDPGSGAYVEQ-MVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVV--LKDRKLPWR 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560 2638 HIHTRDTTEI-----VEALR---QSRGsLDIERGPVLAAVLCDAGERQ-SLFVAIHHLVVD 2689
Cdd:cd19543     81 ELDLSHLSEAeqeaeLEALAeedRERG-FDLARAPLMRLTLIRLGDDRyRLVWSFHHILLD 140
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
2558-2739 2.78e-05

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 50.91  E-value: 2.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2558 AFDLTPIQH--LYLTLDPSGRSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFQRQTGGRWQQYISEHdssslI 2635
Cdd:cd19536      1 MYPLSSLQEgmLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQ-----A 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2636 VNHIHTRDTTEIVEALRQSRGSLDIERG---------PVLAAVLCDAGERQSLFV-AIHHLVVDLVSWRILLEELEDLLL 2705
Cdd:cd19536     76 QVPVTELDLTPLEEQLDPLRAYKEETKIrrfdlgrapLVRAALVRKDERERFLLViSDHHSILDGWSLYLLVKEILAVYN 155
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1820002560 2706 GQTLPPALSTPFQAWHAAQAKYIEEHVPPSAVAQ 2739
Cdd:cd19536    156 QLLEYKPLSLPPAQPYRDFVAHERASIQQAASER 189
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
6851-7063 2.79e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 51.32  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFvnDPAWlveghgkhpgrrgrlYKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:PRK07786   367 PVGEVGEIVYRAPTLMSGYWNNPEATAEAF--AGGW---------------FHSGDLVRQDEEGYVWVVDRKKDMIISGG 429
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6931 QRVELGEIENRLREcMPRATQMAVevispAGAAEQAKTMV-VAFLQLNDEARDALLggnvpnddnlsaqvvfpAKVDEKL 7009
Cdd:PRK07786   430 ENIYCAEVENVLAS-HPDIVEVAV-----IGRADEKWGEVpVAVAAVRNDDAALTL-----------------EDLAEFL 486
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 7010 SNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREigaSFTAQQLAEMRTSSQGP 7063
Cdd:PRK07786   487 TDRLARYKHPKALEIVDALPRNPAGKVLKTELRE---RYGACVNVERRSASAGF 537
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
6845-7043 2.80e-05

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 51.34  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6845 SNAALAPLGSIGELLV---EG-PI-LARGYLNDADKTAAAFvndpawlveghgkHPGrrgrLYKTGDLVYYNKDGNLVYI 6919
Cdd:cd05970    369 REGRSCEAGEEGEIVIrtsKGkPVgLFGGYYKDAEKTAEVW-------------HDG----YYHTGDAAWMDEDGYLWFV 431
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6920 GRKDGQVKVRGQRVELGEIENRLREcMPRATQMAVevispAGAAEQAKTMVV-AFLQLNDeardallgGNVPNDDnLSAQ 6998
Cdd:cd05970    432 GRTDDLIKSSGYRIGPFEVESALIQ-HPAVLECAV-----TGVPDPIRGQVVkATIVLAK--------GYEPSEE-LKKE 496
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 6999 VVFPAKvdeklsNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:cd05970    497 LQDHVK------KVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
3-277 2.90e-05

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 51.42  E-value: 2.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    3 VNWALLTPSVARLLEPS--------HIPSLRILVMGGEQVNSADWdRWPSSV------QTINGYGPTE----CCIVCTGY 64
Cdd:cd17634    327 VNILYTAPTAIRALMAAgddaiegtDRSSLRILGSVGEPINPEAY-EWYWKKigkekcPVVDTWWQTEtggfMITPLPGA 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   65 TSEQD--FTTGTIGTSIAsvswVVDpkDHGRLAPLGSVGELLVEGPI--LARGYLSDPEKTAAVfinnpawlleghggYA 140
Cdd:cd17634    406 IELKAgsATRPVFGVQPA----VVD--NEGHPQPGGTEGNLVITDPWpgQTRTLFGDHERFEQT--------------YF 465
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  141 GRQGRLYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEhHVRECLPEAKQLAVeVVLPlgqknHAtlaafiqld 220
Cdd:cd17634    466 STFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIE-SVLVAHPKVAEAAV-VGIP-----HA--------- 529
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560  221 kgthnallkekVGGDDSIARVVFLAGVE------EELAKRLPKHMVPTVFFALLHF----PTTTSGK 277
Cdd:cd17634    530 -----------IKGQAPYAYVVLNHGVEpspelyAELRNWVRKEIGPLATPDVVHWvdslPKTRSGK 585
PRK07867 PRK07867
acyl-CoA synthetase; Validated
23-199 2.96e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 51.22  E-value: 2.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRIlVMGGEQVnSADWDRWPS--SVQTINGYGPTECCIvctGYTSEQDFTTGTIGTSIASVSwVVDP-----------K 89
Cdd:PRK07867   268 PLRI-VYGNEGA-PGDIARFARrfGCVVVDGFGSTEGGV---AITRTPDTPPGALGPLPPGVA-IVDPdtgtecppaedA 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   90 DHGRLAPLGSVGELL-VEGPILARGYLSDPEKTAAVFinnpawlleghggyagRQGRlYKTGDLVRYDADGNLVCLGRKD 168
Cdd:PRK07867   342 DGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERM----------------RGGV-YWSGDLAYRDADGYAYFAGRLG 404
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1820002560  169 SQVKLRGQRVELGEVEHHVREcLPEAKQLAV 199
Cdd:PRK07867   405 DWMRVDGENLGTAPIERILLR-YPDATEVAV 434
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
51-167 3.15e-05

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 50.93  E-value: 3.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   51 GYGPTECC---IVCTGYTSEqdftTGTIGTSIASVSWVVDPKdhgrlaplgsvGELLVEGPILARGYLSDPEKTAAVFiN 127
Cdd:cd05932    305 AYGMTENFaysHLNYPGRDK----IGTVGNAGPGVEVRISED-----------GEILVRSPALMMGYYKDPEATAEAF-T 368
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1820002560  128 NPAWLleghggyagrqgrlyKTGDLVRYDADGNLVCLGRK 167
Cdd:cd05932    369 ADGFL---------------RTGDKGELDADGNLTITGRV 393
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
6842-7043 3.17e-05

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 51.03  E-value: 3.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGR 6921
Cdd:PRK08751   395 IKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDAD-GWL---------------HTGDIARMDEQGFVYIVDR 458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 KDGQVKVRGQRVELGEIENRLrECMPRATQMAVEVISPAGAAEQAKTMVVAflqlndeardallggnvpNDDNLSAQvvf 7001
Cdd:PRK08751   459 KKDMILVSGFNVYPNEIEDVI-AMMPGVLEVAAVGVPDEKSGEIVKVVIVK------------------KDPALTAE--- 516
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 7002 paKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:PRK08751   517 --DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
6309-6569 3.27e-05

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 50.92  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6309 DVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLL-QVVVE------EKIQWTESKRLEEYLREDKAVSMGL--GDPLaRY 6379
Cdd:cd19532     35 PLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPmQGVLAssplrlEHVQISDEAEVEEEFERLKNHVYDLesGETM-RI 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6380 AIIKeaWGGKR-WFVWTIHHALYDGWSLPRVLQAVKQAYNGAVLETQPSfnafiQYLS-----QQDLEATA-----AYWQ 6448
Cdd:cd19532    114 VLLS--LSPTEhYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPL-----QYLDfaarqRQDYESGAldedlAYWK 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6449 TALADCEATLfPPLP-SSVK---------QLVADTTVEHQCplpsrstsdtttSTLIR---------------AAWAIVA 6503
Cdd:cd19532    187 SEFSTLPEPL-PLLPfAKVKsrppltrydTHTAERRLDAAL------------AARIKeasrklrvtpfhfylAALQVLL 253
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6504 SRYTSSDDVVFGTTITGRNAPvtSIDAIVGPTIATVPLRVRLQKDQTVSSFLgylqqQATEMIAYE 6569
Cdd:cd19532    254 ARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQTFADVL-----KETRDKAYA 312
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
3609-3890 3.31e-05

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 50.38  E-value: 3.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3609 IIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQ----FASYTFDACIAeiitTLLCGG-CICVPSDSDRRn 3683
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNsgplFHIGTLMFTLA----TFHAGGtNVFVRRVDAEE- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3684 sLAKAISTMDVNWAFLTP----SVARLLDPGL--IPSLKilaiggEQSSSADWN--------RWpgsVQKIHVYGPTECc 3749
Cdd:cd17636     80 -VLELIEAERCTHAFLLPptidQIVELNADGLydLSSLR------SSPAAPEWNdmatvdtsPW---GRKPGGYGQTEV- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3750 ifcTGYTTKQGFEPSTIGTSVASVSWV----VDPENhnRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdpAWlle 3825
Cdd:cd17636    149 ---MGLATFAALGGGAIGGAGRPSPLVqvriLDEDG--REVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG--GW--- 218
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 3826 gypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAV 3890
Cdd:cd17636    219 ------------HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQ-HPAVADAAV 270
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
7755-8036 3.31e-05

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 50.38  E-value: 3.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7755 IIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQ----FASYTFDACIAeiitTLLCGG-CICVPSDSDRRn 7829
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNsgplFHIGTLMFTLA----TFHAGGtNVFVRRVDAEE- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7830 sLAKAISTMDVNWAFLTP----SVARLLDPGL--IPSLKilaiggEQSSSADWN--------RWpgsVQKIHVYGPTECc 7895
Cdd:cd17636     80 -VLELIEAERCTHAFLLPptidQIVELNADGLydLSSLR------SSPAAPEWNdmatvdtsPW---GRKPGGYGQTEV- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7896 ifcTGYTTKQGFEPSTIGTSVASVSWV----VDPENhnRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDdpAWlle 7971
Cdd:cd17636    149 ---MGLATFAALGGGAIGGAGRPSPLVqvriLDEDG--REVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG--GW--- 218
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820002560 7972 gypghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAV 8036
Cdd:cd17636    219 ------------HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQ-HPAVADAAV 270
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
6781-7043 3.38e-05

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 50.77  E-value: 3.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6781 PLDPDHpasrHEDILRQTGAQVILASAQNTTLFQ-SSNQTVVTVNRSSYILFPDENREAypfVRPSNAALAPLGSIGELL 6859
Cdd:cd05926    276 SLPPAV----LEALEATFGAPVLEAYGMTEAAHQmTSNPLPPGPRKPGSVGKPVGVEVR---ILDEDGEILPPGVVGEIC 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6860 VEGPILARGYLNDADKTAAAFVNDPaWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIE 6939
Cdd:cd05926    349 LRGPNVTRGYLNNPEANAEAAFKDG-WF---------------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVD 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6940 NRLRECmPratqmavevispagAAEQAktmvVAFlqlndEARDALLGGNVpnddnlSAQVVF--PAKVDEK-----LSNL 7012
Cdd:cd05926    413 GVLLSH-P--------------AVLEA----VAF-----GVPDEKYGEEV------AAAVVLreGASVTEEelrafCRKH 462
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1820002560 7013 LPSYMMP-EVYFaVPQLPMMISGKTDRKRLRE 7043
Cdd:cd05926    463 LAAFKVPkKVYF-VDELPKTATGKIQRRKVAE 493
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
5748-6036 3.47e-05

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 51.27  E-value: 3.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5748 LGQLSTLvnPVGLPAIPENAVyIMFTSGSTGIPKGVVLEHRAVVT----------------------------------- 5792
Cdd:PLN02387   236 LGKENPV--DPDLPSPNDIAV-IMYTSGSTGLPKGVMMTHGNIVAtvagvmtvvpklgkndvylaylplahilelaaesv 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5793 -----SCWGRGRAFGITNLSRVLQFASYTfDACMdeIITTLMyggcICVPSDSDRRNDLVK---------AISTMDVSCA 5858
Cdd:PLN02387   313 maavgAAIGYGSPLTLTDTSNKIKKGTKG-DASA--LKPTLM----TAVPAILDRVRDGVRkkvdakgglAKKLFDIAYK 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5859 LLTPSV------ARLLEPSSVPTL---QMLVLQGEQVSFADWNRWPASVQT---IN---------GYGPTEcsICCN-TY 5916
Cdd:PLN02387   386 RRLAAIegswfgAWGLEKLLWDALvfkKIRAVLGGRIRFMLSGGAPLSGDTqrfINiclgapigqGYGLTE--TCAGaTF 463
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5917 SGKQGFKSGIIGTSVAS-----VSWvvdPEN----HDRLAPLgsiGELLVEGPILARGYLNDIQKTAAVFIDDPawlleg 5987
Cdd:PLN02387   464 SEWDDTSVGRVGPPLPCcyvklVSW---EEGgyliSDKPMPR---GEIVIGGPSVTLGYFKNQEKTDEVYKVDE------ 531
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5988 ypghpgRQGRLYKTGDLVRYDANGNLVCLGRKDSQVKLR-GQRVELGEVE 6036
Cdd:PLN02387   532 ------RGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVE 575
PLN03102 PLN03102
acyl-activating enzyme; Provisional
2079-2453 3.47e-05

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 51.17  E-value: 3.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2079 FTSGSTGTPKGVVLEHRAVVTSCLGH--GQAFGVTNL----LRALQFTAYTFDVCIAEIITTLVhggCICVPSDSERRDN 2152
Cdd:PLN03102   193 YTSGTTADPKGVVISHRGAYLSTLSAiiGWEMGTCPVylwtLPMFHCNGWTFTWGTAARGGTSV---CMRHVTAPEIYKN 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2153 LA-KAITDMqvnwgyltssvarlldpCLVPSLKVLVLGGEQVNST---------DWGKWPSSV----------QTINGYG 2212
Cdd:PLN03102   270 IEmHNVTHM-----------------CCVPTVFNILLKGNSLDLSprsgpvhvlTGGSPPPAAlvkkvqrlgfQVMHAYG 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2213 PTECC---VFCT---GYTGIQGFQSGNI----GTSIASVSwVVDPENHGRLAPL----GSIGELLVEGPILARGYLNDVD 2278
Cdd:PLN03102   333 LTEATgpvLFCEwqdEWNRLPENQQMELkarqGVSILGLA-DVDVKNKETQESVprdgKTMGEIVIKGSSIMKGYLKNPK 411
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2279 KTQAAFidDPAWLlegypghegrqgrlyKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAV 2358
Cdd:PLN03102   412 ATSEAF--KHGWL---------------NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYK-YPKVLETAV 473
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2359 EVVPpsgerdHAMLAafirlddETRNSPLIIKYAEDNSTAQIVFLTGIEEEL----SERLPQHMVPTVFFALVHFPTTTS 2434
Cdd:PLN03102   474 VAMP------HPTWG-------ETPCAFVVLEKGETTKEDRVDKLVTRERDLieycRENLPHFMCPRKVVFLQELPKNGN 540
                          410
                   ....*....|....*....
gi 1820002560 2435 GKTDRKRLREIGASFTAQQ 2453
Cdd:PLN03102   541 GKILKPKLRDIAKGLVVED 559
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
3588-3883 3.50e-05

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 50.82  E-value: 3.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3588 SQLPAVVDStntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGItNLSRVLQ--FASYT----FDACIA 3661
Cdd:cd05933    138 EQLDAIISS----QKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDL-RPATVGQesVVSYLplshIAAQIL 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3662 EIITTLLCGGCICVPSDSDRRNSLAKAI------STMDVNWAF------------LTPSVARLLDP-----GLIPSLKIL 3718
Cdd:cd05933    213 DIWLPIKVGGQVYFAQPDALKGTLVKTLrevrptAFMGVPRVWekiqekmkavgaKSGTLKRKIASwakgvGLETNLKLM 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3719 aiGGEqSSSADWNRWPGS--VQKIH-----------------------------------VYGPTECcifcTGYTT---K 3758
Cdd:cd05933    293 --GGE-SPSPLFYRLAKKlvFKKVRkalgldrcqkfftgaapisretlefflslnipimeLYGMSET----SGPHTisnP 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3759 QGFEPSTIGTSVASVSWVVDPENHNrlaplGSmGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypgHpgrqgrly 3838
Cdd:cd05933    366 QAYRLLSCGKALPGCKTKIHNPDAD-----GI-GEICFWGRHVFMGYLNMEDKTEEA-IDEDGWL------H-------- 424
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 3839 kTGDLVQYNADGNLVYLGR-KDSQVKVRGQRVELGEVEHHVRECLP 3883
Cdd:cd05933    425 -SGDLGKLDEDGFLYITGRiKELIITAGGENVPPVPIEDAVKKELP 469
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
7734-8029 3.50e-05

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 50.82  E-value: 3.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7734 SQLPAVVDStntsVRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGItNLSRVLQ--FASYT----FDACIA 7807
Cdd:cd05933    138 EQLDAIISS----QKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDL-RPATVGQesVVSYLplshIAAQIL 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7808 EIITTLLCGGCICVPSDSDRRNSLAKAI------STMDVNWAF------------LTPSVARLLDP-----GLIPSLKIL 7864
Cdd:cd05933    213 DIWLPIKVGGQVYFAQPDALKGTLVKTLrevrptAFMGVPRVWekiqekmkavgaKSGTLKRKIASwakgvGLETNLKLM 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7865 aiGGEqSSSADWNRWPGS--VQKIH-----------------------------------VYGPTECcifcTGYTT---K 7904
Cdd:cd05933    293 --GGE-SPSPLFYRLAKKlvFKKVRkalgldrcqkfftgaapisretlefflslnipimeLYGMSET----SGPHTisnP 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7905 QGFEPSTIGTSVASVSWVVDPENHNrlaplGSmGELLMEGPILARGYLNDVDKTEAAfIDDPAWLlegypgHpgrqgrly 7984
Cdd:cd05933    366 QAYRLLSCGKALPGCKTKIHNPDAD-----GI-GEICFWGRHVFMGYLNMEDKTEEA-IDEDGWL------H-------- 424
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560 7985 kTGDLVQYNADGNLVYLGR-KDSQVKVRGQRVELGEVEHHVRECLP 8029
Cdd:cd05933    425 -SGDLGKLDEDGFLYITGRiKELIITAGGENVPPVPIEDAVKKELP 469
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
7632-7779 3.71e-05

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 50.81  E-value: 3.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7632 ELTYGELDVLSSNLAGHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVA 7710
Cdd:cd05905     14 TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7711 S-AQYSARWTSSSCHVVTVSKALSSQLPAVVDSTNTS---------------VRPENAAYIIFTSGSTGVPKGVVLEHRA 7774
Cdd:cd05905     94 VeACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPkskrsklkkwgphppTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173

                   ....*
gi 1820002560 7775 VATSC 7779
Cdd:cd05905    174 LLAHC 178
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
5770-6036 4.29e-05

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 49.96  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 IMFTSGSTGIPKGVVLEHRAVVTS------CWGRGRA---------FGITNLSRVLqfasytfdacmdeiiTTLMYGGCI 5834
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNLIAAnlqlihAMGLTEAdvylnmlplFHIAGLNLAL---------------ATFHAGGAN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5835 CVPS--DSDRRNDLVKA--ISTMdvscALLTPSVARLLE-----PSSVPTLqmlvlqgEQVSFADWnrwPASVQ---TIN 5902
Cdd:cd17637     70 VVMEkfDPAEALELIEEekVTLM----GSFPPILSNLLDaaeksGVDLSSL-------RHVLGLDA---PETIQrfeETT 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5903 G------YGPTECS--ICCNTYSGKQGfKSGIIG--TSVAsvswVVDPEnhDRLAPLGSIGELLVEGPILARGYLNDIQK 5972
Cdd:cd17637    136 GatfwslYGQTETSglVTLSPYRERPG-SAGRPGplVRVR----IVDDN--DRPVPAGETGEIVVRGPLVFQGYWNLPEL 208
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 5973 TAAVFIDDpaWllegypghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQ--VKLRGQRVELGEVE 6036
Cdd:cd17637    209 TAYTFRNG--W---------------HHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVE 257
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
6842-6939 4.98e-05

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 50.36  E-value: 4.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALaPLGSIGELLVEGPILARGYLNDADKTAAAFVNDpAWlveghgkhpgrrgrlYKTGDLVYYnKDGNLVYIGR 6921
Cdd:cd05906    368 VDDEGQLL-PEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED-GW---------------FRTGDLGFL-DNGNLTITGR 429
                           90
                   ....*....|....*...
gi 1820002560 6922 KDGQVKVRGQRVELGEIE 6939
Cdd:cd05906    430 TKDTIIVNGVNYYSHEIE 447
PRK07529 PRK07529
AMP-binding domain protein; Validated
46-168 5.00e-05

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 50.34  E-value: 5.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   46 VQTINGYGPTEC-CIVCTGYtSEQDFTTGTIG-----TSIASVswVVDPKDHG-RLAPLGSVGELLVEGPILARGYLsDP 118
Cdd:PRK07529   359 VRIVEGYGLTEAtCVSSVNP-PDGERRIGSVGlrlpyQRVRVV--ILDDAGRYlRDCAVDEVGVLCIAGPNVFSGYL-EA 434
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  119 EKtaavfiNNPAWLleghggyagrQGRLYKTGDLVRYDADGNLVCLGR-KD 168
Cdd:PRK07529   435 AH------NKGLWL----------EDGWLNTGDLGRIDADGYFWLTGRaKD 469
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
73-184 5.02e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 50.55  E-value: 5.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   73 GTIGTSIASVSW-VVDpkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinnpawllegHGGYagrqgrlYKTGD 151
Cdd:PRK07786   345 GSVGKVIPTVAArVVD--ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF----------AGGW-------FHSGD 405
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1820002560  152 LVRYDADGNLVCLGRKDSQVKLRGQRVELGEVE 184
Cdd:PRK07786   406 LVRQDEEGYVWVVDRKKDMIISGGENIYCAEVE 438
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
51-184 5.17e-05

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 50.50  E-value: 5.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   51 GYGPTECCIVCTgYTSEQDFTTGTIG-----TSIASVSWvvdpKDHGRL---APLGSvGELLVEGPILARGYLSDPEKTA 122
Cdd:PLN02387   451 GYGLTETCAGAT-FSEWDDTSVGRVGpplpcCYVKLVSW----EEGGYLisdKPMPR-GEIVIGGPSVTLGYFKNQEKTD 524
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560  123 AVFINNPawlleghggyagRQGRLYKTGDLVRYDADGNLVCLGRKDSQVKLR-GQRVELGEVE 184
Cdd:PLN02387   525 EVYKVDE------------RGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVE 575
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
6851-7050 5.30e-05

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 50.37  E-value: 5.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFVNDPawlveghgkhpgrrgrLYKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:PRK10946   376 PQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANG----------------FYCSGDLVSIDPDGYITVVGREKDQINRGG 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6931 QRVELGEIENRLREcMPRATQMAVEVISPAGAAEQAktmvVAFLQLNDEARDALLggnvpnDDNLSAQVVfpakvdekls 7010
Cdd:PRK10946   440 EKIAAEEIENLLLR-HPAVIHAALVSMEDELMGEKS----CAFLVVKEPLKAVQL------RRFLREQGI---------- 498
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1820002560 7011 nllPSYMMPEVYFAVPQLPMMISGKTDRKRLREIGASFTA 7050
Cdd:PRK10946   499 ---AEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1530-1727 5.45e-05

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 49.94  E-value: 5.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1530 QSVLeLRI--DVDEDVFRAAWEHIVRSTAVLRTRIVQHSelGLLQVVIEENIQWTEP--------KSLEEYLSEDKAVSV 1599
Cdd:cd19534     24 QSVL-LRVpqGLDPDALRQALRALVEHHDALRMRFRRED--GGWQQRIRGDVEELFRlevvdlssLAQAAAIEALAAEAQ 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1600 GLGD----PLARYAFVKEACGGKRwFVWTIHHAVYDGWSLPLIL----HAVKQVYSGGVLQWQP--SFNAFIQ----YLG 1665
Cdd:cd19534    101 SSLDleegPLLAAALFDGTDGGDR-LLLVIHHLVVDGVSWRILLedleAAYEQALAGEPIPLPSktSFQTWAEllaeYAQ 179
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 1666 QQDLEATVAYWQTALADceavLFPTLPPTVTQPVADATVEyqcpplSKATSDTTTSTLIRAA 1727
Cdd:cd19534    180 SPALLEELAYWRELPAA----DYWGLPKDPEQTYGDARTV------SFTLDEEETEALLQEA 231
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
2077-2362 5.56e-05

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 49.61  E-value: 5.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2077 VMFTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTNLLRALQ----FTAYTFDVCIAeiitTLVHGG-CICVPSDSERRd 2151
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNsgplFHIGTLMFTLA----TFHAGGtNVFVRRVDAEE- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2152 nLAKAITDMQVNWGYLTSSV---------ARLLDpclVPSLKVLVLGGE-----QVNSTDWGKWPSsvqtinGYGPTECc 2217
Cdd:cd17636     80 -VLELIEAERCTHAFLLPPTidqivelnaDGLYD---LSSLRSSPAAPEwndmaTVDTSPWGRKPG------GYGQTEV- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2218 vfcTGYTGIQGFQSGNIGTSIASVSWV----VDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDdpAWlle 2293
Cdd:cd17636    149 ---MGLATFAALGGGAIGGAGRPSPLVqvriLDED--GREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG--GW--- 218
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 2294 gypghegrqgrlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVEHHMRKcLPEANQLAVEVVP 2362
Cdd:cd17636    219 ------------HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQ-HPAVADAAVIGVP 274
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
6842-7043 5.58e-05

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 50.07  E-value: 5.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFvnDPAWlveghgkhpgrrgrlYKTGDLVYYNKDGNLVYIGR 6921
Cdd:cd05903    275 VVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA--PEGW---------------FRTGDLARLDEDGYLRITGR 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 -KDgqVKVR-GQRVELGEIENRLREcMPRATQMAVEVISPAGAAEQAktmvVAFLQLNDEAR---DALLggnvpndDNLS 6996
Cdd:cd05903    338 sKD--IIIRgGENIPVLEVEDLLLG-HPGVIEAAVVALPDERLGERA----CAVVVTKSGALltfDELV-------AYLD 403
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 6997 AQVVfpAKvdeklsnllpsYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:cd05903    404 RQGV--AK-----------QYWPERLVHVDDLPRTPSGKVQKFRLRE 437
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
6851-6944 5.94e-05

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 49.58  E-value: 5.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFVNDpaWlvegHgkHpgrrgrlykTGDLVYYNKDGNLVYIGRKDGQ--VKV 6928
Cdd:cd17637    184 PAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG--W----H--H---------TGDLGRFDEDGYLWYAGRKPEKelIKP 246
                           90
                   ....*....|....*.
gi 1820002560 6929 RGQRVELGEIENRLRE 6944
Cdd:cd17637    247 GGENVYPAEVEKVILE 262
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
5770-6044 6.18e-05

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 50.05  E-value: 6.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5770 IMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGItNLSRVLQ--FASYT----FDACMDEIITTLMYGGCICVPSDSDRR 5843
Cdd:cd05933    155 LIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDL-RPATVGQesVVSYLplshIAAQILDIWLPIKVGGQVYFAQPDALK 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5844 NDLVKAISTMDVSCALLTPSV-ARLLE------PSSVPTLQMLVLQGEQVSFADWNRWPAS------------------- 5897
Cdd:cd05933    234 GTLVKTLREVRPTAFMGVPRVwEKIQEkmkavgAKSGTLKRKIASWAKGVGLETNLKLMGGespsplfyrlakklvfkkv 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5898 ---------VQTING----------------------YGPTECSiCCNTYSGKQGFKSGIIGTSVASVSWVVDPENHDrl 5946
Cdd:cd05933    314 rkalgldrcQKFFTGaapisretlefflslnipimelYGMSETS-GPHTISNPQAYRLLSCGKALPGCKTKIHNPDAD-- 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5947 aplgSIGELLVEGPILARGYLNDIQKTAAVfIDDPAWLlegypgHpgrqgrlykTGDLVRYDANGNLVCLGR-KDSQVKL 6025
Cdd:cd05933    391 ----GIGEICFWGRHVFMGYLNMEDKTEEA-IDEDGWL------H---------SGDLGKLDEDGFLYITGRiKELIITA 450
                          330
                   ....*....|....*....
gi 1820002560 6026 RGQRVELGEVEHHVRECLP 6044
Cdd:cd05933    451 GGENVPPVPIEDAVKKELP 469
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
85-184 6.32e-05

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 49.78  E-value: 6.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   85 VVDPKDhGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNpawlleghggyAGRqgRLYKTGDLVRYDADGNLVCL 164
Cdd:cd05935    264 VIDIET-GRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEI-----------KGR--RFFRTGDLGYMDEEGYFFFV 329
                           90       100
                   ....*....|....*....|
gi 1820002560  165 GRKDSQVKLRGQRVELGEVE 184
Cdd:cd05935    330 DRVKRMINVSGFKVWPAEVE 349
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
7632-8032 6.46e-05

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 50.12  E-value: 6.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7632 ELTYGELDVLSSNLAGHLVQLgVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL-DPDHPAsrHEEIFEqtgaqVVVA 7710
Cdd:PRK12476    68 ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPG--HAERLD-----TALR 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7711 SAQYSARWTSSSC-----------------HVVTVSkalssqlpAVVDSTNTSVRP-----ENAAYIIFTSGSTGVPKGV 7768
Cdd:PRK12476   140 DAEPTVVLTTTAAaeavegflrnlprlrrpRVIAID--------AIPDSAGESFVPveldtDDVSHLQYTSGSTRPPVGV 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7769 VLEHRAVATSCLghGRAFGITNLSRVLQFASYT---FDACIAEIITTLLCGGCICV--PSDSDRR-----NSLAKAISTM 7838
Cdd:PRK12476   212 EITHRAVGTNLV--QMILSIDLLDRNTHGVSWLplyHDMGLSMIGFPAVYGGHSTLmsPTAFVRRpqrwiKALSEGSRTG 289
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7839 DV-----NWAFLTPSVARLLDPG--LIPSLKILAIGGEQSSSADWNRW---------PGSVQKIHvYGPTECCIFCTgyT 7902
Cdd:PRK12476   290 RVvtaapNFAYEWAAQRGLPAEGddIDLSNVVLIIGSEPVSIDAVTTFnkafapyglPRTAFKPS-YGIAEATLFVA--T 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7903 TKQGFEPSTI-------------------GTSVASVS--------W--VVDPENHNRLaPLGSMGELLMEGPILARGYLN 7953
Cdd:PRK12476   367 IAPDAEPSVVyldreqlgagravrvaadaPNAVAHVScgqvarsqWavIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWG 445
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7954 DVDKTEAAFIDD-PAWLLEGypGHPGR---QGRLYKTGDLVQYnADGNLVYLGRKDSQVKVRGQRVELGEVEHHVRECLP 8029
Cdd:PRK12476   446 RPEETERTFGAKlQSRLAEG--SHADGaadDGTWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEASP 522

                   ...
gi 1820002560 8030 EAR 8032
Cdd:PRK12476   523 MVR 525
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
6851-7044 6.59e-05

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 50.21  E-value: 6.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAfVNDPAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:PRK12492   408 PLGERGELCIKGPQVMKGYWQQPEATAEA-LDAEGWF---------------KTGDIAVIDPDGFVRIVDRKKDLIIVSG 471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6931 QRVELGEIENRLReCMPRATQMAVEVISPAGAAEQAKTMVvaflqlndeardallggnVPNDDNLSAQVVfPAKVDEKLS 7010
Cdd:PRK12492   472 FNVYPNEIEDVVM-AHPKVANCAAIGVPDERSGEAVKLFV------------------VARDPGLSVEEL-KAYCKENFT 531
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1820002560 7011 nllpSYMMPEVYFAVPQLPMMISGKTDRKRLREI 7044
Cdd:PRK12492   532 ----GYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1955-2444 6.68e-05

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 49.87  E-value: 6.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVP----LDPDHPASRHEdifRQTGAQVV 2030
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRVD---RGGAVYAA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2031 VTSAQHSArwigtnhqvvtvsagsleqfstlvNPVDLpakpenaayvMFTSGSTGTPKGVVLEHRavvTSCLGHGQafgv 2110
Cdd:cd05974     78 VDENTHAD------------------------DPMLL----------YFTSGTTSKPKLVEHTHR---SYPVGHLS---- 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2111 tnllralqfTAYTFDVCIAEIITTLVHGG-------CICVPSDSE---------RRDnlAKAITDMQVNWGYLT----SS 2170
Cdd:cd05974    117 ---------TMYWIGLKPGDVHWNISSPGwakhawsCFFAPWNAGatvflfnyaRFD--AKRVLAALVRYGVTTlcapPT 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2171 VARLLDPCLVPSLKV----LVLGGEQVN-------STDWGKwpssvqTI-NGYGPTECCVFCTGYTGiQGFQSGNIGTSI 2238
Cdd:cd05974    186 VWRMLIQQDLASFDVklreVVGAGEPLNpevieqvRRAWGL------TIrDGYGQTETTALVGNSPG-QPVKAGSMGRPL 258
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2239 ASVSWVV-DPEnhGRLAPLGSIG-ELLVEGPI-LARGYLNDVDKTQAAFiddpawllegypghegrQGRLYKTGDLVRYS 2315
Cdd:cd05974    259 PGYRVALlDPD--GAPATEGEVAlDLGDTRPVgLMKGYAGDPDKTAHAM-----------------RGGYYRTGDIAMRD 319
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2316 SDGNLVCLGRKDSQVKVRGQRVELGEVEhhmrKCLPEANQLA-VEVVP-PSGERdHAMLAAFIRLDDETRNSPliikyae 2393
Cdd:cd05974    320 EDGYLTYVGRADDVFKSSDYRISPFELE----SVLIEHPAVAeAAVVPsPDPVR-LSVPKAFIVLRAGYEPSP------- 387
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 2394 dnSTAQIVFltgieEELSERL-PQHMVPTVFFAlvHFPTTTSGKTDRKRLRE 2444
Cdd:cd05974    388 --ETALEIF-----RFSRERLaPYKRIRRLEFA--ELPKTISGKIRRVELRR 430
PLN02736 PLN02736
long-chain acyl-CoA synthetase
7602-7781 6.96e-05

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 50.10  E-value: 6.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7602 PPAIE-RCVHDLFAEQA-----------RARP-GAPAICAWdgeLTYGELDVLSSNLAGHLVQLGVNPEDVVPLCF-EKS 7667
Cdd:PLN02736    38 PDHPEiGTLHDNFVYAVetfrdykylgtRIRVdGTVGEYKW---MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFiNRP 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7668 MWTVV--AMLAVLKAGgafVPL----DPDhpASR----HEE---IF--------------EQTGAQVVV----ASAQYSA 7716
Cdd:PLN02736   115 EWLIVdhACSAYSYVS---VPLydtlGPD--AVKfivnHAEvaaIFcvpqtlntllsclsEIPSVRLIVvvggADEPLPS 189
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 7717 RWTSSSCHVVTVSKALS---SQLPAVVDStntsvRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLG 7781
Cdd:PLN02736   190 LPSGTGVEIVTYSKLLAqgrSSPQPFRPP-----KPEDVATICYTSGTTGTPKGVVLTHGNLIANVAG 252
PLN02479 PLN02479
acetate-CoA ligase
3611-3975 6.98e-05

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 49.84  E-value: 6.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3611 FTSGSTGVPKGVVLEHRAVATSCLGHGRAFGItNLSRVLQFASYTFDA---CIAEIITTLlCGGCICVpsdsdrRNSLAK 3687
Cdd:PLN02479   202 YTSGTTASPKGVVLHHRGAYLMALSNALIWGM-NEGAVYLWTLPMFHCngwCFTWTLAAL-CGTNICL------RQVTAK 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3688 AISTMDVNW----------------------AFLT-PSVARLLDPGLIPSLKILAIGGEQSssadwnrwpgsVQKIHVYG 3744
Cdd:PLN02479   274 AIYSAIANYgvthfcaapvvlntivnapkseTILPlPRVVHVMTAGAAPPPSVLFAMSEKG-----------FRVTHTYG 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3745 PTECcifctgyttkqgFEPSTIgtsvasVSW------------------------------VVDPENHNRLAPLG-SMGE 3793
Cdd:PLN02479   343 LSET------------YGPSTV------CAWkpewdslppeeqarlnarqgvryiglegldVVDTKTMKPVPADGkTMGE 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3794 LLMEGPILARGYLNDVDKTEAAFiddpawllegypghpgrQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGE 3873
Cdd:PLN02479   405 IVMRGNMVMKGYLKNPKANEEAF-----------------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLE 467
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3874 VEHHVreCLPEArQLAVEVILPSGQKDHAMLAAFVQLEEGTQNAllDKEAGGEDSMAqvvFLASveeelakRLPEHMVP- 3952
Cdd:PLN02479   468 VENVV--YTHPA-VLEASVVARPDERWGESPCAFVTLKPGVDKS--DEAALAEDIMK---FCRE-------RLPAYWVPk 532
                          410       420
                   ....*....|....*....|...
gi 1820002560 3953 TVFFSLLhfPTTTSGKTDRKRLR 3975
Cdd:PLN02479   533 SVVFGPL--PKTATGKIQKHVLR 553
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
5645-5794 7.00e-05

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 49.98  E-value: 7.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5645 DGELTYGELDALSSKLAGHL-TQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAG--GAFVPldpdhPASR-----HedTFR 5716
Cdd:cd05938      3 GETYTYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLN-----TNIRsksllH--CFR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5717 HTGAQVVVTSA--------------QHSARWIGTNHQVVTVSAGSLGQL----STLVNPVGLPA---IPENAVYImFTSG 5775
Cdd:cd05938     76 CCGAKVLVVAPelqeaveevlpalrADGVSVWYLSHTSNTEGVISLLDKvdaaSDEPVPASLRAhvtIKSPALYI-YTSG 154
                          170
                   ....*....|....*....
gi 1820002560 5776 STGIPKGVVLEHRAVVTSC 5794
Cdd:cd05938    155 TTGLPKAARISHLRVLQCS 173
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
10-285 7.03e-05

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 49.87  E-value: 7.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   10 PSVARLLEPSHIPS----LRILVMGGEQVNSADWDR----WPSSVQtiNGYGPTECCiVCTGYTSEQDFTTGTIGTsias 81
Cdd:cd05974    184 PTVWRMLIQQDLASfdvkLREVVGAGEPLNPEVIEQvrraWGLTIR--DGYGQTETT-ALVGNSPGQPVKAGSMGR---- 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   82 vswvvdPKDHGRLAPLGSVGELLVEGPI-----------LARGYLSDPEKTAAVFinnpawlleghggyagrQGRLYKTG 150
Cdd:cd05974    257 ------PLPGYRVALLDPDGAPATEGEValdlgdtrpvgLMKGYAGDPDKTAHAM-----------------RGGYYRTG 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  151 DLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEhhvrECLPEAKQLAVEVVLPLGQKNH-ATLAAFIQLDKGTHNAllk 229
Cdd:cd05974    314 DIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE----SVLIEHPAVAEAAVVPSPDPVRlSVPKAFIVLRAGYEPS--- 386
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560  230 ekvggdDSIARVVFlAGVEEELA--KRLPKhmvptvfFALLHFPTTTSGKTDRKRLRE 285
Cdd:cd05974    387 ------PETALEIF-RFSRERLApyKRIRR-------LEFAELPKTISGKIRRVELRR 430
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
849-1372 7.32e-05

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 49.87  E-value: 7.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  849 AVDRcihdlfaeQARARPDASAVcAWDGE-------LTYGELDELSSKLAAHLVQLGVKREDVVPLCFEKSMWTVVAMLA 921
Cdd:cd05966     58 CLDR--------HLKERGDKVAI-IWEGDepdqsrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLA 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  922 -------------------------------VLKA-----GGAFVPLDP-------GHPASRHEEIFKQIGAQVVLTSsq 958
Cdd:cd05966    129 carigavhsvvfagfsaesladrindaqcklVITAdggyrGGKVIPLKEivdealeKCPSVEKVLVVKRTGGEVPMTE-- 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  959 hamlfassER----HQVtVSKVSTSQLPTvvnfaksPVDPGNTAYIIFTSGTTGIPKGVVlqHravTTSclghgeafGYT 1034
Cdd:cd05966    207 --------GRdlwwHDL-MAKQSPECEPE-------WMDSEDPLFILYTSGSTGKPKGVV--H---TTG--------GYL 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1035 DHARVLQfaSYTFDA-------CIAEI--ITT---LLYG----GCICVPSESdrrnnlakaistmdvncALLTPSVARLL 1098
Cdd:cd05966    258 LYAATTF--KYVFDYhpddiywCTADIgwITGhsyIVYGplanGATTVMFEG-----------------TPTYPDPGRYW 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1099 E-------------PSAVPSLKRlvlQGEQvsfadwnrWP-----------GSV-QTING-----Y----GPTECSVCcN 1144
Cdd:cd05966    319 DivekhkvtifytaPTAIRALMK---FGDE--------WVkkhdlsslrvlGSVgEPINPeawmwYyeviGKERCPIV-D 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1145 TY-------------SGKQGFKSG-----IIGTSVAslswVVDA-GNHnrlAPLGSIGELLVEG--PILARGYLNDidkt 1203
Cdd:cd05966    387 TWwqtetggimitplPGATPLKPGsatrpFFGIEPA----ILDEeGNE---VEGEVEGYLVIKRpwPGMARTIYGD---- 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1204 EAAFIDDpawLLEGYEGHagrrgrlYKTGDLVRCDADGNLVCLGRKDSQVKVRGQRVELGEIE-----HH-VREClpear 1277
Cdd:cd05966    456 HERYEDT---YFSKFPGY-------YFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVEsalvaHPaVAEA----- 520
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1278 qlAVeVILPSGQKEHAlLAAFIQLDKGnhnalfeEKASGEdsmaqvvfltgVEEELAKRLPEHM----VPTILFTVKAMP 1353
Cdd:cd05966    521 --AV-VGRPHDIKGEA-IYAFVTLKDG-------EEPSDE-----------LRKELRKHVRKEIgpiaTPDKIQFVPGLP 578
                          650
                   ....*....|....*....
gi 1820002560 1354 ITTSGKIDRKRLQDIGASF 1372
Cdd:cd05966    579 KTRSGKIMRRILRKIAAGE 597
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3820-3976 7.40e-05

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 49.49  E-value: 7.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3820 PAWLLEGYPGHPGR-----QGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvrECLPEARQLAVEVIL 3894
Cdd:cd05974    287 PVGLMKGYAGDPDKtahamRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE----SVLIEHPAVAEAAVV 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3895 PSgqKDHAMLA---AFVQLEEGTQNAlldkeaggeDSMAQVVFLASvEEELAkrlPEHMVPTVFFSLLhfPTTTSGKTDR 3971
Cdd:cd05974    363 PS--PDPVRLSvpkAFIVLRAGYEPS---------PETALEIFRFS-RERLA---PYKRIRRLEFAEL--PKTISGKIRR 425

                   ....*
gi 1820002560 3972 KRLRE 3976
Cdd:cd05974    426 VELRR 430
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2586-2689 7.49e-05

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 49.57  E-value: 7.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2586 ELRNRVQPQLLVTALTALVQRHSMLRARFQRQTGGRWQQyISEHDSSSLIVNHI--HTRDTTEIVEALRQSRGS-LDIER 2662
Cdd:cd20483     31 HIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQ-VLDDPSFHLIVIDLseAADPEAALDQLVRNLRRQeLDIEE 109
                           90       100
                   ....*....|....*....|....*...
gi 1820002560 2663 GPVL-AAVLCDAGERQSLFVAIHHLVVD 2689
Cdd:cd20483    110 GEVIrGWLVKLPDEEFALVLASHHIAWD 137
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
1133-1249 8.29e-05

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 49.19  E-value: 8.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1133 GYGPTECS--VCCNTYSGKQGfKSGIIG--TSVAslswVVDAgnHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFi 1208
Cdd:cd17637    142 LYGQTETSglVTLSPYRERPG-SAGRPGplVRVR----IVDD--NDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF- 213
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 1209 ddpawllegyeghagrRGRLYKTGDLVRCDADGNLVCLGRK 1249
Cdd:cd17637    214 ----------------RNGWHHTGDLGRFDEDGYLWYAGRK 238
PRK09088 PRK09088
acyl-CoA synthetase; Validated
6851-7047 8.59e-05

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 49.42  E-value: 8.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFVNDpAWlveghgkhpgrrgrlYKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:PRK09088   328 PAGVPGELLLRGPNLSPGYWRRPQATARAFTGD-GW---------------FRTGDIARRDADGFFWVVDRKKDMFISGG 391
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6931 QRVELGEIENRL------RECM------PRATQMAVEVISPAGAAeqaktmvvaflqlndeardallggnvpnddnlsaq 6998
Cdd:PRK09088   392 ENVYPAEIEAVLadhpgiRECAvvgmadAQWGEVGYLAIVPADGA----------------------------------- 436
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 6999 VVFPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREIGAS 7047
Cdd:PRK09088   437 PLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
7632-8121 8.70e-05

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 49.68  E-value: 8.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7632 ELTYGELDVLSSNLAGHLVQLGVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRHEEIFEQTGAQVVVAS 7711
Cdd:PRK08008    37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7712 AQY------SARWTSSSCHVVTVSKALSSQLPAVVD-STNTSVRP-----------ENAAYIIFTSGSTGVPKGVVLEH- 7772
Cdd:PRK08008   117 AQFypmyrqIQQEDATPLRHICLTRVALPADDGVSSfTQLKAQQPatlcyapplstDDTAEILFTSGTTSRPKGVVITHy 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7773 -----------------------------------RAVATSCLG---------HGRAFgitnLSRVLQFASyTFDACIAE 7808
Cdd:PRK08008   197 nlrfagyysawqcalrdddvyltvmpafhidcqctAAMAAFSAGatfvllekySARAF----WGQVCKYRA-TITECIPM 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7809 IITTLLcggcICVPSDSDRRNSLAKAISTMDVN----WAFLTPSVARLLDP-GLIPSLkILAIGgeqSSSADWNRWPgSV 7883
Cdd:PRK08008   272 MIRTLM----VQPPSANDRQHCLREVMFYLNLSdqekDAFEERFGVRLLTSyGMTETI-VGIIG---DRPGDKRRWP-SI 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7884 QKIHVygpteccifctGYTTKqgfepstigtsvasvswVVDpeNHNRLAPLGSMGELLMEG---PILARGYLNDVDKTEA 7960
Cdd:PRK08008   343 GRPGF-----------CYEAE-----------------IRD--DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAK 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7961 AFIDDpAWLlegypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHhVRECLPEARQLAVeVIL 8040
Cdd:PRK08008   393 VLEAD-GWL---------------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELEN-IIATHPKIQDIVV-VGI 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8041 PSGQKNHAMLAvFVQLGKGTHIahleekaggedsmaqvvfltgTEEEL----AKRLPKHMVPTVFFALLHFPMTTSGKAD 8116
Cdd:PRK08008   455 KDSIRDEAIKA-FVVLNEGETL---------------------SEEEFfafcEQNMAKFKVPSYLEIRKDLPRNCSGKII 512

                   ....*
gi 1820002560 8117 RKRLR 8121
Cdd:PRK08008   513 KKNLK 517
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
7748-8116 8.72e-05

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 49.96  E-value: 8.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7748 RPENAAYIIFTSGSTGVPKGVVLEHR------AVATSCLGHGRAFGITNLSRVlqFASYTFdacIAEIITTLLCGgcICV 7821
Cdd:PRK06814   791 DPDDPAVILFTSGSEGTPKGVVLSHRnllanrAQVAARIDFSPEDKVFNALPV--FHSFGL---TGGLVLPLLSG--VKV 863
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7822 ---PSDSDRR-------NSLAKAISTMDVnwaFLTpSVARLLDPGLIPSLKILAIGGEQSSSADWNRWpgsVQK--IHV- 7888
Cdd:PRK06814   864 flyPSPLHYRiipeliyDTNATILFGTDT---FLN-GYARYAHPYDFRSLRYVFAGAEKVKEETRQTW---MEKfgIRIl 936
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7889 --YGPTECC--IFCtgyTTKQGFEPSTIGTSVASVSWVVDPenhnrLAPLGSMGELLMEGPILARGYLndvdKTEAAFID 7964
Cdd:PRK06814   937 egYGVTETApvIAL---NTPMHNKAGTVGRLLPGIEYRLEP-----VPGIDEGGRLFVRGPNVMLGYL----RAENPGVL 1004
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7965 DPawLLEGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVRECLPEARQLAVEVilPSGQ 8044
Cdd:PRK06814  1005 EP--PADGW----------YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSI--PDAR 1070
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8045 KnhamlavfvqlgkgthiahleekagGEdsmaQVVFLT----GTEEEL-----AKRLPKHMVPTVFFALLHFPMTTSGKA 8115
Cdd:PRK06814  1071 K-------------------------GE----RIILLTtasdATRAAFlahakAAGASELMVPAEIITIDEIPLLGTGKI 1121

                   .
gi 1820002560 8116 D 8116
Cdd:PRK06814  1122 D 1122
PRK07514 PRK07514
malonyl-CoA synthase; Validated
73-168 9.37e-05

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 49.49  E-value: 9.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   73 GTIGTSIASVSW-VVDPkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINNpawlleghgGYagrqgrlYKTGD 151
Cdd:PRK07514   321 GTVGFPLPGVSLrVTDP-ETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRAD---------GF-------FITGD 383
                           90
                   ....*....|....*...
gi 1820002560  152 LVRYDADGNLVCLGR-KD 168
Cdd:PRK07514   384 LGKIDERGYVHIVGRgKD 401
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
6851-6972 1.02e-04

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 49.38  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFvNDPAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:PRK05677   400 PLGEVGELCVKGPQVMKGYWQRPEATDEIL-DSDGWL---------------KTGDIALIQEDGYMRIVDRKKDMILVSG 463
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 6931 QRVELGEIENRLrECMPRATQMAVEVISPAGAAEQAKTMVVA 6972
Cdd:PRK05677   464 FNVYPNELEDVL-AALPGVLQCAAIGVPDEKSGEAIKVFVVV 504
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
6706-6778 1.04e-04

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 49.49  E-value: 1.04e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 6706 DLFTEQALARPNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGA 6778
Cdd:PRK08279    41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
2066-2444 1.07e-04

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 49.30  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2066 DLPAKPENAAYVMFTS-GSTGTPKGV------VLEHRAVVTSC-LGHGQAFGVTNLLRALQFTAYTFDVCiaeiITTLVH 2137
Cdd:cd05929    118 ETPIEDEAAGWKMLYSgGTTGRPKGIkrglpgGPPDNDTLMAAaLGFGPGADSVYLSPAPLYHAAPFRWS----MTALFM 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2138 GGCICVpsdSERRD--NLAKAITDMQVNWGYLTSSV-ARLLD-PCLVP------SLKVLVLGGE------QVNSTDWgkW 2201
Cdd:cd05929    194 GGTLVL---MEKFDpeEFLRLIERYRVTFAQFVPTMfVRLLKlPEAVRnaydlsSLKRVIHAAApcppwvKEQWIDW--G 268
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2202 PSSVqtINGYGPTEccvfCTGYTGIQGFQ----SGNIGTSIASVSWVVDpENhGRLAPLGSIGELLVEGPIlARGYLNDV 2277
Cdd:cd05929    269 GPII--WEYYGGTE----GQGLTIINGEEwlthPGSVGRAVLGKVHILD-ED-GNEVPPGEIGEVYFANGP-GFEYTNDP 339
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2278 DKTQAAfIDDPAWLLEGYPGHEGRQGRLYKTgdlvryssdgnlvclGRKDSQVKVRGQRVELGEVEHHMRKClPEANQLA 2357
Cdd:cd05929    340 EKTAAA-RNEGGWSTLGDVGYLDEDGYLYLT---------------DRRSDMIISGGVNIYPQEIENALIAH-PKVLDAA 402
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2358 VEVVPPS--GERDHAMLaafirlddETrnspliikyaEDNSTAQIVFLTGIEEELSERLPQHMVPTVFFALVHFPTTTSG 2435
Cdd:cd05929    403 VVGVPDEelGQRVHAVV--------QP----------APGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTG 464

                   ....*....
gi 1820002560 2436 KTDRKRLRE 2444
Cdd:cd05929    465 KLYRRLLRD 473
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
3159-3430 1.12e-04

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 49.02  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3159 DAHSRGILMHDLQEAYDANLN-------PQSTSFRDFASYIKQ-----QSQE----EAGRYWAEYLDGVEPCFFPSLGDS 3222
Cdd:cd19546    137 DDESLDVLVRDLAAAYGARREgraperaPLPLQFADYALWEREllageDDRDsligDQIAYWRDALAGAPDELELPTDRP 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3223 GGANTIPRTVEVPSIDSSAVHMfcKIWEVTPA------TIIQTAWALVLSRYTNSTNPCFGNLSSGRDLPIhNVNSIFGP 3296
Cdd:cd19546    217 RPVLPSRRAGAVPLRLDAEVHA--RLMEAAESagatmfTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEG-DLEGMVGP 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3297 LISILPCRIHLHKQLTVLEALKTVQENYASSLSFQTFPLASMHSFLGLGTSA----LFNTALSLqRIDDIGPCSASEI-- 3370
Cdd:cd19546    294 FARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELLALPPSAdrhpVFQVALDV-RDDDNDPWDAPELpg 372
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 3371 --TLKMKEGLDPTEYNITL------SAGYSKDAIDISMTFRAGCMDLVQAKRLASNFSQAIKAVTTEP 3430
Cdd:cd19546    373 lrTSPVPLGTEAMELDLSLalterrNDDGDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3606-3975 1.12e-04

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 48.63  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3606 AAYIiFTSGSTGVPKgvVLEHR---AVATS-CLGHGRAFGITNlsrVLQFASYTF--DACIAEIITTLLCGGCICVPSDS 3679
Cdd:cd05944      5 AAYF-HTGGTTGTPK--LAQHThsnEVYNAwMLALNSLFDPDD---VLLCGLPLFhvNGSVVTLLTPLASGAHVVLAGPA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3680 DRRN-----SLAKAISTMDVNWAFLTPSV--ARLLDPGL--IPSLKILAIGGEQSSSADWNRWPGS--VQKIHVYGPTEC 3748
Cdd:cd05944     79 GYRNpglfdNFWKLVERYRITSLSTVPTVyaALLQVPVNadISSLRFAMSGAAPLPVELRARFEDAtgLPVVEGYGLTEA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3749 CIFCTGYTTKQGFEPSTIGTSV--ASVSWVV-DPENHN--RLAPlGSMGELLMEGPILARGYLNDVDKtEAAFIDDpAWL 3823
Cdd:cd05944    159 TCLVAVNPPDGPKRPGSVGLRLpyARVRIKVlDGVGRLlrDCAP-DEVGEICVAGPGVFGGYLYTEGN-KNAFVAD-GWL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3824 legypghpgrqgrlyKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvrECLpeARQLAVEVILPSGQKD-HA 3902
Cdd:cd05944    236 ---------------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIE----EAL--LRHPAVAFAGAVGQPDaHA 294
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 3903 --MLAAFVQLEEGTqnalldkeaggedsmaqVVFLASVEEELAKRLPEH-MVPTVFFSLLHFPTTTSGKTDRKRLR 3975
Cdd:cd05944    295 geLPVAYVQLKPGA-----------------VVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALR 353
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
7203-7501 1.12e-04

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 49.19  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7203 YIMQSVLELRADVDEDVFCAAWEHVVQSTAALRTRIVQHSELGlLQVVVEEK-------IQWTESEALEEYLKEDKAVSM 7275
Cdd:cd19538     24 YNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVP-YQLILEEDeatpkleIKEVDEEELESEINEAVRYPF 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7276 GLGDPLAHYALVKEAWGGKRWFVWTIHHALYDGGSLPLILHAVKQVYSGAVLERQPSFNAF-IQY----LGQQ------- 7343
Cdd:cd19538    103 DLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLpVQYadyaLWQQellgdes 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7344 ----DLEATAAYWQTALSDCEAVLfpPLPSTVTQPVADT----TVEYQCPP--------LSKATlDTTTSTLIRAAWAIV 7407
Cdd:cd19538    183 dpdsLIARQLAYWKKQLAGLPDEI--ELPTDYPRPAESSyeggTLTFEIDSelhqqllqLAKDN-NVTLFMVLQAGFAAL 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7408 TSCYTSSDDVVYGTTVTGRNApiAGVEAMVGPTIATVPVRLRVQRDQTvfaFLQGLQQ-QSTDMIAHEQtglQHIA--KL 7484
Cdd:cd19538    260 LTRLGAGTDIPIGSPVAGRND--DSLEDLVGFFVNTLVLRTDTSGNPS---FRELLERvKETNLEAYEH---QDIPfeRL 331
                          330       340
                   ....*....|....*....|....
gi 1820002560 7485 -------GSGPRHACgFQTLLVVQ 7501
Cdd:cd19538    332 vealnptRSRSRHPL-FQIMLALQ 354
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
6856-6981 1.12e-04

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 49.39  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6856 GELLVEGPILARGYLNDADKTAAAFVNDpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKV-RGQRVE 6934
Cdd:cd05932    343 GEILVRSPALMMGYYKDPEATAEAFTAD-GFL---------------RTGDKGELDADGNLTITGRVKDIFKTsKGKYVA 406
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 6935 LGEIENRLrecmprATQMAVEVISPAGAAEQAKtmvVAFLQLNDEAR 6981
Cdd:cd05932    407 PAPIENKL------AEHDRVEMVCVIGSGLPAP---LALVVLSEEAR 444
PRK07529 PRK07529
AMP-binding domain protein; Validated
6705-6848 1.14e-04

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 49.18  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6705 HDLFTEQALARPNAPAVC------AWDG--ELTYGELEALSTKLAGHLVQLGVKPEDVV----PLCFEksmwTVVAMLAV 6772
Cdd:PRK07529    28 YELLSRAAARHPDAPALSflldadPLDRpeTWTYAELLADVTRTANLLHSLGVGPGDVVafllPNLPE----THFALWGG 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6773 LKAGGAFvP----LDPDHPASrhedILRQTGAQVI--LASAQNTTLFQSSN---------QTVVTVNRSSYIlfPDENRE 6837
Cdd:PRK07529   104 EAAGIAN-PinplLEPEQIAE----LLRAAGAKVLvtLGPFPGTDIWQKVAevlaalpelRTVVEVDLARYL--PGPKRL 176
                          170
                   ....*....|.
gi 1820002560 6838 AYPFVRPSNAA 6848
Cdd:PRK07529   177 AVPLIRRKAHA 187
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
2070-2351 1.14e-04

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 49.28  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2070 KPENAAYVMFTSGSTGTPKGVVLEH-------RAVVTS----CLGHGQAFGVTNLlrALQFTAYTfdvcIAEIITTLVHG 2138
Cdd:cd05933    148 KPNQCCTLIYTSGTTGMPKGVMLSHdnitwtaKAASQHmdlrPATVGQESVVSYL--PLSHIAAQ----ILDIWLPIKVG 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2139 GCIC-------------------------VP----------------SDSERR--DNLAKAITdMQVNW----GYLTSSV 2171
Cdd:cd05933    222 GQVYfaqpdalkgtlvktlrevrptafmgVPrvwekiqekmkavgakSGTLKRkiASWAKGVG-LETNLklmgGESPSPL 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2172 ARLLDPCLVPSLKVLVLGGEQVNSTDWGKWPSSVQTIN-----------GYGPTECcvfcTG---YTGIQGFQSGNIGTS 2237
Cdd:cd05933    301 FYRLAKKLVFKKVRKALGLDRCQKFFTGAAPISRETLEfflslnipimeLYGMSET----SGphtISNPQAYRLLSCGKA 376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2238 IASV-SWVVDPENHGrlaplgsIGELLVEGPILARGYLNDVDKTQAAfIDDPAWLlegypgHegrqgrlykTGDLVRYSS 2316
Cdd:cd05933    377 LPGCkTKIHNPDADG-------IGEICFWGRHVFMGYLNMEDKTEEA-IDEDGWL------H---------SGDLGKLDE 433
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1820002560 2317 DGNLVCLGR-KDSQVKVRGQRVELGEVEHHMRKCLP 2351
Cdd:cd05933    434 DGFLYITGRiKELIITAGGENVPPVPIEDAVKKELP 469
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
3484-3643 1.26e-04

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 49.21  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3484 DGELTYGELDALSSKLASHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAG--GAFVPldpdhPASRHEEI---FEQT 3557
Cdd:cd05938      3 GETYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLN-----TNIRSKSLlhcFRCC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3558 GAQVVVASAQ-------------------YSARWTSSSCHVVTVSKALSSQLP-AVVDSTNTSVRPENAAYIIFTSGSTG 3617
Cdd:cd05938     78 GAKVLVVAPElqeaveevlpalradgvsvWYLSHTSNTEGVISLLDKVDAASDePVPASLRAHVTIKSPALYIYTSGTTG 157
                          170       180
                   ....*....|....*....|....*.
gi 1820002560 3618 VPKGVVLEHRAVaTSCLGHGRAFGIT 3643
Cdd:cd05938    158 LPKAARISHLRV-LQCSGFLSLCGVT 182
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
875-1024 1.27e-04

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 49.21  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  875 DGELTYGELDELSSKLA-AHLVQLGVKREDVVPLCFEKSMWTVVAMLAVLKAG--GAFVPldpghPASRHEEI---FKQI 948
Cdd:cd05938      3 GETYTYRDVDRRSNQAArALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLN-----TNIRSKSLlhcFRCC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  949 GAQVVLTSS--QHA----------------MLFASSERHQVT--VSKVSTSQLPTVVNFAKSPVDPGNTAYIIFTSGTTG 1008
Cdd:cd05938     78 GAKVLVVAPelQEAveevlpalradgvsvwYLSHTSNTEGVIslLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTG 157
                          170
                   ....*....|....*.
gi 1820002560 1009 IPKGVVLQHRAVTTSC 1024
Cdd:cd05938    158 LPKAARISHLRVLQCS 173
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
2561-2731 1.33e-04

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 48.59  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2561 LTPIQ------HLyltLDPSGrssfD---QCFFLELRNRVQPQLLVTALTALVQRHSMLRarfqrqTGGRWQQyISE--- 2628
Cdd:cd19544      4 LAPLQegilfhHL---LAEEG----DpylLRSLLAFDSRARLDAFLAALQQVIDRHDILR------TAILWEG-LSEpvq 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2629 --HDSSSLIVNHIHTRDTTEIVEALRQ----SRGSLDIERGPVLAAVLCDAGERQSLFVA--IHHLVVDLVSWRILLEEL 2700
Cdd:cd19544     70 vvWRQAELPVEELTLDPGDDALAQLRArfdpRRYRLDLRQAPLLRAHVAEDPANGRWLLLllFHHLISDHTSLELLLEEI 149
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1820002560 2701 EDLLLGQT--LPPALstPF-----QAWHAAQAkyiEEH 2731
Cdd:cd19544    150 QAILAGRAaaLPPPV--PYrnfvaQARLGASQ---AEH 182
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
7747-8124 1.33e-04

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 48.97  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7747 VRPENAAYIIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQ-FASYTFDACIAEIITTLLCGGCICVpsds 7825
Cdd:cd05937     84 VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTcMPLYHGTAAFLGACNCLMSGGTLAL---- 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7826 DRRNSLAKAISTMDVNWAFLTPSVARLLDPGLI--PSL-----KILAIGGEQSSSADWNRWPG--SVQKIH-VYGPTECc 7895
Cdd:cd05937    160 SRKFSASQFWKDVRDSGATIIQYVGELCRYLLStpPSPydrdhKVRVAWGNGLRPDIWERFRErfNVPEIGeFYAATEG- 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7896 ifcTGYTTKQGFEPSTIGtSVASVSWV-------------VDPENHNRL----------APLGSMGELLMEGPILAR--- 7949
Cdd:cd05937    239 ---VFALTNHNVGDFGAG-AIGHHGLIrrwkfenqvvlvkMDPETDDPIrdpktgfcvrAPVGEPGEMLGRVPFKNReaf 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7950 -GYLNDVDKTEAAFIDDPAwllegypghpgRQGRLY-KTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREC 8027
Cdd:cd05937    315 qGYLHNEDATESKLVRDVF-----------RKGDIYfRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAH 383
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8028 LPEARQLAVEVILPsgqkNHAMLAvfvqlgkGTHIAHLEEKAGGEDSMaqvvfltgTEEELA----KRLPKHMVPtVFFA 8103
Cdd:cd05937    384 PDIAEANVYGVKVP----GHDGRA-------GCAAITLEESSAVPTEF--------TKSLLAslarKNLPSYAVP-LFLR 443
                          410       420
                   ....*....|....*....|..
gi 1820002560 8104 LLHFPMTT-SGKADRKRLREIG 8124
Cdd:cd05937    444 LTEEVATTdNHKQQKGVLRDEG 465
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
4567-4711 1.34e-04

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 48.99  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4567 LTYGEL-DTLSSKLASHLVQLGVKPEDMVP-LCFEKSMWTVVAmLAVLKAGGAFVPLDPDHPASRHEHIFRQTGAQVVLA 4644
Cdd:cd17632     68 ITYAELwERVGAVAAAHDPEQPVRPGDFVAvLGFTSPDYATVD-LALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4645 SAQYATLWTSL-------GRSVVI-----------VSEASTSQL-----PVVTKTA----DPSVNPGNAAYA-------- 4689
Cdd:cd17632    147 SAEHLDLAVEAvleggtpPRLVVFdhrpevdahraALESARERLaavgiPVTTLTLiavrGRDLPPAPLFRPepdddpla 226
                          170       180
                   ....*....|....*....|....
gi 1820002560 4690 --IFTSGSTGIPKGVVLEHKAVVT 4711
Cdd:cd17632    227 llIYTSGSTGTPKGAMYTERLVAT 250
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
1532-1797 1.39e-04

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 48.72  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1532 VLELRIDVDEDVFRAAWEHIVRSTAVLRTRIVQhSELGLLQVVIEENIQ---------WTE---PKSLEEylsedkavsv 1599
Cdd:cd19537     29 ACRLSGDVDRDRLASAWNTVLARHRILRSRYVP-RDGGLRRSYSSSPPRvqrvdtldvWKEinrPFDLER---------- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1600 glgDPLARyAFVKEACggkrwFVWTIHHAVYDGWSLPLILHAVKQVYSGGVLQwqPSFNAFIQY--LGQQDLEATVAYWQ 1677
Cdd:cd19537     98 ---EDPIR-VFISPDT-----LLVVMSHIICDLTTLQLLLREVSAAYNGKLLP--PVRREYLDStaWSRPASPEDLDFWS 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1678 TALADCEAVLFPtlPPTVTQPVADATVEYQCPP-LSKATSDTTTST------LIRAAWAIVTSRYTTSDDVVFGTTVTGR 1750
Cdd:cd19537    167 EYLSGLPLLNLP--RRTSSKSYRGTSRVFQLPGsLYRSLLQFSTSSgitlhqLALAAVALALQDLSDRTDIVLGAPYLNR 244
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 1751 NTPVTgvEAMVG----PtiatVPVRLRV--QRDQTVFAFLQGLQ---QQAtdmIAH 1797
Cdd:cd19537    245 TSEED--METVGlfleP----LPIRIRFpsSSDASAADFLRAVRrssQAA---LAH 291
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
3609-3875 1.48e-04

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 48.42  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3609 IIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRnSLAKA 3688
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPA-EALEL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3689 ISTMDVN-WAFLTPSVARLLD-----PGLIPSLKIlaIGGEQSssadwnrwPGSVQKIHV---------YGPTECCIFCT 3753
Cdd:cd17637     84 IEEEKVTlMGSFPPILSNLLDaaeksGVDLSSLRH--VLGLDA--------PETIQRFEEttgatfwslYGQTETSGLVT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3754 G--YTTKqgfePSTIGTSVASVSW-VVDPENhnRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWllegypgh 3830
Cdd:cd17637    154 LspYRER----PGSAGRPGPLVRVrIVDDND--RPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG--W-------- 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 3831 pgrqgrlYKTGDLVQYNADGNLVYLGRKDSQ--VKVRGQRVELGEVE 3875
Cdd:cd17637    218 -------HHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVE 257
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
7755-8021 1.48e-04

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 48.42  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7755 IIFTSGSTGVPKGVVLEHRAVATSCLGHGRAFGITNLSRVLQFASYTFDACIAEIITTLLCGGCICVPSDSDRRnSLAKA 7834
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPA-EALEL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7835 ISTMDVN-WAFLTPSVARLLD-----PGLIPSLKIlaIGGEQSssadwnrwPGSVQKIHV---------YGPTECCIFCT 7899
Cdd:cd17637     84 IEEEKVTlMGSFPPILSNLLDaaeksGVDLSSLRH--VLGLDA--------PETIQRFEEttgatfwslYGQTETSGLVT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7900 G--YTTKqgfePSTIGTSVASVSW-VVDPENhnRLAPLGSMGELLMEGPILARGYLNDVDKTEAAFIDDpaWllegypgh 7976
Cdd:cd17637    154 LspYRER----PGSAGRPGPLVRVrIVDDND--RPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG--W-------- 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1820002560 7977 pgrqgrlYKTGDLVQYNADGNLVYLGRKDSQ--VKVRGQRVELGEVE 8021
Cdd:cd17637    218 -------HHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVE 257
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
16-286 1.49e-04

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 48.90  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   16 LEPSHIPSLRILVMGGEQVNSA----DWDRWPSSVqtINGYGPTECCIVCTGYTSEQDFTTGTigTSIASVSW----VVD 87
Cdd:PRK13295   306 ESGRPVSSLRTFLCAGAPIPGAlverARAALGAKI--VSAWGMTENGAVTLTKLDDPDERAST--TDGCPLPGvevrVVD 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   88 PKdhGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFinnPAWlleghggyagrqgrlYKTGDLVRYDADGNLVCLGR- 166
Cdd:PRK13295   382 AD--GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA---DGW---------------FDTGDLARIDADGYIRISGRs 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  167 KDsqVKLRG-QRVELGEVE----HHvreclPEAKQLAVeVVLP---LGQKnhatLAAFIQLDKGthnallkekvGGDDSI 238
Cdd:PRK13295   442 KD--VIIRGgENIPVVEIEallyRH-----PAIAQVAI-VAYPderLGER----ACAFVVPRPG----------QSLDFE 499
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560  239 ARVVFLAgveeelAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREI 286
Cdd:PRK13295   500 EMVEFLK------AQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREM 541
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
13-286 1.62e-04

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 48.94  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   13 ARLLEPSHIPSLRILVMGGEQVNSADWDRWPSS--VQTINGYGPTECCIVCTgytseqdfttgtIGTSIASVSWVVD--- 87
Cdd:PRK08043   470 ARFANPYDFARLRYVVAGAEKLQESTKQLWQDKfgLRILEGYGVTECAPVVS------------INVPMAAKPGTVGril 537
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   88 PKDHGRLAPLGSV---GELLVEGPILARGYLSdpektaavfINNPAwLLE------GHGGyagRQGRLYKTGDLVRYDAD 158
Cdd:PRK08043   538 PGMDARLLSVPGIeqgGRLQLKGPNIMNGYLR---------VEKPG-VLEvptaenARGE---MERGWYDTGDIVRFDEQ 604
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  159 GNLVCLGRKDSQVKLRGQRVELGEVEhhvreclpeakQLAVEVVlplGQKNHATLAafiQLDKGTHNALLKEKVggDDSI 238
Cdd:PRK08043   605 GFVQIQGRAKRFAKIAGEMVSLEMVE-----------QLALGVS---PDKQHATAI---KSDASKGEALVLFTT--DSEL 665
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1820002560  239 ARVVFLAGVEEelaKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLREI 286
Cdd:PRK08043   666 TREKLQQYARE---HGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSM 710
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
6804-6954 1.73e-04

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 48.75  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6804 LASAQNTTLFQSSNQTVVTVNRSSYILFPD-ENREAYPFVRPsnaalAPLGSIGELLVEGPILARGYLNDADKTAAAFVN 6882
Cdd:PRK07656   316 LSEASGVTTFNRLDDDRKTVAGTIGTAIAGvENKIVNELGEE-----VPVGEVGELLVRGPNVMKGYYDDPEATAAAIDA 390
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 6883 DpAWLvegHgkhpgrrgrlykTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLREcMPRATQMAV 6954
Cdd:PRK07656   391 D-GWL---H------------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYE-HPAVAEAAV 445
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
8282-8511 1.78e-04

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 48.47  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8282 AFNYPF-IDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIprHQDLPFSIFEVNGALAEESQAI-HIR---- 8355
Cdd:cd20484     23 AYNVPLcFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKI--EPSKPLSFQEEDISSLKESEIIaYLRekak 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8356 ---DLDQtSPLglpTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQ-----EPLL--STTGFHSYLAYVH 8425
Cdd:cd20484    101 epfVLEN-GPL---MRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQAllqgkQPTLasSPASYYDFVAWEQ 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8426 NQRS-----ASINYWSRLLKGSH-----ITNITSKLRPKLGKDT-TIR-SVKVERVIRTPQLPTGLTMASLVSSAWAVVL 8493
Cdd:cd20484    177 DMLAgaegeEHRAYWKQQLSGTLpilelPADRPRSSAPSFEGQTyTRRlPSELSNQIKSFARSQSINLSTVFLGIFKLLL 256
                          250
                   ....*....|....*...
gi 1820002560 8494 SHISGEEDVVYGLVVAGR 8511
Cdd:cd20484    257 HRYTGQEDIIVGMPTMGR 274
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
3602-3875 1.95e-04

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 48.57  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3602 RPENAAYIIFTSGSTGVPKGVVLEHR-AVAT---------------------------------------SCLGHGRAFG 3641
Cdd:PLN02387   248 SPNDIAVIMYTSGSTGLPKGVMMTHGnIVATvagvmtvvpklgkndvylaylplahilelaaesvmaavgAAIGYGSPLT 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3642 ITNLSRVLQFASYTfDAciAEIITTLLcggcICVPSDSDR-----------RNSLAKA---------ISTMDVNWaFLTP 3701
Cdd:PLN02387   328 LTDTSNKIKKGTKG-DA--SALKPTLM----TAVPAILDRvrdgvrkkvdaKGGLAKKlfdiaykrrLAAIEGSW-FGAW 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3702 SVARLLDPGLIPSlKILAIGGEQSS---------SADWNRWpgsvqkIHV---------YGPTECCifcTGYTTKQgFEP 3763
Cdd:PLN02387   400 GLEKLLWDALVFK-KIRAVLGGRIRfmlsggaplSGDTQRF------INIclgapigqgYGLTETC---AGATFSE-WDD 468
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3764 STIG--------TSVASVSWvvdPENHNRLA--PLgSMGELLMEGPILARGYLNDVDKTEAAFIDDPawllegypghpgR 3833
Cdd:PLN02387   469 TSVGrvgpplpcCYVKLVSW---EEGGYLISdkPM-PRGEIVIGGPSVTLGYFKNQEKTDEVYKVDE------------R 532
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 3834 QGRLYKTGDLVQYNADGNLVYLGRKDSQVKVR-GQRVELGEVE 3875
Cdd:PLN02387   533 GMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVE 575
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
7748-8021 1.95e-04

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 48.57  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7748 RPENAAYIIFTSGSTGVPKGVVLEHR-AVAT---------------------------------------SCLGHGRAFG 7787
Cdd:PLN02387   248 SPNDIAVIMYTSGSTGLPKGVMMTHGnIVATvagvmtvvpklgkndvylaylplahilelaaesvmaavgAAIGYGSPLT 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7788 ITNLSRVLQFASYTfDAciAEIITTLLcggcICVPSDSDR-----------RNSLAKA---------ISTMDVNWaFLTP 7847
Cdd:PLN02387   328 LTDTSNKIKKGTKG-DA--SALKPTLM----TAVPAILDRvrdgvrkkvdaKGGLAKKlfdiaykrrLAAIEGSW-FGAW 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7848 SVARLLDPGLIPSlKILAIGGEQSS---------SADWNRWpgsvqkIHV---------YGPTECCifcTGYTTKQgFEP 7909
Cdd:PLN02387   400 GLEKLLWDALVFK-KIRAVLGGRIRfmlsggaplSGDTQRF------INIclgapigqgYGLTETC---AGATFSE-WDD 468
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7910 STIG--------TSVASVSWvvdPENHNRLA--PLgSMGELLMEGPILARGYLNDVDKTEAAFIDDPawllegypghpgR 7979
Cdd:PLN02387   469 TSVGrvgpplpcCYVKLVSW---EEGGYLISdkPM-PRGEIVIGGPSVTLGYFKNQEKTDEVYKVDE------------R 532
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 7980 QGRLYKTGDLVQYNADGNLVYLGRKDSQVKVR-GQRVELGEVE 8021
Cdd:PLN02387   533 GMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVE 575
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
1665-1844 1.97e-04

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 48.24  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1665 GQQDLEA----TVAYWQTALADCEAVLF-------PTLPPTVTQPVA---DATVEYQCPPLSKATSdTTTSTLIRAAWAI 1730
Cdd:cd19546    183 GEDDRDSligdQIAYWRDALAGAPDELElptdrprPVLPSRRAGAVPlrlDAEVHARLMEAAESAG-ATMFTVVQAALAM 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1731 VTSRYTTSDDVVFGTTVTgRNTPVTGVEAMVGPTIATVPVRLRVQRDQTVFAFLQGLQQQATDMIAHEQTGLQRIAKM-- 1808
Cdd:cd19546    262 LLTRLGAGTDVTVGTVLP-RDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELla 340
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1820002560 1809 --GQGPQHAcsfqtllVVQPVDDVLDNTLGEWrDHSEL 1844
Cdd:cd19546    341 lpPSADRHP-------VFQVALDVRDDDNDPW-DAPEL 370
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
6851-7043 1.99e-04

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 48.49  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFVNdpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:PRK06710   399 PPGEIGEIVVKGPQIMKGYWNKPEETAAVLQD--GWL---------------HTGDVGYMDEDGFFYVKDRKKDMIVASG 461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6931 QRVELGEIENRLRECMPRATQMAVEVISPAgAAEQAKTMVVaflqlndeardaLLGGNVPNDDNLsaqvvfpakvDEKLS 7010
Cdd:PRK06710   462 FNVYPREVEEVLYEHEKVQEVVTIGVPDPY-RGETVKAFVV------------LKEGTECSEEEL----------NQFAR 518
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1820002560 7011 NLLPSYMMPEVYFAVPQLPMMISGKTDRKRLRE 7043
Cdd:PRK06710   519 KYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2468-2540 2.10e-04

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 43.78  E-value: 2.10e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560  2468 PSTEAERTMQQL----WAQVLGIE-LESIGLDDSFFRLGGDSITAMQISSS-ARALHLSVSTGDILKKKTIALIAREIL 2540
Cdd:smart00823    5 PPAERRRLLLDLvreqVAAVLGHAaAEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALAEHLA 83
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
4689-4975 2.24e-04

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 47.68  E-value: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4689 AIFTSGSTGIPKGVVLEHKAVVTSCLGHGQAFGITDHTRVLQ----FASYTFDACIAeiitTLLCCG-CICVPSDSDRRn 4763
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNsgplFHIGTLMFTLA----TFHAGGtNVFVRRVDAEE- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4764 nLAKAINAMDVNWALLTPsvarmldPCVVQSLKILVLGGEQVNS-----ADWDRWPKSIQTINA-------YGPTECSiC 4831
Cdd:cd17636     80 -VLELIEAERCTHAFLLP-------PTIDQIVELNADGLYDLSSlrsspAAPEWNDMATVDTSPwgrkpggYGQTEVM-G 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4832 CTTYSGKQGFKSGTIG--TSIVSVSwVVDPENhnRLAPLGSIGELLVEGPILARGYLNDMEKTEAAFIDdpawllegyGG 4909
Cdd:cd17636    151 LATFAALGGGAIGGAGrpSPLVQVR-ILDEDG--REVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG---------GW 218
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 4910 HsgrqgrlyKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEhhvrECLTEAKQLA-VEVI-VP 4975
Cdd:cd17636    219 H--------HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVE----RCLRQHPAVAdAAVIgVP 274
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
1952-2111 2.25e-04

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 48.44  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1952 DGELTYGELDALSSKLASHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAG--GAFVPldpdhPASRHEDI---FRQT 2025
Cdd:cd05938      3 GETYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLN-----TNIRSKSLlhcFRCC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2026 GAQVVVTSA--------------QHSARWIGTNHQVVTVSAGSL-----EQFSTLVnPVDLPAKP---ENAAYVmFTSGS 2083
Cdd:cd05938     78 GAKVLVVAPelqeaveevlpalrADGVSVWYLSHTSNTEGVISLldkvdAASDEPV-PASLRAHVtikSPALYI-YTSGT 155
                          170       180
                   ....*....|....*....|....*...
gi 1820002560 2084 TGTPKGVVLEHRAVVtSCLGHGQAFGVT 2111
Cdd:cd05938    156 TGLPKAARISHLRVL-QCSGFLSLCGVT 182
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
6708-6785 2.49e-04

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 48.42  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6708 FTEQALAR---PNAPAVCAWDG----ELTYGELEALSTKLAGHLVQLGVKPED----VVPLCFEksmwTVVAMLAVLKAG 6776
Cdd:cd05943     72 YAENLLRHadaDDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDrvagYLPNIPE----AVVAMLATASIG 147

                   ....*....
gi 1820002560 6777 GAFVPLDPD 6785
Cdd:cd05943    148 AIWSSCSPD 156
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
1944-2102 2.52e-04

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 48.20  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1944 HAPAICAWdgELTYGELDALSSKLASHLVQLgVNPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL-DPDHP--ASRHED 2020
Cdd:PRK12476    60 HSAAGCAV--ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDT 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2021 IFRQTGAQVVVTSaqhsarwigtnhqvvTVSAGSLEQFSTLVNPVDLP------AKPENA--------------AYVMFT 2080
Cdd:PRK12476   137 ALRDAEPTVVLTT---------------TAAAEAVEGFLRNLPRLRRPrviaidAIPDSAgesfvpveldtddvSHLQYT 201
                          170       180
                   ....*....|....*....|..
gi 1820002560 2081 SGSTGTPKGVVLEHRAVVTSCL 2102
Cdd:PRK12476   202 SGSTRPPVGVEITHRAVGTNLV 223
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
24-245 2.71e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 48.12  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   24 LRILVMGGEQVNSADWDRWPS-SVQTI-------NGYGPTEC--CIVCTGYTSEQdftTGTIGTSIASVSWvvdpkdhgR 93
Cdd:PRK12582   348 LRLMAYGGATLSDDLYERMQAlAVRTTghripfyTGYGATETapTTTGTHWDTER---VGLIGLPLPGVEL--------K 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   94 LAPLGSVGELLVEGPILARGYLSDPEKTAAVFINnpawllEGhggyagrqgrLYKTGDLVRY----DADGNLVCLGRKDS 169
Cdd:PRK12582   417 LAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDE------EG----------FYRLGDAARFvdpdDPEKGLIFDGRVAE 480
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  170 QVKL-RGQRVELGEVEHH-VRECLP------------------------EAKQLAVEVVLPLGQ-KNHATLAAFIQLDKG 222
Cdd:PRK12582   481 DFKLsTGTWVSVGTLRPDaVAACSPvihdavvagqdrafigllawpnpaACRQLAGDPDAAPEDvVKHPAVLAILREGLS 560
                          250       260
                   ....*....|....*....|....
gi 1820002560  223 THNAllkeKVGGDDS-IARVVFLA 245
Cdd:PRK12582   561 AHNA----EAGGSSSrIARALLMT 580
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
6701-6784 2.77e-04

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 48.13  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6701 DRCVHDLFTEQALARPNAPAVCAWDGE------LTYGELEALSTKLAGHLVQLGVKPEDVVPlCFEKSMWTVVAM-LAVL 6773
Cdd:PRK13295    23 DRTINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVS-CQLPNWWEFTVLyLACS 101
                           90
                   ....*....|.
gi 1820002560 6774 KAGGAFVPLDP 6784
Cdd:PRK13295   102 RIGAVLNPLMP 112
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
6309-6559 2.83e-04

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 47.70  E-value: 2.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6309 DVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLLQV-------VVEEKIQWTESKRLEEYLREDKAVSMGL-GDPLARYA 6380
Cdd:cd20484     35 KLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIepskplsFQEEDISSLKESEIIAYLREKAKEPFVLeNGPLMRVH 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6381 IIKEawGGKRWFVW-TIHHALYDGWSLPRVLQAVKQAY----NGAVLETQPS---FNAFIQ----YLSQQDLEATAAYWQ 6448
Cdd:cd20484    115 LFSR--SEQEHFVLiTIHHIIFDGSSSLTLIHSLLDAYqallQGKQPTLASSpasYYDFVAweqdMLAGAEGEEHRAYWK 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6449 TALADCEATL--FPPLP-SSVKQLVADTtveHQCPLPSR---------STSDTTTSTLIRAAWAIVASRYTSSDDVVFGT 6516
Cdd:cd20484    193 QQLSGTLPILelPADRPrSSAPSFEGQT---YTRRLPSElsnqiksfaRSQSINLSTVFLGIFKLLLHRYTGQEDIIVGM 269
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 6517 TITGRnaPVTSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQ 6559
Cdd:cd20484    270 PTMGR--PEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQ 310
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3023-3206 2.90e-04

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 47.63  E-value: 2.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3023 FPCTPMQEGILtSQGKDPDAYWvcfiyevipNQ------ETSISLARLQQAWKGVVHQHSLLRTLLVDNvpgSTGTTNVV 3096
Cdd:cd19534      2 VPLTPIQRWFF-EQNLAGRHHF---------NQsvllrvPQGLDPDALRQALRALVEHHDALRMRFRRE---DGGWQQRI 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3097 LKDPQPSISVFSSEGTAtielfrSRYNPAAQRSIGQLQHHLSI----------CQLNNGKVYLCLDINHAIIDAHSRGIL 3166
Cdd:cd19534     69 RGDVEELFRLEVVDLSS------LAQAAAIEALAAEAQSSLDLeegpllaaalFDGTDGGDRLLLVIHHLVVDGVSWRIL 142
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3167 MHDLQEAY------DANLNPQSTSFRDFASYIKQQSQEEAGR----YWAE 3206
Cdd:cd19534    143 LEDLEAAYeqalagEPIPLPSKTSFQTWAELLAEYAQSPALLeelaYWRE 192
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
6856-6943 3.19e-04

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 47.80  E-value: 3.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6856 GELLVEGPILARGYLNDADKTAAAFVNDpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGR-KDGQVKVRGQRVE 6934
Cdd:cd17641    392 GEILVRSPGVFVGYYKNPEATAEDFDED-GWL---------------HTGDAGYFKENGHLVVIDRaKDVGTTSDGTRFS 455

                   ....*....
gi 1820002560 6935 LGEIENRLR 6943
Cdd:cd17641    456 PQFIENKLK 464
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
7938-8016 3.62e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 47.79  E-value: 3.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7938 GELLMEGPILARGYLNDVDKTEAAFIDDpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKV-RGQRVE 8016
Cdd:PTZ00342   542 GELLIKSDSIFSGYFLEKEQTKNAFTED------GY----------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
3792-3870 3.62e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 47.79  E-value: 3.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3792 GELLMEGPILARGYLNDVDKTEAAFIDDpawlleGYpghpgrqgrlYKTGDLVQYNADGNLVYLGRKDSQVKV-RGQRVE 3870
Cdd:PTZ00342   542 GELLIKSDSIFSGYFLEKEQTKNAFTED------GY----------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
PLN02736 PLN02736
long-chain acyl-CoA synthetase
5617-5796 3.79e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 47.79  E-value: 3.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5617 PPAIE-RCVHDLFTEQAKARPHAPA----ICAwDGE------LTYGELDALSSKLAGHLTQLGVKPEDMVPLCF-EKSMW 5684
Cdd:PLN02736    38 PDHPEiGTLHDNFVYAVETFRDYKYlgtrIRV-DGTvgeykwMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFiNRPEW 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5685 TVV--AMLAVLKAGgafVPL----DPDhpASRHedTFRHTGAQVVVTSAQH------------SARWI----GTNHQVVT 5742
Cdd:PLN02736   117 LIVdhACSAYSYVS---VPLydtlGPD--AVKF--IVNHAEVAAIFCVPQTlntllsclseipSVRLIvvvgGADEPLPS 189
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820002560 5743 VSAGSLGQLSTL--------VNPVG-LPAIPENAVYIMFTSGSTGIPKGVVLEHRAVVTSCWG 5796
Cdd:PLN02736   190 LPSGTGVEIVTYskllaqgrSSPQPfRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAG 252
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
7966-8122 3.82e-04

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 47.18  E-value: 3.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7966 PAWLLEGYPGHPGR-----QGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEhhvrECLPEARQLAVEVIL 8040
Cdd:cd05974    287 PVGLMKGYAGDPDKtahamRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE----SVLIEHPAVAEAAVV 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8041 PSgqKNHAMLAV---FVQLgkgthiahleeKAGGEDSMA-QVVFLTGTEEELA--KRLPKhmvptvfFALLHFPMTTSGK 8114
Cdd:cd05974    363 PS--PDPVRLSVpkaFIVL-----------RAGYEPSPEtALEIFRFSRERLApyKRIRR-------LEFAELPKTISGK 422

                   ....*...
gi 1820002560 8115 ADRKRLRE 8122
Cdd:cd05974    423 IRRVELRR 430
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
4872-4950 4.01e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 47.79  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4872 GELLVEGPILARGYLNDMEKTEAAFIDDpawlleGYgghsgrqgrlYKTGDLVRYDADGNLVYLGRKDSQVKL-RGQRVE 4950
Cdd:PTZ00342   542 GELLIKSDSIFSGYFLEKEQTKNAFTED------GY----------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
PRK08315 PRK08315
AMP-binding domain protein; Validated
48-168 4.04e-04

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 47.50  E-value: 4.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   48 TInGYGPTECCIVC--TGYTSEQDFTTGTIGTSIASV-SWVVDPkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAV 124
Cdd:PRK08315   345 TI-AYGMTETSPVStqTRTDDPLEKRVTTVGRALPHLeVKIVDP-ETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA 422
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560  125 fINNPAWLlegHggyagrqgrlykTGDLVRYDADGNLVCLGR-KD 168
Cdd:PRK08315   423 -IDADGWM---H------------TGDLAVMDEEGYVNIVGRiKD 451
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
6853-7038 4.44e-04

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 46.63  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6853 GSIGELLVEGPILARGYLNdadktaAAFVNDPAWlveghgkhpgrrgrlYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQR 6932
Cdd:cd17633    182 GEIGKIFVKSEMVFSGYVR------GGFSNPDGW---------------MSVGDIGYVDEEGYLYLVGRESDMIIIGGIN 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6933 VELGEIENRLRECmPRATQMAVEVISPAGAAEQAKtmvvaflqlndeardALLGGNVPNDDNLSAqvvfpakvdeKLSNL 7012
Cdd:cd17633    241 IFPTEIESVLKAI-PGIEEAIVVGIPDARFGEIAV---------------ALYSGDKLTYKQLKR----------FLKQK 294
                          170       180
                   ....*....|....*....|....*.
gi 1820002560 7013 LPSYMMPEVYFAVPQLPMMISGKTDR 7038
Cdd:cd17633    295 LSRYEIPKKIIFVDSLPYTSSGKIAR 320
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
6865-7043 4.95e-04

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 46.79  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6865 LARGYLNDADKTAAAFvndpawlveghgkhpgrRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLRE 6944
Cdd:cd05974    290 LMKGYAGDPDKTAHAM-----------------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIE 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6945 cMPRATQMAVeVISP-AGAAEQAKTMVVaflqlndeardaLLGGNVPNDDnlSAQVVFPAKVDEklsnLLPSYMMPEVYF 7023
Cdd:cd05974    353 -HPAVAEAAV-VPSPdPVRLSVPKAFIV------------LRAGYEPSPE--TALEIFRFSRER----LAPYKRIRRLEF 412
                          170       180
                   ....*....|....*....|
gi 1820002560 7024 AvpQLPMMISGKTDRKRLRE 7043
Cdd:cd05974    413 A--ELPKTISGKIRRVELRR 430
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
46-287 5.14e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 46.94  E-value: 5.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   46 VQTINGYGPTE-CCIVctgyTSEQDFTTGTIGTSIASVSwVVDPK-----------DHGRLA-PLGSVGELL-VEGPILA 111
Cdd:PRK13388   289 CQVEDGYGSSEgAVIV----VREPGTPPGSIGRGAPGVA-IYNPEtltecavarfdAHGALLnADEAIGELVnTAGAGFF 363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  112 RGYLSDPEKTAAVFinnpawlleghggyagRQGRlYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcL 191
Cdd:PRK13388   364 EGYYNNPEATAERM----------------RHGM-YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLR-H 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  192 PEAKQLAVEVVlPLGQKNHATLAAFIQLDKGTHnallkekvggdDSIARVVFLAGVEEELAKRLPKHM-VPTvffallHF 270
Cdd:PRK13388   426 PAINRVAVYAV-PDERVGDQVMAALVLRDGATF-----------DPDAFAAFLAAQPDLGTKAWPRYVrIAA------DL 487
                          250
                   ....*....|....*..
gi 1820002560  271 PTTTSGKTDRKRLREIG 287
Cdd:PRK13388   488 PSTATNKVLKRELIAQG 504
PRK07798 PRK07798
acyl-CoA synthetase; Validated
6-171 5.39e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 47.19  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    6 ALLTPSV-ARLLEpsHIPSLRIlvmggeqvnsadwdrwpssvqtINGYGPTECCIVCTGYTSEQDFTTGTIGTSIASVSW 84
Cdd:PRK07798   306 ALFSPSVkEALLE--LLPNVVL----------------------TDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRTV 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   85 VVDPkDHGRLAPlGS--VGELLVEGPIlARGYLSDPEKTAAVF--INNPAWLLeghggyagrqgrlykTGDLVRYDADGN 160
Cdd:PRK07798   362 VLDE-DGNPVEP-GSgeIGWIARRGHI-PLGYYKDPEKTAETFptIDGVRYAI---------------PGDRARVEADGT 423
                          170
                   ....*....|.
gi 1820002560  161 LVCLGRkDSQV 171
Cdd:PRK07798   424 ITLLGR-GSVC 433
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
5637-5792 5.54e-04

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 47.04  E-value: 5.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5637 HAPAICAWdgELTYGELDALSSKLAGHLTQLgVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL-DPDHP--ASRHED 5713
Cdd:PRK12476    60 HSAAGCAV--ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDT 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5714 TFRHTGAQVVVTSAqhSARwigtnhQVVTvsaGSLGQLSTLVNP--VGLPAIPENA--------------VYIMFTSGST 5777
Cdd:PRK12476   137 ALRDAEPTVVLTTT--AAA------EAVE---GFLRNLPRLRRPrvIAIDAIPDSAgesfvpveldtddvSHLQYTSGST 205
                          170
                   ....*....|....*
gi 1820002560 5778 GIPKGVVLEHRAVVT 5792
Cdd:PRK12476   206 RPPVGVEITHRAVGT 220
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
6851-6922 5.60e-04

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 46.68  E-value: 5.60e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFVNDPawlveghgkhpgRRGRLYKTGDLVYYNKDGNLVYIGRK 6922
Cdd:cd05910    294 PRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN------------SEGFWHRMGDLGYLDDEGRLWFCGRK 353
PLN02246 PLN02246
4-coumarate--CoA ligase
23-285 5.86e-04

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 46.90  E-value: 5.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   23 SLRILVMG----GEQVNSADWDRWPSSV--QtinGYGPTECCIV---CTGYTSEQdFTT--GTIGTSI--ASVSwVVDPk 89
Cdd:PLN02246   299 SIRMVLSGaaplGKELEDAFRAKLPNAVlgQ---GYGMTEAGPVlamCLAFAKEP-FPVksGSCGTVVrnAELK-IVDP- 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   90 DHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVfINNPAWLlegHggyagrqgrlykTGDLVRYDADGNLVCLGRKDS 169
Cdd:PLN02246   373 ETGASLPRNQPGEICIRGPQIMKGYLNDPEATANT-IDKDGWL---H------------TGDIGYIDDDDELFIVDRLKE 436
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  170 QVKLRGQRVELGEVE-----HhvreclPEAKQLAVevvlpLGQKNHAT---LAAFIQLDKGTHnaLLKEKVggDDSIAR- 240
Cdd:PLN02246   437 LIKYKGFQVAPAELEallisH------PSIADAAV-----VPMKDEVAgevPVAFVVRSNGSE--ITEDEI--KQFVAKq 501
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560  241 VVFLagveeelaKRLPKhmvptVFFAlLHFPTTTSGKTDRKRLRE 285
Cdd:PLN02246   502 VVFY--------KRIHK-----VFFV-DSIPKAPSGKILRKDLRA 532
PRK05691 PRK05691
peptide synthase; Validated
8293-8594 5.95e-04

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 47.47  E-value: 5.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8293 AVDIQVLQASCSALLEHFPILRTHFVYFQGK-LYQVIPRHQDLPFSIFEVNGaLAEESQAIHIRDLDQTSPlglPTSFTL 8371
Cdd:PRK05691  3291 ALDPERFAQAWQAVVARHEALRASFSWNAGEtMLQVIHKPGRTPIDYLDWRG-LPEDGQEQRLQALHKQER---EAGFDL 3366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8372 VRNASGMNRLIiRLSHAQY-----------DGVCMPVIWASLASIYQ------QEPLLSTTGFHSYLAYVHNQR-SASIN 8433
Cdd:PRK05691  3367 LNQPPFHLRLI-RVDEARYwfmmsnhhiliDAWCRSLLMNDFFEIYTalgegrEAQLPVPPRYRDYIGWLQRQDlAQARQ 3445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8434 YWSRLLKGSHITNITSKLRPKL------------GKDTTIRSVKVERVIRTPQLPTGLTMASLVSSAWAVVLSHISGEED 8501
Cdd:PRK05691  3446 WWQDNLRGFERPTPIPSDRPFLrehagdsggmvvGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRD 3525
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8502 VVYGLVVAGRNSDLPSITE-VSVQDQYISLgesdSIGLDDIVQHCT--DWpAKSEFDSIIQHQNIEEQP--EIQFAGETT 8576
Cdd:PRK05691  3526 VLFGVTVAGRPVSMPQMQRtVGLFINSIAL----RVQLPAAGQRCSvrQW-LQGLLDSNMELREYEYLPlvAIQECSELP 3600
                          330
                   ....*....|....*...
gi 1820002560 8577 KLQWFKNSfavsrqLFVF 8594
Cdd:PRK05691  3601 KGQPLFDS------LFVF 3612
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
6855-6978 6.07e-04

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 47.10  E-value: 6.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6855 IGELLVEGPILARGYLNDADKTAAAFVNDpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVE 6934
Cdd:PLN02860   385 VGRILTRGPHVMLGYWGQNSETASVLSND-GWL---------------DTGDIGWIDKAGNLWLIGRSNDRIKTGGENVY 448
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1820002560 6935 LGEIENRLREcMPRATQMAVEVISPAGAAEqaktMVVAFLQLND 6978
Cdd:PLN02860   449 PEEVEAVLSQ-HPGVASVVVVGVPDSRLTE----MVVACVRLRD 487
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
6852-6972 6.07e-04

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 46.34  E-value: 6.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6852 LGSIGELLVEGPILARGYLNDADKTAAAfVNDPAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGRKDGQVKVRGQ 6931
Cdd:cd17638    183 IADDGEVLVRGYNVMQGYLDDPEATAEA-IDADGWL---------------HTGDVGELDERGYLRITDRLKDMYIVGGF 246
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 6932 RVELGEIENRLREcMPRATQMAVEVISPAGAAEQAKTMVVA 6972
Cdd:cd17638    247 NVYPAEVEGALAE-HPGVAQVAVIGVPDERMGEVGKAFVVA 286
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
1172-1365 6.65e-04

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 46.71  E-value: 6.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1172 NHNRLAPLGSIGELLVEGPILARGYLNDIDKTEAAFIDDpAWLlegyeghagrrgrlyKTGDL--VRcdaDGNLVCLGRK 1249
Cdd:cd05908    330 EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDD-GWL---------------KTGDLgfIR---NGRLVITGRE 390
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1250 DSQVKVRGQRVELGEIEhhvreclpearQLAVEVIlpsgqkehallaaFIQLDKGNHNALFEEKASGEDSMAQVVFLTGV 1329
Cdd:cd05908    391 KDIIFVNGQNVYPHDIE-----------RIAEELE-------------GVELGRVVACGVNNSNTRNEEIFCFIEHRKSE 446
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 1330 EE--ELAKRLPEHM-------VPTILfTVKAMPITTSGKIDRKRL 1365
Cdd:cd05908    447 DDfyPLGKKIKKHLnkrggwqINEVL-PIRRIPKTTSGKVKRYEL 490
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
7755-8122 6.69e-04

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 46.69  E-value: 6.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7755 IIFTSGSTGVPKgvVLEHravATSCLGHGRAFG---ITNL--SRVLQFASYT--FDACIAEIITTLLCGGCICVPS---- 7823
Cdd:cd05928    179 IYFTSGTTGSPK--MAEH---SHSSLGLGLKVNgryWLDLtaSDIMWNTSDTgwIKSAWSSLFEPWIQGACVFVHHlprf 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7824 DSdrrNSLAKAISTMDVNWAFLTPSVARLLDPGLI-----PSLKILAIGGEQSSSADWNRWPG--SVQKIHVYGPTECCI 7896
Cdd:cd05928    254 DP---LVILKTLSSYPITTFCGAPTVYRMLVQQDLssykfPSLQHCVTGGEPLNPEVLEKWKAqtGLDIYEGYGQTETGL 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7897 FCTGYTTKQgFEPSTIGTSVASVSWVVDPENHNRLAPlGSMGELLME-GPI----LARGYLNDVDKTEAAFiddpawlle 7971
Cdd:cd05928    331 ICANFKGMK-IKPGSMGKASPPYDVQIIDDNGNVLPP-GTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATI--------- 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7972 gypghpgrQGRLYKTGDLVQYNADGNLVYLGRKDSQVKVRGQRVELGEVEHHVREcLPEARQLAVeVILPSGQKNHAMLA 8051
Cdd:cd05928    400 --------RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIE-HPAVVESAV-VSSPDPIRGEVVKA 469
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560 8052 vFVQLGKGthiahleekaggedsmaqvvFLTGTEEELAKRLPKHM--------VPTVFFALLHFPMTTSGKADRKRLRE 8122
Cdd:cd05928    470 -FVVLAPQ--------------------FLSHDPEQLTKELQQHVksvtapykYPRKVEFVQELPKTVTGKIQRNELRD 527
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
2-285 6.84e-04

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 46.60  E-value: 6.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    2 RVNWALLTPSV-ARLLE-PSHIP------SLRILVMGGE----QVNSADWDRWPSSVqtINGYGPTECCIVCtgYTSEQD 69
Cdd:cd05929    216 RVTFAQFVPTMfVRLLKlPEAVRnaydlsSLKRVIHAAApcppWVKEQWIDWGGPII--WEYYGGTEGQGLT--IINGEE 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   70 FTT--GTIGTSIASVSWVVDpkDHGRLAPLGSVGELLVEGPIlARGYLSDPEKTAAvfinnpawlleghggyAGRQGRLY 147
Cdd:cd05929    292 WLThpGSVGRAVLGKVHILD--EDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAA----------------ARNEGGWS 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  148 KTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREClPEAKQLAVeVVLP---LGQKNHATlaafIQldkgth 224
Cdd:cd05929    353 TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH-PKVLDAAV-VGVPdeeLGQRVHAV----VQ------ 420
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560  225 nallkekvGGDDSIARVVFLAGVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:cd05929    421 --------PAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
6712-6808 7.25e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 46.61  E-value: 7.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6712 ALARPNAPAVC-AWDGE-LTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 6789
Cdd:PRK13391     7 AQTTPDKPAVImASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90
                   ....*....|....*....
gi 1820002560 6790 RHEDILRQTGAQVILASAQ 6808
Cdd:PRK13391    87 EAAYIVDDSGARALITSAA 105
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
4566-5055 7.46e-04

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 46.66  E-value: 7.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4566 ELTYGELDTLSSKLASHLVQLgVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPL-DPDHP--ASRHEHIFRQTGAQVV 4642
Cdd:PRK12476    68 ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVV 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4643 LASAQYATLWTS-------LGRSVVIV-----SEASTSQLPVVTKTADpsvnpgnAAYAIFTSGSTGIPKGVVLEHKAVV 4710
Cdd:PRK12476   147 LTTTAAAEAVEGflrnlprLRRPRVIAidaipDSAGESFVPVELDTDD-------VSHLQYTSGSTRPPVGVEITHRAVG 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4711 TSCLGHGQAFGITD-HTRVLQFASYTFDACIAEIITTLLCCGCICV--PSDSDRRNNL---AKAINAMDVNWALLTPSVA 4784
Cdd:PRK12476   220 TNLVQMILSIDLLDrNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLmsPTAFVRRPQRwikALSEGSRTGRVVTAAPNFA 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4785 ------RMLDPC---VVQSLKILVLGGEQVNSAdwdrwpkSIQTINA---------------YGPTECSICCTT------ 4834
Cdd:PRK12476   300 yewaaqRGLPAEgddIDLSNVVLIIGSEPVSID-------AVTTFNKafapyglprtafkpsYGIAEATLFVATiapdae 372
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4835 ----YSGKQGFKSGTI-------GTSIVSVS--------W--VVDPENHNRLaPLGSIGELLVEGPILARGYLNDMEKTE 4893
Cdd:PRK12476   373 psvvYLDREQLGAGRAvrvaadaPNAVAHVScgqvarsqWavIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETE 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4894 AAFIDDPAWLLEGyGGHSGR---QGRLYKTGDLVRYdADGNLVYLGRKDSQVKLRGQrvelgevEHHVREclTEAkqlAV 4970
Cdd:PRK12476   452 RTFGAKLQSRLAE-GSHADGaadDGTWLRTGDLGVY-LDGELYITGRIADLIVIDGR-------NHYPQD--IEA---TV 517
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4971 EVIVPEGEGGYAmlAAFVQLGDDTYN-TLVKEKAGGDSLTVQVVFLDRVEEELAKRVPEHMMLTTFFTLEAMPTTTSGKI 5049
Cdd:PRK12476   518 AEASPMVRRGYV--TAFTVPAEDNERlVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKL 595

                   ....*.
gi 1820002560 5050 DRKRLR 5055
Cdd:PRK12476   596 ARRACR 601
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
6842-6971 7.69e-04

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 46.42  E-value: 7.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPlGSIGELLVEGPILARGYLNDADKTAAAFVNdpAWLveghgkhpgrrgrlyKTGDLVYYNKDGNLVYIGR 6921
Cdd:PRK05852   368 VGSDGLPLPA-GAVGEVWLRGTTVVRGYLGDPTITAANFTD--GWL---------------RTGDLGSLSAAGDLSIRGR 429
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6922 KDGQVKVRGQRVELGEIENRLRECmPRATQMAVEVISPAGAAEQAKTMVV 6971
Cdd:PRK05852   430 IKELINRGGEKISPERVEGVLASH-PNVMEAAVFGVPDQLYGEAVAAVIV 478
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
6851-6942 7.87e-04

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 46.49  E-value: 7.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFvndpawlVEGHGKhpgrrgRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:PRK08314   380 PPGEVGEIVVHGPQVFKGYWNRPEATAEAF-------IEIDGK------RFFRTGDLGRMDEEGYFFITDRLKRMINASG 446
                           90
                   ....*....|..
gi 1820002560 6931 QRVELGEIENRL 6942
Cdd:PRK08314   447 FKVWPAEVENLL 458
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
5228-5476 8.34e-04

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 46.30  E-value: 8.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5228 DVDEDAFRAAWEHVVQLTAALRTRIVQHSELGLL-QVVVE------EKIQWTESKRLEEYLREDKAVSMGLGD-RLARYA 5299
Cdd:cd19532     35 PLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPmQGVLAssplrlEHVQISDEAEVEEEFERLKNHVYDLESgETMRIV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5300 LIKEPYDggKRWFVWTIHHALYDGWSLPRILQAVKQIYSGAVPERQPSfnafiQYLG-----QQDLEAATL-----YWQT 5369
Cdd:cd19532    115 LLSLSPT--EHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPL-----QYLDfaarqRQDYESGALdedlaYWKS 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5370 ALADckaaLFPTLPPTvtqPVADTTVEyqcPPPSQSAT-------DITTSTLVR---------------AAWAIVTSRYT 5427
Cdd:cd19532    188 EFST----LPEPLPLL---PFAKVKSR---PPLTRYDThtaerrlDAALAARIKeasrklrvtpfhfylAALQVLLARLL 257
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1820002560 5428 SSDDVVFGATVTGRNAPiaGVEAMVGPTIATVPLRVCLQKDQTVSTLLE 5476
Cdd:cd19532    258 DVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQTFADVLK 304
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
4818-5058 9.24e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 46.17  E-value: 9.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4818 QTINAYGPTECSICCTTysgKQGFKSGTIGTSIVSVSwVVDPEN-----------HNRLA-PLGSIGELL-VEGPILARG 4884
Cdd:PRK13388   290 QVEDGYGSSEGAVIVVR---EPGTPPGSIGRGAPGVA-IYNPETltecavarfdaHGALLnADEAIGELVnTAGAGFFEG 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4885 YLNDMEKTEAAFiddpawllegygghsgRQGRlYKTGDLVRYDADGNLVYLGRKDSQVKLRGQRVELGEVEHHVREcLTE 4964
Cdd:PRK13388   366 YYNNPEATAERM----------------RHGM-YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLR-HPA 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4965 AKQLAVeVIVPEGEGGYAMLAAFVQLGDDTYNTlvkekaggDSLTvqvVFLDRVEEELAKRVPEHMMLTTfftleAMPTT 5044
Cdd:PRK13388   428 INRVAV-YAVPDERVGDQVMAALVLRDGATFDP--------DAFA---AFLAAQPDLGTKAWPRYVRIAA-----DLPST 490
                          250
                   ....*....|....
gi 1820002560 5045 TSGKIDRKRLREIG 5058
Cdd:PRK13388   491 ATNKVLKRELIAQG 504
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
79-175 9.46e-04

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 46.27  E-value: 9.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   79 IASVSW--VVDPkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINN-PAWLLEG-HGGYAGRQGRLYKTGDLVR 154
Cdd:PRK12476   407 VARSQWavIVDP-DTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKlQSRLAEGsHADGAADDGTWLRTGDLGV 485
                           90       100
                   ....*....|....*....|.
gi 1820002560  155 YdADGNLVCLGRKDSQVKLRG 175
Cdd:PRK12476   486 Y-LDGELYITGRIADLIVIDG 505
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
5220-5396 9.64e-04

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 46.09  E-value: 9.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5220 QSVLeLRV--DVDEDAFRAAWEHVVQLTAALRTRIVQHS----------ELGLLQVVVEEKIQWTESKRLEEyLREDKAV 5287
Cdd:cd19534     24 QSVL-LRVpqGLDPDALRQALRALVEHHDALRMRFRREDggwqqrirgdVEELFRLEVVDLSSLAQAAAIEA-LAAEAQS 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5288 SMGLGD-RLARYALIKEPYDGGKRWFVwtIHHALYDG--WslpRIL-----QAVKQIYSGAVPERQP--SFNAFIQ---- 5353
Cdd:cd19534    102 SLDLEEgPLLAAALFDGTDGGDRLLLV--IHHLVVDGvsW---RILledleAAYEQALAGEPIPLPSktSFQTWAEllae 176
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1820002560 5354 YLGQQDLEAATLYWQTALADckaaLFPTLPPTVTQPVADTTVE 5396
Cdd:cd19534    177 YAQSPALLEELAYWRELPAA----DYWGLPKDPEQTYGDARTV 215
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
6900-7044 9.68e-04

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 46.14  E-value: 9.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6900 RLYKTGDLVYYNKDGNLVYIGRKDGQVKVRGQRVELGEIENRLRecmprATQMaVEVISPAGAA-EQAKTMVVAFLqlnd 6978
Cdd:PRK07445   324 GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAIL-----ATGL-VQDVCVLGLPdPHWGEVVTAIY---- 393
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820002560 6979 eardallggnVPNDDNLSaqvvfPAKVDEKLSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRLREI 7044
Cdd:PRK07445   394 ----------VPKDPSIS-----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
5768-6051 9.76e-04

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 45.76  E-value: 9.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5768 VYIMFTSGSTGIPKGVVLEHRAVVTSCWGRGRAFGITNlsrvlqfaSYTFDAC---------MDEIITTLMYGGCICVPS 5838
Cdd:cd17636      3 VLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDE--------GTVFLNSgplfhigtlMFTLATFHAGGTNVFVRR 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5839 DSDRRndLVKAISTMDVSCALLT-PSVARLLEPSSVPTLQMLVLQgEQVSFADWN--------RWPASVqtiNGYGPTEC 5909
Cdd:cd17636     75 VDAEE--VLELIEAERCTHAFLLpPTIDQIVELNADGLYDLSSLR-SSPAAPEWNdmatvdtsPWGRKP---GGYGQTEV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5910 S--ICCNTYSGKQgfksgiIGTSVASVSWV----VDPEnhDRLAPLGSIGELLVEGPILARGYLNDIQKTAAVFIDdpAW 5983
Cdd:cd17636    149 MglATFAALGGGA------IGGAGRPSPLVqvriLDED--GREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG--GW 218
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820002560 5984 llegypghpgrqgrlYKTGDLVRYDANGNLVCLGRKDSQVKLRGQRVELGEVEHHVREcLPEARQLAV 6051
Cdd:cd17636    219 ---------------HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQ-HPAVADAAV 270
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
2063-2103 1.00e-03

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 46.35  E-value: 1.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1820002560 2063 NPVDL-PAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLG 2103
Cdd:PLN02430   210 NPSETnPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRG 251
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
7630-7789 1.03e-03

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 46.13  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7630 DGELTYGELDVLSSNLAGHLV-QLGVNPEDVVPLCFEKSMWTVVAMLAVLKAG--GAFVPldpdhPASRHEEI---FEQT 7703
Cdd:cd05938      3 GETYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLN-----TNIRSKSLlhcFRCC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 7704 GAQVVVASAQ-------------------YSARWTSSSCHVVTVSKALSSQLP-AVVDSTNTSVRPENAAYIIFTSGSTG 7763
Cdd:cd05938     78 GAKVLVVAPElqeaveevlpalradgvsvWYLSHTSNTEGVISLLDKVDAASDePVPASLRAHVTIKSPALYIYTSGTTG 157
                          170       180
                   ....*....|....*....|....*.
gi 1820002560 7764 VPKGVVLEHRAVaTSCLGHGRAFGIT 7789
Cdd:cd05938    158 LPKAARISHLRV-LQCSGFLSLCGVT 182
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
6856-6934 1.03e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 46.25  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6856 GELLVEGPILARGYLNDADKTAAAFVNDpawlveghgkhpgrrgRLYKTGDLVYYNKDGNLVYIGRKDGQVKV-RGQRVE 6934
Cdd:PTZ00342   542 GELLIKSDSIFSGYFLEKEQTKNAFTED----------------GYFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
6850-6939 1.06e-03

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 46.20  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6850 APLGSIGELLVEGPILARGYLNDADKTAAafVNDPAWLVeghgkhpgrrgrlykTGDLVYYNKDGNLVYIGRKDGQVKVR 6929
Cdd:PRK08974   399 VPPGEPGELWVKGPQVMLGYWQRPEATDE--VIKDGWLA---------------TGDIAVMDEEGFLRIVDRKKDMILVS 461
                           90
                   ....*....|
gi 1820002560 6930 GQRVELGEIE 6939
Cdd:PRK08974   462 GFNVYPNEIE 471
PRK09274 PRK09274
peptide synthase; Provisional
6851-6933 1.07e-03

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 46.05  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFVNDpawlveghgkhpGRRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:PRK09274   383 ATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPD------------GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAG 450

                   ...
gi 1820002560 6931 QRV 6933
Cdd:PRK09274   451 GTL 453
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
65-280 1.12e-03

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 45.47  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   65 TSEQDFTT----------GTIGTSIASVSWVVDPKDHGrlaplgSVGELLVEGPILARGYLSdpektaAVFINNPAWlle 134
Cdd:cd17633    145 TSELSFITynfnqesrppNSVGRPFPNVEIEIRNADGG------EIGKIFVKSEMVFSGYVR------GGFSNPDGW--- 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  135 ghggyagrqgrlYKTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEHHVREC--LPEAkqlaveVVLPLGQKNHAT 212
Cdd:cd17633    210 ------------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIpgIEEA------IVVGIPDARFGE 271
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560  213 LAAFIQL-DKGTHNALLKEkvggddsiarvvflagveeeLAKRLPKHMVPTVFFALLHFPTTTSGKTDR 280
Cdd:cd17633    272 IAVALYSgDKLTYKQLKRF--------------------LKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK12316 PRK12316
peptide synthase; Provisional
8282-8512 1.16e-03

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 46.49  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8282 AFNYP-FIDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIPRHQDLPFSIFEVNGaLAEESQAIHIRDLDQT 8360
Cdd:PRK12316    71 AYNLPsAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSG-LPEAEQEARLRDEAQR 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8361 SPL-------GLPTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQ-----QEPLLSTTGFHsYLAYVHNQR 8428
Cdd:PRK12316   150 ESLqpfdlceGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSayatgAEPGLPALPIQ-YADYALWQR 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8429 S--------ASINYWSRLLKGSH--ITNITSKLRPKLgkdTTIRSVKVE--------RVIRTPQLPTGLTMASLVSSAWA 8490
Cdd:PRK12316   229 SwleageqeRQLEYWRAQLGEEHpvLELPTDHPRPAV---PSYRGSRYEfsidpalaEALRGTARRQGLTLFMLLLGAFN 305
                          250       260
                   ....*....|....*....|..
gi 1820002560 8491 VVLSHISGEEDVVYGLVVAGRN 8512
Cdd:PRK12316   306 VLLHRYSGQTDIRVGVPIANRN 327
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
6842-6923 1.21e-03

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 46.08  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6842 VRPSNAALAPLGSIGELLVEGPILARGYLNDADKTAAAFVNDPAwlveghgkhpGRRGRLYKTGDLVYYnKDGNLVYIGR 6921
Cdd:cd05931    369 VDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAA----------TDEGGWLRTGDLGFL-HDGELYITGR 437

                   ...
gi 1820002560 6922 -KD 6923
Cdd:cd05931    438 lKD 440
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
22-179 1.29e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 45.86  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   22 PSLRILVMGGEQVnSADWDRWPS---SVQTINGYGPTECcivcTGYTSEQ---DFTTGTIGTSIAS------VSW-VVDP 88
Cdd:PTZ00342   461 PNLEVILNGGGKL-SPKIAEELSvllNVNYYQGYGLTET----TGPIFVQhadDNNTESIGGPISPntkykvRTWeTYKA 535
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   89 KDhgrLAPLGsvgELLVEGPILARGYLSDPEKTAAVFINNpawlleghgGYagrqgrlYKTGDLVRYDADGNLVCLGRKD 168
Cdd:PTZ00342   536 TD---TLPKG---ELLIKSDSIFSGYFLEKEQTKNAFTED---------GY-------FKTGDIVQINKNGSLTFLDRSK 593
                          170
                   ....*....|..
gi 1820002560  169 SQVKL-RGQRVE 179
Cdd:PTZ00342   594 GLVKLsQGEYIE 605
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
880-1020 1.35e-03

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 45.91  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  880 YGELDELSSKLAAHLVQLGvkREDVVPLCFEKSMWTVVAMLAVLKAGGAFVPL-------DPGHPASRHEEIFKQIGAQV 952
Cdd:PRK05851    34 WPEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAAVSILpgpvrgaDDGRWADATLTRFAGIGVRT 111
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560  953 VLTSSQHAmlfassERHQVTVSKVSTSQLPTVVNFAKS----PVDPGNTAYIIFTSGTTGIPKGVVLQHRAV 1020
Cdd:PRK05851   112 VLSHGSHL------ERLRAVDSSVTVHDLATAAHTNRSasltPPDSGGPAVLQGTAGSTGTPRTAILSPGAV 177
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
21-286 1.42e-03

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 45.77  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   21 IPSLRILVMGGEQVNS--ADWDRWPSSVQTINGYGPTEC-CIVCTGYTSEQDFTTGTiGTSIASVSW----VVDpkDHGR 93
Cdd:cd05967    354 LSSLRTLFLAGERLDPptLEWAENTLGVPVIDHWWQTETgWPITANPVGLEPLPIKA-GSPGKPVPGyqvqVLD--EDGE 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   94 LAPLGSVGELLVEGPIlargylsdPEKTAAVFINNPAWLLEGhggYAGRQGRLYKTGDLVRYDADGNLVCLGRKDSQVKL 173
Cdd:cd05967    431 PVGPNELGNIVIKLPL--------PPGCLLTLWKNDERFKKL---YLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINV 499
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  174 RGQRVELGEVEhhvreclpeakqlavEVVLplgqkNHATLA--AFIqldkGTHNALlkekvGGDDSIARVVFLAGV---E 248
Cdd:cd05967    500 AGHRLSTGEME---------------ESVL-----SHPAVAecAVV----GVRDEL-----KGQVPLGLVVLKEGVkitA 550
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1820002560  249 EELAKRLPKHMV----PTVFFALLHF----PTTTSGKTDRKRLREI 286
Cdd:cd05967    551 EELEKELVALVReqigPVAAFRLVIFvkrlPKTRSGKILRRTLRKI 596
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
21-284 1.57e-03

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 45.16  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   21 IPSLRILVMGGEQVNSADWDRWP--SSVQTINGYGPTECCIVCTGYTSEQDFTTGTIGTSI--ASVSWVV-DPKDHG--R 93
Cdd:cd05944    120 ISSLRFAMSGAAPLPVELRARFEdaTGLPVVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLpyARVRIKVlDGVGRLlrD 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   94 LAPlGSVGELLVEGPILARGYLSDPEktaavfiNNPAWLleghggyagrQGRLYKTGDLVRYDADGNLVCLGRKDSQVKL 173
Cdd:cd05944    200 CAP-DEVGEICVAGPGVFGGYLYTEG-------NKNAFV----------ADGWLNTGDLGRLDADGYLFITGRAKDLIIR 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  174 RGQRVELGEVEhhvrECLpeAKQLAVEVVLPLGQKN-HA--TLAAFIQLDKGThnallkekvggddSIARVVFLAGVEEE 250
Cdd:cd05944    262 GGHNIDPALIE----EAL--LRHPAVAFAGAVGQPDaHAgeLPVAYVQLKPGA-------------VVEEEELLAWARDH 322
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1820002560  251 LAKR--LPKHMVPtvffaLLHFPTTTSGKTDRKRLR 284
Cdd:cd05944    323 VPERaaVPKHIEV-----LEELPVTAVGKVFKPALR 353
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
1993-2446 1.62e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 45.40  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1993 VVAMLAVLKAGGAFVPLDPDH-PASRHEDIfRQTGAQVVVTSAQHSARWIGTNHQVVTVSAGSLEQFSTLVNPvDLPAKP 2071
Cdd:PRK13388    66 LFWLAAAALGGYVLVGLNTTRrGAALAADI-RRADCQLLVTDAEHRPLLDGLDLPGVRVLDVDTPAYAELVAA-AGALTP 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2072 ENAAYVM------FTSGSTGTPKGVVLEHRAVVTSCLGHGQAFGVTnllRAlqftaytfDVC------------IAEIIT 2133
Cdd:PRK13388   144 HREVDAMdpfmliFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT---RD--------DVCyvsmplfhsnavMAGWAP 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2134 TLVHGGCICVPS--------DSERR------DNLAKAItdmqvnwGYLTSSVARLLDpclvpSLKVLVLG-GEQVNSTDW 2198
Cdd:PRK13388   213 AVASGAAVALPAkfsasgflDDVRRygatyfNYVGKPL-------AYILATPERPDD-----ADNPLRVAfGNEASPRDI 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2199 GKWPS--SVQTINGYGPTECCVFCTGytgIQGFQSGNIGTSIASVSwVVDPEN-----------HGRLA-PLGSIGELL- 2263
Cdd:PRK13388   281 AEFSRrfGCQVEDGYGSSEGAVIVVR---EPGTPPGSIGRGAPGVA-IYNPETltecavarfdaHGALLnADEAIGELVn 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2264 VEGPILARGYLNDVDKTQAAFiddpawllegypghegRQGRlYKTGDLVRYSSDGNLVCLGRKDSQVKVRGQRVELGEVE 2343
Cdd:PRK13388   357 TAGAGFFEGYYNNPEATAERM----------------RHGM-YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIE 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2344 HHMRKcLPEANQLAVEVVPPSGERDHAMlAAFIRLDDETrnspliikYAEDNSTAqivFLTGIEEelserLPQHMVPTVF 2423
Cdd:PRK13388   420 RILLR-HPAINRVAVYAVPDERVGDQVM-AALVLRDGAT--------FDPDAFAA---FLAAQPD-----LGTKAWPRYV 481
                          490       500
                   ....*....|....*....|...
gi 1820002560 2424 FALVHFPTTTSGKTDRKRLREIG 2446
Cdd:PRK13388   482 RIAADLPSTATNKVLKRELIAQG 504
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
6849-7041 1.72e-03

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 45.19  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6849 LAPLGSIGELLVEGPILA--RGYLNDADKTAAAfvndpawLVEGhgkhpgrrgrLYKTGDLVYYNKDGNLVYIGRKDGQV 6926
Cdd:cd05923    339 ALANGEEGELIVAAAADAafTGYLNQPEATAKK-------LQDG----------WYRTGDVGYVDPSGDVRILGRVDDMI 401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6927 KVRGQRVELGEIEnrlrECMPRATQMaVEVISPAGAAEQAKTMVVAFLqlndeardallggnVPNDDNLSAQvvfpaKVD 7006
Cdd:cd05923    402 ISGGENIHPSEIE----RVLSRHPGV-TEVVVIGVADERWGQSVTACV--------------VPREGTLSAD-----ELD 457
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1820002560 7007 EK-LSNLLPSYMMPEVYFAVPQLPMMISGKTDRKRL 7041
Cdd:cd05923    458 QFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
592-761 1.73e-03

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 45.16  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  592 AYWQTALADCEAVLFPP-------LPSTVTQPVAdttVKYQCPPSPEVT----SSNITTSTLIRAAWAIIASRYTSSEDI 660
Cdd:cd19546    196 AYWRDALAGAPDELELPtdrprpvLPSRRAGAVP---LRLDAEVHARLMeaaeSAGATMFTVVQAALAMLLTRLGAGTDV 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  661 VFGTTVTgRNAPITGVEAMVGPTIATVPLRVRPRKGQTVSAFLENLQQQATEMIAYEQTGLQRIMKM----GPGPQHACg 736
Cdd:cd19546    273 TVGTVLP-RDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELlalpPSADRHPV- 350
                          170       180
                   ....*....|....*....|....*
gi 1820002560  737 FQTLLVVHptddvlssDDTLGEWHS 761
Cdd:cd19546    351 FQVALDVR--------DDDNDPWDA 367
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
6716-6831 1.74e-03

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 45.16  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6716 PNAPAVC----AWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPASRH 6791
Cdd:cd17654      1 PDRPALIidqtTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1820002560 6792 EDILRQTGAQVILASAQNTTLFQSSNQTVVTVNRS-----SYILF 6831
Cdd:cd17654     81 LTVMKKCHVSYLLQNKELDNAPLSFTPEHRHFNIRtdeclAYVIH 125
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
79-168 1.75e-03

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 45.49  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   79 IASVSW--VVDPkDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINN-PAWLLEGHGGYAGRQGRLYKTGDLVRY 155
Cdd:PRK07769   396 VGVSEWavIVDP-ETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNIlKSRLSESHAEGAPDDALWVRTGDYGVY 474
                           90
                   ....*....|....
gi 1820002560  156 dADGNLVCLGR-KD 168
Cdd:PRK07769   475 -FDGELYITGRvKD 487
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
6804-6923 1.78e-03

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 45.49  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6804 LASAqntTLFQSSNQ-----TVVTVNRSS-----YILFPDENREAYP--------------FVRPSNAALAPLGSIGELL 6859
Cdd:PRK07769   346 MAEA---TLFVSTTPmdeepTVIYVDRDElnagrFVEVPADAPNAVAqvsagkvgvsewavIVDPETASELPDGQIGEIW 422
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820002560 6860 VEGPILARGYLNDADKTAAAFVND-PAWLVEGHGKHPGRRGRLYKTGDL-VYYnkDGNLVYIGR-KD 6923
Cdd:PRK07769   423 LHGNNIGTGYWGKPEETAATFQNIlKSRLSESHAEGAPDDALWVRTGDYgVYF--DGELYITGRvKD 487
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
2244-2343 1.90e-03

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 44.95  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2244 VVDPEnhGRLAPLGSIGELLVEGPILARGYLNDVDKTQAAFIDDpaWllegypghegrqgrlYKTGDLVRYSSDGNLVCL 2323
Cdd:cd17637    175 IVDDN--DRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG--W---------------HHTGDLGRFDEDGYLWYA 235
                           90       100
                   ....*....|....*....|..
gi 1820002560 2324 GRKDSQ--VKVRGQRVELGEVE 2343
Cdd:cd17637    236 GRKPEKelIKPGGENVYPAEVE 257
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
450-710 1.96e-03

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 44.87  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  450 VLELRADVDEHAFRAAWEYVVQSIAVLRTRIVQhSELGLLQVVVEE--KMQWTESESLEEYLNedkaasmgLGDRLARYA 527
Cdd:cd19537     29 ACRLSGDVDRDRLASAWNTVLARHRILRSRYVP-RDGGLRRSYSSSppRVQRVDTLDVWKEIN--------RPFDLERED 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  528 LIKESCgGKRWFVWTIHHALYDGWSLPLVLDAVKQVYSGAALerQPSFNTFIQYV--SQQDVKAAAAYWQTALADCEAVL 605
Cdd:cd19537    100 PIRVFI-SPDTLLVVMSHIICDLTTLQLLLREVSAAYNGKLL--PPVRREYLDSTawSRPASPEDLDFWSEYLSGLPLLN 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  606 FPPLPSTVTqpVADTTVKYQCPPSPE------VTSSNITTSTLIRAAWAIIASRYTSSEDIVFGTTVTGRNAPITgvEAM 679
Cdd:cd19537    177 LPRRTSSKS--YRGTSRVFQLPGSLYrsllqfSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEED--MET 252
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1820002560  680 VG----PtiatVPLRVR--PRKGQTVSAFLENLQ---QQA 710
Cdd:cd19537    253 VGlfleP----LPIRIRfpSSSDASAADFLRAVRrssQAA 288
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
4141-4315 1.97e-03

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 44.94  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4141 VLELRADVNEDAFRAAWELVVQLTAVLRTRIVQHSElGLLQVV---VEERIQWtESESLEEYPREDK-----AVSMGVGD 4212
Cdd:cd19534     27 LLRVPQGLDPDALRQALRALVEHHDALRMRFRREDG-GWQQRIrgdVEELFRL-EVVDLSSLAQAAAiealaAEAQSSLD 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4213 ----RLARYALIKEPYDGGKRWFVwtMHHALYDG--WslpRILH-----AVKQAYSG--VVLERQPSFNAFIQ----YLS 4275
Cdd:cd19534    105 leegPLLAAALFDGTDGGDRLLLV--IHHLVVDGvsW---RILLedleaAYEQALAGepIPLPSKTSFQTWAEllaeYAQ 179
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1820002560 4276 QQDPEAAAAYWQTALvdckAALFPTLPPTVTQPVADTTVE 4315
Cdd:cd19534    180 SPALLEELAYWRELP----AADYWGLPKDPEQTYGDARTV 215
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
6708-6849 2.15e-03

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 45.02  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6708 FTEQALAR-PNAPAVCAWDGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDH 6786
Cdd:PRK06710    29 YVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 6787 PASRHEDILRQTGAQVIL---------ASAQNTTLFQSsnqtVVTVNRSSYILFPdeNREAYPFVRPSNAAL 6849
Cdd:PRK06710   109 TERELEYQLHDSGAKVILcldlvfprvTNVQSATKIEH----VIVTRIADFLPFP--KNLLYPFVQKKQSNL 174
PRK07470 PRK07470
acyl-CoA synthetase; Validated
90-150 2.29e-03

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 45.03  E-value: 2.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820002560   90 DHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVFINnpAWLLEGHGGYAGRQGRLYKTG 150
Cdd:PRK07470   356 DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRD--GWFRTGDLGHLDARGFLYITG 414
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
990-1026 2.60e-03

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 44.81  E-value: 2.60e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1820002560  990 SPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLG 1026
Cdd:PLN02430   215 NPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRG 251
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
989-1026 2.81e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 44.97  E-value: 2.81e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1820002560  989 KSPVDPGNTAYIIFTSGTTGIPKGVVLQHRAVTTSCLG 1026
Cdd:PTZ00216   258 NIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILA 295
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
4276-4452 2.91e-03

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 44.39  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4276 QQDPEAAA----AYWQTALVDCKAALfpTLPPTVTQPVADT----TVEYQCPPPSQS-------ATDITTSTLARAAWAI 4340
Cdd:cd19546    184 EDDRDSLIgdqiAYWRDALAGAPDEL--ELPTDRPRPVLPSrragAVPLRLDAEVHArlmeaaeSAGATMFTVVQAALAM 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 4341 VTSRYTSSDDVVFGaTVTGRNAPIAGGEAIVGPTIATVPVRLRVQRDQTVFAFLQGVQQQATDMIAHEQTGLQRIAKM-- 4418
Cdd:cd19546    262 LLTRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELla 340
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1820002560 4419 --SPGARHACgFQTLLVVQptddvlgsDDMLGEWRS 4452
Cdd:cd19546    341 lpPSADRHPV-FQVALDVR--------DDDNDPWDA 367
PRK13382 PRK13382
bile acid CoA ligase;
50-285 2.92e-03

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 44.75  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   50 NGYGPTECCIVCTGYTSEQDFTTGTIGT-SIASVSWVVDPKdhGRLAPLGSVGELLVEGPILARGYLSDPEKtaavfinn 128
Cdd:PRK13382   342 NNYNATEAGMIATATPADLRAAPDTAGRpAEGTEIRILDQD--FREVPTGEVGTIFVRNDTQFDGYTSGSTK-------- 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560  129 pawllEGHGGYAGrqgrlykTGDLVRYDADGNLVCLGRKDSQVKLRGQRVELGEVEhHVRECLPEAKQLAVEVV--LPLG 206
Cdd:PRK13382   412 -----DFHDGFMA-------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVE-KTLATHPDVAEAAVIGVddEQYG 478
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820002560  207 QKnhatLAAFIQLDKGThnALLKEKvggddsiarvvflagVEEELAKRLPKHMVPTVFFALLHFPTTTSGKTDRKRLRE 285
Cdd:PRK13382   479 QR----LAAFVVLKPGA--SATPET---------------LKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
1955-2112 3.11e-03

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 44.83  E-value: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 1955 LTYGELDALSSKLASHLVQLGVNPEDVVPL----CFEksmWtVVAMLAVLKAGGAFVPLDPDHPASRHEDIFRQtgAQVV 2030
Cdd:PLN02861    78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIygsnCPE---W-IIAMEACNSQGITYVPLYDTLGANAVEFIINH--AEVS 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2031 VTSAQHSA---------------RWIGTNHQVVT----------VSAGSLEQFSTLVN-PVDLPAK-PENAAYVMFTSGS 2083
Cdd:PLN02861   152 IAFVQESKissilsclpkcssnlKTIVSFGDVSSeqkeeaeelgVSCFSWEEFSLMGSlDCELPPKqKTDICTIMYTSGT 231
                          170       180
                   ....*....|....*....|....*....
gi 1820002560 2084 TGTPKGVVLEHRAVVTSCLGHGQAFGVTN 2112
Cdd:PLN02861   232 TGEPKGVILTNRAIIAEVLSTDHLLKVTD 260
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
8478-8511 3.38e-03

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 44.35  E-value: 3.38e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1820002560 8478 GLTMASLVSSAWAVVLSHISGEEDVVYGLVVAGR 8511
Cdd:cd19544    235 GVSPASLFHLAWALVLARCSGRDDVVFGTVLSGR 268
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
5-125 3.40e-03

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 44.34  E-value: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560    5 WALLTPSVAR--LLEPSHIPSLRILVMGGEQVNSADWDRWPS-SVQTIN-------GYGPTECCIVCTGYTSEQDfTTGT 74
Cdd:cd05921    271 WEMLVAALEKdeALRRRFFKRLKLMFYAGAGLSQDVWDRLQAlAVATVGeripmmaGLGATETAPTATFTHWPTE-RSGL 349
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820002560   75 IGTSIasvswvvdPKDHGRLAPLGSVGELLVEGPILARGYLSDPEKTAAVF 125
Cdd:cd05921    350 IGLPA--------PGTELKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAF 392
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
85-184 3.42e-03

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 44.50  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560   85 VVDPKDHGRlaPLGSVGEL-LVEG-PILARGYLSDPEKTAAVFINNpaWlleghggyagrqgrlYKTGDLVRYDADGNLV 162
Cdd:PRK04319   389 IVDDQGNEL--PPNRMGNLaIKKGwPSMMRGIWNNPEKYESYFAGD--W---------------YVSGDSAYMDEDGYFW 449
                           90       100
                   ....*....|....*....|..
gi 1820002560  163 CLGRKDSQVKLRGQRVELGEVE 184
Cdd:PRK04319   450 FQGRVDDVIKTSGERVGPFEVE 471
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
3059-3211 4.00e-03

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 44.18  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3059 ISLARLQQAWKGVVHQHSLLRTLL--VDNVPgstgtTNVVLKDPQPSIsVFSSEGTATIELfRSRYNPAAQRSIgQLQH- 3135
Cdd:cd19538     36 LDVQALQQALYDVVERHESLRTVFpeEDGVP-----YQLILEEDEATP-KLEIKEVDEEEL-ESEINEAVRYPF-DLSEe 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 3136 ---HLSICQLNNGKVYLCLDINHAIIDAHSRGILMHDLQEAYDANLNPQSTSF-------RDFASYIKQQSQEEAGR--- 3202
Cdd:cd19538    108 ppfRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELaplpvqyADYALWQQELLGDESDPdsl 187
                          170
                   ....*....|....*
gi 1820002560 3203 ------YWAEYLDGV 3211
Cdd:cd19538    188 iarqlaYWKKQLAGL 202
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
8262-8439 4.48e-03

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 43.78  E-value: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8262 VPASYIQQFYIATgVRAPREAFNYPF-IDLSDAVDIQVLQASCSALLEHFPILRTHFVYFQGKLYQVIPR--HQDLPFSI 8338
Cdd:cd19534      2 VPLTPIQRWFFEQ-NLAGRHHFNQSVlLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGdvEELFRLEV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 8339 FEVNG--------ALAEESQaihiRDLD-QTSPLglpTSFTLVRNASGMNRLIIRLSHAQYDGVCMPVIWASLASIYQQE 8409
Cdd:cd19534     81 VDLSSlaqaaaieALAAEAQ----SSLDlEEGPL---LAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQA 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1820002560 8410 ------PLLSTTGFHSYLAYVHN-----QRSASINYWSRLL 8439
Cdd:cd19534    154 lagepiPLPSKTSFQTWAELLAEyaqspALLEELAYWRELP 194
PRK06188 PRK06188
acyl-CoA synthetase; Validated
6851-6922 5.19e-03

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 43.82  E-value: 5.19e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFVNDpaWLvegHgkhpgrrgrlykTGDLVYYNKDGNLVYIGRK 6922
Cdd:PRK06188   361 AQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG--WL---H------------TGDVAREDEDGFYYIVDRK 415
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
2852-2994 5.22e-03

non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.


Pssm-ID: 273774 [Multi-domain]  Cd Length: 153  Bit Score: 41.49  E-value: 5.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2852 DAIRETKDCIRSFQDNGWSYFASQFASASAADAFASLFPmEVLFNYQGLYQQLERkDSLFKnlPMPDSCEPALAALCPRF 2931
Cdd:TIGR01720    4 RLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEKLAASPQP-EISFNYLGQFDADSN-DELFQ--PSSYSPGEAISPESPRP 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 2932 ALFDVSFVVEQGCAKVSFVSDKRARHQYRIRQWIQKYKVTLIDMSAL-LPNRSAEWTLSDLPLA 2994
Cdd:TIGR01720   80 YALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHcAGKEGGGLTPSDFSLK 143
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
2561-2727 5.65e-03

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 43.51  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2561 LTPIQH-LYLT--LDPSGrSSFDQCFFLELRNRVQPQLLVTALTALVQRHSMLRARFQRQTGGRWqQYISEhdSSSLIVN 2637
Cdd:cd19533      4 LTSAQRgVWFAeqLDPEG-SIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPY-QWIDP--YTPVPIR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 2638 HIHTR-DTTEIVEALR----QSRGSLDIERGP-VLAAVLCDAGERQSLFVAIHHLVVDLVSWRILLEELEDL----LLGQ 2707
Cdd:cd19533     80 HIDLSgDPDPEGAAQQwmqeDLRKPLPLDNDPlFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIytalLKGR 159
                          170       180
                   ....*....|....*....|
gi 1820002560 2708 TLPPALSTPFQAWHAAQAKY 2727
Cdd:cd19533    160 PAPPAPFGSFLDLVEEEQAY 179
PRK08316 PRK08316
acyl-CoA synthetase; Validated
6851-6939 5.81e-03

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 43.77  E-value: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6851 PLGSIGELLVEGPILARGYLNDADKTAAAFvndpawlveghgkhpgrRGRLYKTGDLVYYNKDGNLVYIGRKDGQVKVRG 6930
Cdd:PRK08316   363 APGEVGEIVHRSPQLMLGYWDDPEKTAEAF-----------------RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGG 425

                   ....*....
gi 1820002560 6931 QRVELGEIE 6939
Cdd:PRK08316   426 ENVASREVE 434
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
6711-6808 7.73e-03

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 43.31  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6711 QALARPNAPAVCAWDGELTYGELEALSTKLAGHLV-QLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGAFVPLDPDHPAS 6789
Cdd:PRK06839    11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
                           90
                   ....*....|....*....
gi 1820002560 6790 RHEDILRQTGAQVILASAQ 6808
Cdd:PRK06839    91 ELIFQLKDSGTTVLFVEKT 109
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
6725-6778 8.12e-03

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 43.11  E-value: 8.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1820002560 6725 DGELTYGELEALSTKLAGHLVQLGVKPEDVVPLCFEKSMWTVVAMLAVLKAGGA 6778
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV 54
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
2064-2103 8.94e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 43.04  E-value: 8.94e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1820002560 2064 PVDLPAKPENAAYVMFTSGSTGTPKGVVLEHRAVVTSCLG 2103
Cdd:PTZ00216   256 PLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILA 295
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
6445-6611 9.75e-03

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 42.85  E-value: 9.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6445 AYWQTALADCEATLFPPLPSSVKQLVADTTVE---------HQCPLPSRSTSDTTTSTLIRAAWAIVASRYTSSDDVVFG 6515
Cdd:cd19546    196 AYWRDALAGAPDELELPTDRPRPVLPSRRAGAvplrldaevHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVG 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 6516 TTITgRNAPVTSIDAIVGPTIATVPLRVRLQKDQTVSSFLGYLQQQATEMIAYEQTGLQQIAKM----GPDPQHAcgfqt 6591
Cdd:cd19546    276 TVLP-RDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELlalpPSADRHP----- 349
                          170       180
                   ....*....|....*....|
gi 1820002560 6592 llVVQPAGDVlgSDDTLGKW 6611
Cdd:cd19546    350 --VFQVALDV--RDDDNDPW 365
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
5636-5792 9.94e-03

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 43.06  E-value: 9.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5636 PHAPAicawdgELTYGELDALSSKLAGHLTQLGVKPEDMVPLCFEKSMWTVVAMLAVLKAGGAFVPLdpdH-PASR---- 5710
Cdd:PRK07768    24 PDAPV------RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTML---HqPTPRtdla 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820002560 5711 --HEDT---FRHTGAQVVVTSA-------QHSARWIgtnhQVVTVSAgSLGQLstlvnPVGLPAIPENAVYIM-FTSGST 5777
Cdd:PRK07768    95 vwAEDTlrvIGMIGAKAVVVGEpflaaapVLEEKGI----RVLTVAD-LLAAD-----PIDPVETGEDDLALMqLTSGST 164
                          170
                   ....*....|....*
gi 1820002560 5778 GIPKGVVLEHRAVVT 5792
Cdd:PRK07768   165 GSPKAVQITHGNLYA 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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