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Conserved domains on  [gi|490930577|ref|WP_004792430|]
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MULTISPECIES: non-ribosomal peptide synthetase [Acinetobacter]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 1017720)

non-ribosomal peptide synthetase is a modular multidomain enzyme that acts as an assembly line to catalyze the biosynthesis of complex natural products

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
entF super family cl35902
enterobactin non-ribosomal peptide synthetase EntF;
1098-2372 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


The actual alignment was detected with superfamily member PRK10252:

Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 1046.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1098 STILPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQA 1176
Cdd:PRK10252    5 SQHLPLVAAQPGIWMAEKLSPLPSaWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1177 WPVQFCSVTPDLLEQT---IQEALQQPIHLDQPYGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDF--IKAYQQ 1251
Cdd:PRK10252   85 PEIIDLRTQPDPHAAAqalMQADLQQDLRVDSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIaaIYCAWL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1252 TNQQLPVLEHSYETVIKALSGRDHETSKviWQRD-------LADLQPLILFNQAQQAVQETSYR-----LSAELGAKLQH 1319
Cdd:PRK10252  165 RGEPTPASPFTPFADVVEEYQRYRASEA--WQRDaafwaeqRRQLPPPASLSPAPLPGRSASADilrlkLEFTDGAFRQL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1320 KLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGR--SAPIngleQQIGLFLNTIPVRVKLNMQQTLWE------- 1390
Cdd:PRK10252  243 AAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlgSAAL----TATGPVLNVLPLRVHIAAQETLPElatrlaa 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1391 QLPQL---QQLHVEHLEHDgLGLSAIQQliaqgNLFDSLLVVE------NYPDNQYLQQKLGDAAISKLTnrgyshypLA 1461
Cdd:PRK10252  319 QLKKMrrhQRYDAEQIVRD-SGRAAGDE-----PLFGPVLNIKvfdyqlDFPGVQAQTHTLATGPVNDLE--------LA 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1462 LLVIPDHQIELLLE---QRGVIDQPEHFLERMIQLIEIALNEPETSLSHYRLQLAEEHDLIQKTNQTQYYVRQSTLQQLL 1538
Cdd:PRK10252  385 LFPDEHGGLSIEILanpQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALV 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1539 REQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPT 1618
Cdd:PRK10252  465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1619 ERIKFMLQDAKSKLVIGEQKDLAAIVH-PSIATFAFNELF---DETKVDLSSykttvitPQHPAYLIYTSGTTGQPKGVM 1694
Cdd:PRK10252  545 DRLKMMLEDARPSLLITTADQLPRFADvPDLTSLCYNAPLapqGAAPLQLSQ-------PHHTAYIIFTSGSTGRPKGVM 617
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVP 1774
Cdd:PRK10252  618 VGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVP 697
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1775 SMLAVFENAATEilSSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATlglhPEE---- 1850
Cdd:PRK10252  698 SMLAAFVASLTP--EGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAF----GEElaav 771
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1851 --SCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADG 1928
Cdd:PRK10252  772 rgSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDG 851
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1929 SIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD-VVVHAISSEQNKANV----QLVAYL--QTTAPVDIDQLKKQLAK 2001
Cdd:PRK10252  852 AVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEqAVTHACVINQAAATGgdarQLVGYLvsQSGLPLDTSALQAQLRE 931
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2002 HLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTpSNTEKQYATSAFEHELTRIFQQILNTDQNiGVNEDFFAIGGHS 2081
Cdd:PRK10252  932 RLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELK-AQVPGRAPKTGTETIIAAAFSSLLGCDVV-DADADFFALGGHS 1009
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2082 ILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQErlAEVEQTGMQPILPIRSGSGHPLFCFYPGSGSAWQYTVL 2161
Cdd:PRK10252 1010 LLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEE--DESRRLGFGTILPLREGDGPTLFCFHPASGFAWQFSVL 1087
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2162 NRYLHSDLPIIGLQSPRPDGLLANSTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVAAKLTEQGEKVDYLGLL 2241
Cdd:PRK10252 1088 SRYLDPQWSIYGIQSPRPDGPMQTATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLL 1167
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2242 DTYPAEIHQWLDLSVEEMN----AEAEQEQLQFfndiLADADSALSEEtrrLQEDIFANYRDAVRLLKPYKMPHFDGELH 2317
Cdd:PRK10252 1168 DTWPPETQNWREKEANGLDpevlAEIDREREAF----LAAQQGSLSTE---LFTTIEGNYADAVRLLTTAHSVPFDGKAT 1240
                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 2318 LVVAEKDLLPYIQPEQQWSPLVKKLNIVRLSEAdHTDILSPQQLETLGPILNRMI 2372
Cdd:PRK10252 1241 LFVAERTLQEGMSPEQAWSPWIAELDVYRQDCA-HVDIISPEAFEKIGPILRATL 1294
PRK12316 super family cl36106
peptide synthase; Provisional
53-2138 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12316:

Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 912.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   53 VDIPTFKKAIQIGLNEADTVIASY--SSDPSQPFIELNNQVQFQIEEFDFchLTPKKAQQRLWDWMPSDRQCAKSLKAGE 130
Cdd:PRK12316 1590 LDPDRFRAAWQATVDRHEILRSGFlwQDGLEQPLQVIHKQVELPFAELDW--RGREDLGQALDALAQAERQKGFDLTRAP 1667
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  131 tqLFRQVLFTT----HDKVYwyqRYHHIMLDGFSMINLTKRIVELYQ-QLQEGKDLSVSPFIGvnevISERQAYENShqf 205
Cdd:PRK12316 1668 --LLRLVLVRTgegrHHLIY---TNHHILMDGWSNAQLLGEVLQRYAgQPVAAPGGRYRDYIA----WLQRQDAAAS--- 1735
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  206 kidQAFWKAYCEDLPSPISLSTHHLAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAEL 285
Cdd:PRK12316 1736 ---EAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETV 1812
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  286 VNGipfmrrlGSKAIRST-LPTV--------NVLPVkfkVAEKDSWVSLA---QHVQEQLREIRPHQKYDAEQILRdlns 353
Cdd:PRK12316 1813 AFG-------ATVAGRPAeLPGIeqqiglfiNTLPV---IAAPRPDQSVAdwlQEVQALNLALREHEHTPLYDIQR---- 1878
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  354 idihermYGPILNYKAFDQDLVIDGEKVkTHHISTGPIDDFEFSFIVqDHE---------------LIIELRADSQRYTQ 418
Cdd:PRK12316 1879 -------WAGQGGEALFDSLLVFENYPV-AEALKQGAPAGLVFGRVS-NHEqtnypltlavtlgetLSLQYSYDRGHFDA 1949
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  419 DELFNHGQRLTLLLEQALIRPEQPCSNFNITTPQELTALTQSGIGPRVSHPEQYNnVLDIFYEQVKKYPERTAIVSGErp 498
Cdd:PRK12316 1950 AAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPG-VHQRIAEQAARAPEAIAVVFGD-- 2026
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  499 nlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFV 578
Cdd:PRK12316 2027 --QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  579 LTTQALAQQLP--QNIQQLHLDQEGvqtqirkqDASDIPAENRKFDF--QDVAYVIFTSGSTGRPKGVMNTHGSLLNLIl 654
Cdd:PRK12316 2105 LTQRHLLERLPlpAGVARLPLDRDA--------EWADYPDTAPAVQLagENLAYVIYTSGSTGLPKGVAVSHGALVAHC- 2175
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  655 shkptiywpvlEAVNERFPDRPL-RAAHTHSFSFDSSWLQVFW-MLWGQELHIFDENMRrDAFGLVQEIQQRQIDTLDLP 732
Cdd:PRK12316 2176 -----------QAAGERYELSPAdCELQFMSFSFDGAHEQWFHpLLNGARVLIRDDELW-DPEQLYDEMERHGVTILDFP 2243
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  733 PSFCAQmmtnglFVENQHH----PSL--ILIGGEAAPLALW-QQLNAQPALFAHNLYGPTEYTVDTF-----RAELKQTA 800
Cdd:PRK12316 2244 PVYLQQ------LAEHAERdgrpPAVrvYCFGGEAVPAASLrLAWEALRPVYLFNGYGPTEAVVTPLlwkcrPQDPCGAA 2317
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  801 RPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEH-GQRMYRTGDLVRWNSAGKL 879
Cdd:PRK12316 2318 YVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsGERLYRTGDLARYRADGVV 2397
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  880 EFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIeldektSEQLSQQYLSQLRQNLP 959
Cdd:PRK12316 2398 EYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDA------AEDLLAELRAWLAARLP 2471
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  960 EYMVPSALTVMSEFPRNVSGKVDKKALPKPQIRAHSRMAETPE---QQLLCQITASVLKLDAIGIDDDFFMTGGDSISAI 1036
Cdd:PRK12316 2472 AYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQeglEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLAT 2551
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1037 MLCTQLRQ-RGYSLRPSDVFQFKTVAAMApqlTRLDEQQAAVSKPLFSADLEQKvqekygknstiLPLLPLQKGMLFLSQ 1115
Cdd:PRK12316 2552 QVVSRVRQdLGLEVPLRILFERPTLAAFA---ASLESGQTSRAPVLQKVTRVQP-----------LPLSHAQQRQWFLWQ 2617
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1116 VENQS-NYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQAWPVQFCSVTPDLLEQTIQ 1194
Cdd:PRK12316 2618 LEPESaAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVA 2697
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1195 EALQQPIHLdQPYGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQ--QLPVLEHSYETVIKALSG 1272
Cdd:PRK12316 2698 EEIQRPFDL-ARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRgeQPTLPPLPLQYADYAAWQ 2776
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1273 RDHETSK------VIWQRDLADLQPLILF-------NQAQQAVQETSYRLSAELGAKLQHKLRQQGITLNVFMQMIWAMT 1339
Cdd:PRK12316 2777 RAWMDSGegarqlDYWRERLGGEQPVLELpldrprpALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVL 2856
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1340 LNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGL----SAIQQ 1415
Cdd:PRK12316 2857 LHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFeqlvEALQP 2934
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1416 LIAQGN--LFDSLLVVENYPDNQYLQQKLGDAAISKLTNRGYSHYPLALLVIPDHQIELLLEQRGVIDQP--EHFLERMI 1491
Cdd:PRK12316 2935 ERSLSHspLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARtvERLARHWQ 3014
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1492 QLIEIALNEPETSLSHYRLQLAEEHDLI-QKTNQTQ-YYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCA 1569
Cdd:PRK12316 3015 NLLRGMVENPQRSVDELAMLDAEERGQLlEAWNATAaEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANR 3094
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQkdlaaivHPSIA 1649
Cdd:PRK12316 3095 LAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS-------HLRLP 3167
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1650 TFAFNE--LFDETKVDLSSYKTTV-ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCT 1726
Cdd:PRK12316 3168 LAQGVQvlDLDRGDENYAEANPAIrTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS 3247
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1727 FDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaateILSSAQRQSLPICRVFCSGE 1806
Cdd:PRK12316 3248 FDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAF------LEEEDAHRCTSLKRIVCGGE 3321
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1807 ALPTALAKSFTEHFSceLHNLYGPTEAAVDVSYMDATlglHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAG 1886
Cdd:PRK12316 3322 ALPADLQQQVFAGLP--LYNLYGPTEATITVTHWQCV---EEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGG 3396
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1887 HQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVV 1965
Cdd:PRK12316 3397 EGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVrEAV 3476
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1966 VHAISSEqnkanvQLVAYLQTTAPVDI--DQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEK 2043
Cdd:PRK12316 3477 VLAVDGR------QLVAYVVPEDEAGDlrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDY 3550
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2044 QYATSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPiGQLMSHVTIQRLAALLLTQERL 2123
Cdd:PRK12316 3551 VAPVNELERRLAAIWADVLKLEQ-VGLTDNFFELGGDSIISLQVVSRARQAGIRFTP-KDLFQHQTIQGLARVARVGGGV 3628
                        2170
                  ....*....|....*...
gi 490930577 2124 AeVEQ---TGMQPILPIR 2138
Cdd:PRK12316 3629 A-VDQgpvSGETLLLPIQ 3645
 
Name Accession Description Interval E-value
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1098-2372 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 1046.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1098 STILPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQA 1176
Cdd:PRK10252    5 SQHLPLVAAQPGIWMAEKLSPLPSaWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1177 WPVQFCSVTPDLLEQT---IQEALQQPIHLDQPYGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDF--IKAYQQ 1251
Cdd:PRK10252   85 PEIIDLRTQPDPHAAAqalMQADLQQDLRVDSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIaaIYCAWL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1252 TNQQLPVLEHSYETVIKALSGRDHETSKviWQRD-------LADLQPLILFNQAQQAVQETSYR-----LSAELGAKLQH 1319
Cdd:PRK10252  165 RGEPTPASPFTPFADVVEEYQRYRASEA--WQRDaafwaeqRRQLPPPASLSPAPLPGRSASADilrlkLEFTDGAFRQL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1320 KLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGR--SAPIngleQQIGLFLNTIPVRVKLNMQQTLWE------- 1390
Cdd:PRK10252  243 AAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlgSAAL----TATGPVLNVLPLRVHIAAQETLPElatrlaa 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1391 QLPQL---QQLHVEHLEHDgLGLSAIQQliaqgNLFDSLLVVE------NYPDNQYLQQKLGDAAISKLTnrgyshypLA 1461
Cdd:PRK10252  319 QLKKMrrhQRYDAEQIVRD-SGRAAGDE-----PLFGPVLNIKvfdyqlDFPGVQAQTHTLATGPVNDLE--------LA 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1462 LLVIPDHQIELLLE---QRGVIDQPEHFLERMIQLIEIALNEPETSLSHYRLQLAEEHDLIQKTNQTQYYVRQSTLQQLL 1538
Cdd:PRK10252  385 LFPDEHGGLSIEILanpQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALV 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1539 REQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPT 1618
Cdd:PRK10252  465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1619 ERIKFMLQDAKSKLVIGEQKDLAAIVH-PSIATFAFNELF---DETKVDLSSykttvitPQHPAYLIYTSGTTGQPKGVM 1694
Cdd:PRK10252  545 DRLKMMLEDARPSLLITTADQLPRFADvPDLTSLCYNAPLapqGAAPLQLSQ-------PHHTAYIIFTSGSTGRPKGVM 617
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVP 1774
Cdd:PRK10252  618 VGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVP 697
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1775 SMLAVFENAATEilSSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATlglhPEE---- 1850
Cdd:PRK10252  698 SMLAAFVASLTP--EGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAF----GEElaav 771
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1851 --SCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADG 1928
Cdd:PRK10252  772 rgSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDG 851
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1929 SIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD-VVVHAISSEQNKANV----QLVAYL--QTTAPVDIDQLKKQLAK 2001
Cdd:PRK10252  852 AVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEqAVTHACVINQAAATGgdarQLVGYLvsQSGLPLDTSALQAQLRE 931
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2002 HLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTpSNTEKQYATSAFEHELTRIFQQILNTDQNiGVNEDFFAIGGHS 2081
Cdd:PRK10252  932 RLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELK-AQVPGRAPKTGTETIIAAAFSSLLGCDVV-DADADFFALGGHS 1009
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2082 ILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQErlAEVEQTGMQPILPIRSGSGHPLFCFYPGSGSAWQYTVL 2161
Cdd:PRK10252 1010 LLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEE--DESRRLGFGTILPLREGDGPTLFCFHPASGFAWQFSVL 1087
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2162 NRYLHSDLPIIGLQSPRPDGLLANSTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVAAKLTEQGEKVDYLGLL 2241
Cdd:PRK10252 1088 SRYLDPQWSIYGIQSPRPDGPMQTATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLL 1167
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2242 DTYPAEIHQWLDLSVEEMN----AEAEQEQLQFfndiLADADSALSEEtrrLQEDIFANYRDAVRLLKPYKMPHFDGELH 2317
Cdd:PRK10252 1168 DTWPPETQNWREKEANGLDpevlAEIDREREAF----LAAQQGSLSTE---LFTTIEGNYADAVRLLTTAHSVPFDGKAT 1240
                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 2318 LVVAEKDLLPYIQPEQQWSPLVKKLNIVRLSEAdHTDILSPQQLETLGPILNRMI 2372
Cdd:PRK10252 1241 LFVAERTLQEGMSPEQAWSPWIAELDVYRQDCA-HVDIISPEAFEKIGPILRATL 1294
PRK12316 PRK12316
peptide synthase; Provisional
53-2138 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 912.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   53 VDIPTFKKAIQIGLNEADTVIASY--SSDPSQPFIELNNQVQFQIEEFDFchLTPKKAQQRLWDWMPSDRQCAKSLKAGE 130
Cdd:PRK12316 1590 LDPDRFRAAWQATVDRHEILRSGFlwQDGLEQPLQVIHKQVELPFAELDW--RGREDLGQALDALAQAERQKGFDLTRAP 1667
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  131 tqLFRQVLFTT----HDKVYwyqRYHHIMLDGFSMINLTKRIVELYQ-QLQEGKDLSVSPFIGvnevISERQAYENShqf 205
Cdd:PRK12316 1668 --LLRLVLVRTgegrHHLIY---TNHHILMDGWSNAQLLGEVLQRYAgQPVAAPGGRYRDYIA----WLQRQDAAAS--- 1735
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  206 kidQAFWKAYCEDLPSPISLSTHHLAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAEL 285
Cdd:PRK12316 1736 ---EAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETV 1812
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  286 VNGipfmrrlGSKAIRST-LPTV--------NVLPVkfkVAEKDSWVSLA---QHVQEQLREIRPHQKYDAEQILRdlns 353
Cdd:PRK12316 1813 AFG-------ATVAGRPAeLPGIeqqiglfiNTLPV---IAAPRPDQSVAdwlQEVQALNLALREHEHTPLYDIQR---- 1878
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  354 idihermYGPILNYKAFDQDLVIDGEKVkTHHISTGPIDDFEFSFIVqDHE---------------LIIELRADSQRYTQ 418
Cdd:PRK12316 1879 -------WAGQGGEALFDSLLVFENYPV-AEALKQGAPAGLVFGRVS-NHEqtnypltlavtlgetLSLQYSYDRGHFDA 1949
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  419 DELFNHGQRLTLLLEQALIRPEQPCSNFNITTPQELTALTQSGIGPRVSHPEQYNnVLDIFYEQVKKYPERTAIVSGErp 498
Cdd:PRK12316 1950 AAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPG-VHQRIAEQAARAPEAIAVVFGD-- 2026
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  499 nlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFV 578
Cdd:PRK12316 2027 --QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  579 LTTQALAQQLP--QNIQQLHLDQEGvqtqirkqDASDIPAENRKFDF--QDVAYVIFTSGSTGRPKGVMNTHGSLLNLIl 654
Cdd:PRK12316 2105 LTQRHLLERLPlpAGVARLPLDRDA--------EWADYPDTAPAVQLagENLAYVIYTSGSTGLPKGVAVSHGALVAHC- 2175
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  655 shkptiywpvlEAVNERFPDRPL-RAAHTHSFSFDSSWLQVFW-MLWGQELHIFDENMRrDAFGLVQEIQQRQIDTLDLP 732
Cdd:PRK12316 2176 -----------QAAGERYELSPAdCELQFMSFSFDGAHEQWFHpLLNGARVLIRDDELW-DPEQLYDEMERHGVTILDFP 2243
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  733 PSFCAQmmtnglFVENQHH----PSL--ILIGGEAAPLALW-QQLNAQPALFAHNLYGPTEYTVDTF-----RAELKQTA 800
Cdd:PRK12316 2244 PVYLQQ------LAEHAERdgrpPAVrvYCFGGEAVPAASLrLAWEALRPVYLFNGYGPTEAVVTPLlwkcrPQDPCGAA 2317
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  801 RPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEH-GQRMYRTGDLVRWNSAGKL 879
Cdd:PRK12316 2318 YVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsGERLYRTGDLARYRADGVV 2397
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  880 EFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIeldektSEQLSQQYLSQLRQNLP 959
Cdd:PRK12316 2398 EYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDA------AEDLLAELRAWLAARLP 2471
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  960 EYMVPSALTVMSEFPRNVSGKVDKKALPKPQIRAHSRMAETPE---QQLLCQITASVLKLDAIGIDDDFFMTGGDSISAI 1036
Cdd:PRK12316 2472 AYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQeglEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLAT 2551
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1037 MLCTQLRQ-RGYSLRPSDVFQFKTVAAMApqlTRLDEQQAAVSKPLFSADLEQKvqekygknstiLPLLPLQKGMLFLSQ 1115
Cdd:PRK12316 2552 QVVSRVRQdLGLEVPLRILFERPTLAAFA---ASLESGQTSRAPVLQKVTRVQP-----------LPLSHAQQRQWFLWQ 2617
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1116 VENQS-NYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQAWPVQFCSVTPDLLEQTIQ 1194
Cdd:PRK12316 2618 LEPESaAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVA 2697
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1195 EALQQPIHLdQPYGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQ--QLPVLEHSYETVIKALSG 1272
Cdd:PRK12316 2698 EEIQRPFDL-ARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRgeQPTLPPLPLQYADYAAWQ 2776
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1273 RDHETSK------VIWQRDLADLQPLILF-------NQAQQAVQETSYRLSAELGAKLQHKLRQQGITLNVFMQMIWAMT 1339
Cdd:PRK12316 2777 RAWMDSGegarqlDYWRERLGGEQPVLELpldrprpALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVL 2856
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1340 LNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGL----SAIQQ 1415
Cdd:PRK12316 2857 LHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFeqlvEALQP 2934
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1416 LIAQGN--LFDSLLVVENYPDNQYLQQKLGDAAISKLTNRGYSHYPLALLVIPDHQIELLLEQRGVIDQP--EHFLERMI 1491
Cdd:PRK12316 2935 ERSLSHspLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARtvERLARHWQ 3014
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1492 QLIEIALNEPETSLSHYRLQLAEEHDLI-QKTNQTQ-YYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCA 1569
Cdd:PRK12316 3015 NLLRGMVENPQRSVDELAMLDAEERGQLlEAWNATAaEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANR 3094
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQkdlaaivHPSIA 1649
Cdd:PRK12316 3095 LAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS-------HLRLP 3167
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1650 TFAFNE--LFDETKVDLSSYKTTV-ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCT 1726
Cdd:PRK12316 3168 LAQGVQvlDLDRGDENYAEANPAIrTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS 3247
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1727 FDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaateILSSAQRQSLPICRVFCSGE 1806
Cdd:PRK12316 3248 FDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAF------LEEEDAHRCTSLKRIVCGGE 3321
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1807 ALPTALAKSFTEHFSceLHNLYGPTEAAVDVSYMDATlglHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAG 1886
Cdd:PRK12316 3322 ALPADLQQQVFAGLP--LYNLYGPTEATITVTHWQCV---EEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGG 3396
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1887 HQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVV 1965
Cdd:PRK12316 3397 EGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVrEAV 3476
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1966 VHAISSEqnkanvQLVAYLQTTAPVDI--DQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEK 2043
Cdd:PRK12316 3477 VLAVDGR------QLVAYVVPEDEAGDlrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDY 3550
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2044 QYATSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPiGQLMSHVTIQRLAALLLTQERL 2123
Cdd:PRK12316 3551 VAPVNELERRLAAIWADVLKLEQ-VGLTDNFFELGGDSIISLQVVSRARQAGIRFTP-KDLFQHQTIQGLARVARVGGGV 3628
                        2170
                  ....*....|....*...
gi 490930577 2124 AeVEQ---TGMQPILPIR 2138
Cdd:PRK12316 3629 A-VDQgpvSGETLLLPIQ 3645
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1097-2338 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: 785.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1097 NSTILPLLPLQKGMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQA 1176
Cdd:COG1020    15 AAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1177 WPVQFCSVTPDL----LEQTIQEALQQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ- 1251
Cdd:COG1020    95 PVVVLLVDLEALaeaaAEAAAAAEALAPFDLLRG-PLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAa 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1252 -TNQQLPVLE------HSYETVIKALSGRDHETSKVIWQRDLADLQPLILFNQAQQAVQETSYR-------LSAELGAKL 1317
Cdd:COG1020   174 yAGAPLPLPPlpiqyaDYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRgarvsfrLPAELTAAL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1318 QHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQ 1397
Cdd:COG1020   254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRE 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1398 LHVEHLEHDGLGLSAIQQLI------AQGNLFDSLLVVENYPDNQylqQKLGDAAISKLT-NRGYSHYPLALLVIP-DHQ 1469
Cdd:COG1020   332 TLLAAYAHQDLPFERLVEELqperdlSRNPLFQVMFVLQNAPADE---LELPGLTLEPLElDSGTAKFDLTLTVVEtGDG 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1470 IELLLE-QRGVIDQP--EHFLERMIQLIEIALNEPETSLSHYRLQLAEEHD-LIQKTNQTQ-YYVRQSTLQQLLREQARI 1544
Cdd:COG1020   409 LRLTLEyNTDLFDAAtiERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQqLLAEWNATAaPYPADATLHELFEAQAAR 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1545 TPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFM 1624
Cdd:COG1020   489 TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYM 568
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1625 LQDAKSKLVIGEQKDLAAIVHPSIATFAFNELfdetkvDLSSYKTT----VITPQHPAYLIYTSGTTGQPKGVMVSHQAI 1700
Cdd:COG1020   569 LEDAGARLVLTQSALAARLPELGVPVLALDAL------ALAAEPATnppvPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL 642
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVF 1780
Cdd:COG1020   643 VNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRAL 722
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1781 ENAATEILSSAQrqslpicRVFCSGEALPTALAKSFTEHFS-CELHNLYGPTEAAVDVSYMDATLGLHPEEScVAIGYPV 1859
Cdd:COG1020   723 LDAAPEALPSLR-------LVLVGGEALPPELVRRWRARLPgARLVNLYGPTETTVDSTYYEVTPPDADGGS-VPIGRPI 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1860 WNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFT-AGQRMYRTGDIARWHADGSIQYIGRADD 1938
Cdd:COG1020   795 ANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfPGARLYRTGDLARWLPDGNLEFLGRADD 874
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1939 QLKIRGQRIELGEIEQQLRLISGL-DVVVHAIssEQNKANVQLVAYL--QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLV 2015
Cdd:COG1020   875 QVKIRGFRIELGEIEAALLQHPGVrEAVVVAR--EDAPGDKRLVAYVvpEAGAAAAAALLRLALALLLPPYMVPAAVVLL 952
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2016 EQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSAFEHELTRIFQQILNTDqnIGVNEDFFAIGGHSILVMKLAIEIRKVF 2095
Cdd:COG1020   953 LPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVV--VGDDDFFFFGGGLGLLLLLALARAARLL 1030
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2096 KRTIPIGQLMSHVTIQRLAALLLTQERLAEVEQTGMQPILPIRsgsghPLFCFYPGSGSAWQYTVLNRYLHSDLPIIGLQ 2175
Cdd:COG1020  1031 LLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLP-----PLLLSLLALLLALLLLLALLALLALLLLLLLL 1105
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2176 SPRPDGLLANSTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVAAKLTEQGEKVDylgLLDTYPAEIHQWLDLS 2255
Cdd:COG1020  1106 LLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAE---LLAAAALLLLLALLLL 1182
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2256 VEEMNAEAEQEQLQFFNDILADADSALSEETRRLQEDIFANYRDAVRLLKPYKMPHFDGELHLVVAEKDLLPYIQPEQQW 2335
Cdd:COG1020  1183 ALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLAL 1262

                  ...
gi 490930577 2336 SPL 2338
Cdd:COG1020  1263 ALA 1265
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
133-1340 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: 621.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  133 LFRQVLFTTHDKVYW-YQRYHHIMLDGFSMINLTKRIVELYQQLQEGKDLSVSP-FIGVNEVISERQAYENSHQFKIDQA 210
Cdd:COG1020   130 LLRLLLLLLLLLLLLlLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPlPIQYADYALWQREWLQGEELARQLA 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  211 FWKAYCEDLPSPISLSTHHL-AAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGI 289
Cdd:COG1020   210 YWRQQLAGLPPLLELPTDRPrPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGT 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  290 PFMRRLGSkAIRSTL-PTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSIDIHERM--YGPILN 366
Cdd:COG1020   290 PVAGRPRP-ELEGLVgFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNplFQVMFV 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  367 YKAFDQD-LVIDGEKVKTHHISTG-PIDDFEFSFIVQDHELIIELRADSQRYTQDELFNHGQRLTLLLEQALIRPEQPCS 444
Cdd:COG1020   369 LQNAPADeLELPGLTLEPLELDSGtAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLG 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  445 NFNITTPQELTALTQSGIGPRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGA 524
Cdd:COG1020   449 DLPLLTAAERQQLLAEWNATAAPYPAD-ATLHELFEAQAARTPDAVAVVFGD----QSLTYAELNARANRLAHHLRALGV 523
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  525 RKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQ-NIQQLHLDQEgvq 603
Cdd:COG1020   524 GPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPElGVPVLALDAL--- 600
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  604 tQIRKQDASDIPAENRKfdfQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHkptiywpvleavNERFPDRP-LRAAHT 682
Cdd:COG1020   601 -ALAAEPATNPPVPVTP---DDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM------------QRRYGLGPgDRVLQF 664
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  683 HSFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLfvENQHHPSLILIGGEA 761
Cdd:COG1020   665 ASLSFDASVWEIFGALLsGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP--EALPSLRLVLVGGEA 742
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  762 APLALWQQLNAQ-PALFAHNLYGPTEYTVDT----FRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGF 836
Cdd:COG1020   743 LPPELVRRWRARlPGARLVNLYGPTETTVDStyyeVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGA 822
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  837 GIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAV 915
Cdd:COG1020   823 GLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAV 902
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  916 VIAEPINNSHRLLGYCVVkdielDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQIRAHS 995
Cdd:COG1020   903 VVAREDAPGDKRLVAYVV-----PEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA 977
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  996 RMAETPEQQLLCQITASVLKL---DAIGIDDDFFMTGGDSISAIMLCTQLRQRGYSLRPSDVFQFKTVAAMAPQLTRLDE 1072
Cdd:COG1020   978 AAAAPPAEEEEEEAALALLLLlvvVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAA 1057
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1073 QQAAVSKPLFSADLEQKVQEKYGKNSTILPLLPLQKGMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQ 1152
Cdd:COG1020  1058 AAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPR 1137
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1153 LGGHFDSELAEEPVFIYSLHPTQAWPVQfcsvtpdLLEQTIQEALQQPIHLDQPYGLIRATLIQHAPEQSELLIMVHHLL 1232
Cdd:COG1020  1138 LRLLVALAAALALAALLALLLAAAAAAA-------ELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLL 1210
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1233 TDGWSTPLFLQDFIKAYQQTNQQLPVLEHSYETVI----------KALSGRDHETSKVIWQRDLADLQPLILFNQAQQAV 1302
Cdd:COG1020  1211 LLLLLLLLLLLLLLAAAAAALLALALLLALLALAAllalaalaalAAALLALALALLALALLLLALALLLPALARARAAR 1290
                        1210      1220      1230
                  ....*....|....*....|....*....|....*...
gi 490930577 1303 QETSYRLSAELGAKLQHKLRQQGITLNVFMQMIWAMTL 1340
Cdd:COG1020  1291 TARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
1537-2031 0e+00

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: 620.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:cd17646     3 LVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKDLAAIVHPSIATFAFNELFDETKVDLssyKTTVITPQHPAYLIYTSGTTGQPKGVMVS 1696
Cdd:cd17646    83 PADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATP---PLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1697 HQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSM 1776
Cdd:cd17646   160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1777 LAVFENAATeilsSAQRQSLPicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATlGLHPEEScVAIG 1856
Cdd:cd17646   240 LRVFLAEPA----AGSCASLR--RVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVR-GPAETPS-VPIG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1857 YPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRA 1936
Cdd:cd17646   312 RPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRS 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1937 DDQLKIRGQRIELGEIEQQLR---LISGLDVVVHaissEQNKANVQLVAYLQ---TTAPVDIDQLKKQLAKHLPAYMVPT 2010
Cdd:cd17646   392 DDQVKIRGFRVEPGEIEAALAahpAVTHAVVVAR----AAPAGAARLVGYVVpaaGAAGPDTAALRAHLAERLPEYMVPA 467
                         490       500
                  ....*....|....*....|.
gi 490930577 2011 HYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd17646   468 AFVVLDALPLTANGKLDRAAL 488
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
487-986 2.13e-158

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: 497.05  E-value: 2.13e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd05930     1 PDAVAVVDGD----QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  567 QMMCEDANPLFVLTTQalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd05930    77 AYILEDSGAKLVLTDP-----------------------------------------DDLAYVIYTSGSTGKPKGVMVEH 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  647 GSLLNLILSHkptiywpvleavNERFPDRP-LRAAHTHSFSFDSSWLQVFWML-WGQELHIFDENMRRDAFGLVQEIQQR 724
Cdd:cd05930   116 RGLVNLLLWM------------QEAYPLTPgDRVLQFTSFSFDVSVWEIFGALlAGATLVVLPEEVRKDPEALADLLAEE 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  725 QIDTLDLPPSFCAQMMTNGlfvENQHHPSL--ILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVD-TF---RAELK 797
Cdd:cd05930   184 GITVLHLTPSLLRLLLQEL---ELAALPSLrlVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDaTYyrvPPDDE 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  798 QTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAG 877
Cdd:cd05930   261 EDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDG 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  878 KLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYCVVKDieldekTSEQLSQQYLSQLRQ 956
Cdd:cd05930   341 NLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEkRLVAYVVPDE------GGELDEEELRAHLAE 414
                         490       500       510
                  ....*....|....*....|....*....|
gi 490930577  957 NLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05930   415 RLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
NRPS_MxcG NF038078
myxochelin non-ribosomal peptide synthetase MxcG;
15-1079 4.50e-155

myxochelin non-ribosomal peptide synthetase MxcG;


Pssm-ID: 468336 [Multi-domain]  Cd Length: 1444  Bit Score: 521.59  E-value: 4.50e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   15 QPARFELASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELNNQVQFQ 94
Cdd:NF038078    1 QEARWPLSAAQHGIWLGQQLDLASPVYNAGECIEIRGPVDPAVFEAALRQAVGEAEALHMRFVPGEEGPRQLLDPSADWP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   95 IEEFDFCHLT-PKKAQQrlwDWMPSDrqCAKSLKAGETQLFRQVLFTTH-DKVYWYQRYHHIMLDGFSMINLTKRIVELY 172
Cdd:NF038078   81 LHRVDVSGTPdPWAAAQ---AWMRED--LARTVDLSRGPLFAEALFKAApDRFFWYQRAHHIALDGFGFSLLARRVAELY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  173 QQLQEGKDlSVSPFIGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSThhlAAKTTATFVKHQLRFSTGILEQ 252
Cdd:NF038078  156 TARVTGRP-ATGGFGSLRAVLDEDAAYRAGPQCELDRAFWMERFADRPTPVSLAE---PAPMSRSFVRQTRHLSPSEMER 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  253 IQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQ 332
Cdd:NF038078  232 LQAVARQAGLSWPDLVLAATAAWLHRRTGAPEVVLGLPVMGRLGSAALRVPCMAMNIVPLRVPVRPGAGLLALARGVAAE 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  333 LREIRPHQKYDAEQILRDLNSIDIHERMYGPILNYKAFDQDLVIDGEKVKTHHISTGPIDDFEFSFIVQD--HELIIELR 410
Cdd:NF038078  312 LRAIRPHLRYRYEQLRRDLKLVGGQRRLFGPVVNIMPFDYALRFAGMPAIAHNISAGPVEDLSIGVYARSdgRGPRVDFD 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  411 ADSQRYTQDELFNHGQRLTLLLEQALIRPEQPCSNFNITTP-------QELTALTQSGIGPRVSHPeqynnVLDIFYEQV 483
Cdd:NF038078  392 ANPACYSADELDAHQREFLQLLEALLAAPEQAVARALIPGAaapapaaSRPGSLLDGGPLPAPARP-----VLELIAERA 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  484 KKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPI 563
Cdd:NF038078  467 REQPDAIAVEHGPR----RMTYRELLLAARALAARLVAAGARPDTLVAVMLPRSIDAIVASLGVLFSGAGYLPLDPFGPS 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  564 DRMQMMCEDANPLFVLTTQALA---QQLPQNIQQLHLDQEGVQTQIRKQDASDIPAENRkfdfqdVAYVIFTSGSTGRPK 640
Cdd:NF038078  543 SRTAAILADAAPALIVTSSEHAptaKAGPQAPGALVVRRLEEAVPSPAPEAPPRPADER------LAYVIYTSGSTGQPN 616
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  641 GVMNTHGSLLNLILShkPTIYWPVleavneRFPDRPLRAAHTHsfsFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQ 719
Cdd:NF038078  617 GVQISRGALAHFVAG--ATQRYGV------RRDDRVLQFAPLH---FDASVEEIFLTLCaGARLVLRTDEMLQSVPRLLD 685
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  720 EIQQRQIDTLDLPPSF---CAQMMTNGLFVenqhHPS---LILIGGEAA-P--LALWQQlNAQPALFAHNLYGPTEYTVD 790
Cdd:NF038078  686 ACAEHGITVLDLPTAFwheLAYSVSTGAAR----LPSslrTVIIGGEAAlPerVARWRA-AVGPRVRLLNTYGPTEATVV 760
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  791 TFRAELKQTARPV-------IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVA-NPFEHGQ 862
Cdd:NF038078  761 ATVATLSGGGAAGdegdevpIGRPLPGVRAALLDAQGRLVAPGAEGELYLLGGGLARGYLGRPELDAARFTTlEALPGRP 840
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  863 RMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIAEPINNSHRLLGYCVVKDIeldEK 941
Cdd:NF038078  841 RAYRTGDLVRLREDGQLVFVGRVDDEFKISGHRIDPAEVETVLLGHPGVrEAAVVGQVLPGGTRRLCAHVVADAP---AP 917
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  942 TSEQLSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQI---RAHSRMAETPEQQLLCQITASVLKLDA 1018
Cdd:NF038078  918 SAAELRR----HLLSALPAPMVPGAFVFAERLPRTSTGKIDRAALRRAGPaeeSATSAAAATALERVVLRVWEQVLGVSG 993
                        1050      1060      1070      1080      1090      1100
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1019 IGIDDDFFMTGGDSISAIMLCTQLR-QRGYSLRPSDVFQFKTVAAMAPQLtrldEQQAAVSK 1079
Cdd:NF038078  994 LSAQDDFFELGGQSLQSIQVANRLGvALGREVPVATVFRHPTAAGLAQAL----EHGASVAA 1051
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1569-1966 1.63e-138

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: 439.39  E-value: 1.63e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1569 ALAQQLQ-RAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQK--DLAAIVH 1645
Cdd:TIGR01733   11 RLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSAlaSRLAGLV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1646 PSIATFAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPC 1725
Cdd:TIGR01733   91 LPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASL 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1726 TFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLS-LIQKYQVTTLHFVPSMLAVfenaateiLSSAQRQSLPICR-VFC 1803
Cdd:TIGR01733  171 SFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaLIAEHPVTVLNLTPSLLAL--------LAAALPPALASLRlVIL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1804 SGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGEL 1882
Cdd:TIGR01733  243 GGEALTPALVDRWRARGpGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGEL 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1883 YLAGHQLAMGYLHRADLTASRFVANPF--TAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLIS 1960
Cdd:TIGR01733  323 YIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHP 402

                   ....*.
gi 490930577  1961 GLDVVV 1966
Cdd:TIGR01733  403 GVREAV 408
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
504-916 8.48e-115

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: 371.21  E-value: 8.48e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   504 SFAELAVKVNQLTRFLQEN-GARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQ 582
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   583 ALAQQLPQnIQQLHLDQEGVQTQIRkQDASDIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHkptiyw 662
Cdd:TIGR01733   81 ALASRLAG-LVLPVILLDPLELAAL-DDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL------ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   663 pvleavNERFPDRPL-RAAHTHSFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQE-IQQRQIDTLDLPPSFcAQM 739
Cdd:TIGR01733  153 ------ARRYGLDPDdRVLQFASLSFDASVEEIFGALLaGATLVVPPEDEERDDAALLAAlIAEHPVTVLNLTPSL-LAL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   740 MTNGLfVENQHHPSLILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVDTF-----RAELKQTARPVIGNPIGNTQA 813
Cdd:TIGR01733  226 LAAAL-PPALASLRLVILGGEALTPALVDRWRARgPGARLINLYGPTETTVWSTatlvdPDDAPRESPVPIGRPLANTRL 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   814 YVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF--EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKI 891
Cdd:TIGR01733  305 YVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI 384
                          410       420
                   ....*....|....*....|....*
gi 490930577   892 RGYRVEIGEVENALSILTNVESAVV 916
Cdd:TIGR01733  385 RGYRIELGEIEAALLRHPGVREAVV 409
AMP-binding pfam00501
AMP-binding enzyme;
1538-1943 1.47e-111

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 362.40  E-value: 1.47e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1538 LREQARITPEQTALS-DENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:pfam00501    1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1617 PTERIKFMLQDAKSKLVIGEQKDLAAIVHP--------------SIATFAFNELFDETKVDLSSYKTTVITPQ--HPAYL 1680
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEalgklevvklvlvlDRDPVLKEEPLPEEAKPADVPPPPPPPPDpdDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1681 IYTSGTTGQPKGVMVSHQAIVNRILWMQSEYP----LSATDTILQKTPCTFDVSV-WEFFWSYLVGARLVIAPIDAHRDP 1755
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1756 LALLSLIQKYQVTTLHFVPSMLAVFENAATeiLSSAQRQSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAV 1835
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGA--PKRALLSSLRL--VLSGGAPLPPELARRFRELFGGALVNGYGLTETTG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1836 DVSYMDatLGLHPEESCVAIGYPVWNTQLYILDQY-LRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVAnpftagQR 1914
Cdd:pfam00501  317 VVTTPL--PLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DG 388
                          410       420
                   ....*....|....*....|....*....
gi 490930577  1915 MYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:pfam00501  389 WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
479-892 5.65e-86

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 288.44  E-value: 5.65e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   479 FYEQVKKYPERTAIVSGERpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLD 558
Cdd:pfam00501    1 LERQAARTPDKTALEVGEG---RRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   559 LDYPIDRMQMMCEDANPLFVLTTQAL--------AQQLPQNIQQLHLDQEGVQT----QIRKQDASDIPAENRKFDFQDV 626
Cdd:pfam00501   78 PRLPAEELAYILEDSGAKVLITDDALkleelleaLGKLEVVKLVLVLDRDPVLKeeplPEEAKPADVPPPPPPPPDPDDL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   627 AYVIFTSGSTGRPKGVMNTHGSLLNLILSHKptIYWPVLEAVNERfpdrpLRAAHTHSFSFDSSWLQVFW--MLWGQELH 704
Cdd:pfam00501  158 AYIIYTSGTTGKPKGVMLTHRNLVANVLSIK--RVRPRGFGLGPD-----DRVLSTLPLFHDFGLSLGLLgpLLAGATVV 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   705 IFDENMRRDAFGLVQEIQQRQIDTLDLPPSFcAQMMTNGLFVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFAHNLY 782
Cdd:pfam00501  231 LPPGFPALDPAALLELIERYKVTVLYGVPTL-LNMLLEAGAPKRALLSSLrlVLSGGAPLPPELARRFRELFGGALVNGY 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   783 GPTEYTVDT---FRAELKQTARPVIGNPIGNTQAYVLD-RHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVAnpf 858
Cdd:pfam00501  310 GLTETTGVVttpLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE--- 386
                          410       420       430
                   ....*....|....*....|....*....|....
gi 490930577   859 ehgQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIR 892
Cdd:pfam00501  387 ---DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
2148-2265 4.86e-10

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 61.47  E-value: 4.86e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   2148 FYPGSGsAWQYTVLNRYLHSDLPIIGLQSP--RPDGLLAnsTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVA 2225
Cdd:smart00824    6 TAAPSG-PHEYARLAAALRGRRDVSALPLPgfGPGEPLP--ASADALVEAQAEAVLRAAGGRPFVLVGHSSGGLLAHAVA 82
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 490930577   2226 AKLTEQGEKVDYLGLLDTYPAE---IHQWLDLSVEEMNAEAEQ 2265
Cdd:smart00824   83 ARLEARGIPPAAVVLLDTYPPGdpaPEGWLPELLRGVFEREDS 125
 
Name Accession Description Interval E-value
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1098-2372 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 1046.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1098 STILPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQA 1176
Cdd:PRK10252    5 SQHLPLVAAQPGIWMAEKLSPLPSaWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1177 WPVQFCSVTPDLLEQT---IQEALQQPIHLDQPYGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDF--IKAYQQ 1251
Cdd:PRK10252   85 PEIIDLRTQPDPHAAAqalMQADLQQDLRVDSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIaaIYCAWL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1252 TNQQLPVLEHSYETVIKALSGRDHETSKviWQRD-------LADLQPLILFNQAQQAVQETSYR-----LSAELGAKLQH 1319
Cdd:PRK10252  165 RGEPTPASPFTPFADVVEEYQRYRASEA--WQRDaafwaeqRRQLPPPASLSPAPLPGRSASADilrlkLEFTDGAFRQL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1320 KLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGR--SAPIngleQQIGLFLNTIPVRVKLNMQQTLWE------- 1390
Cdd:PRK10252  243 AAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlgSAAL----TATGPVLNVLPLRVHIAAQETLPElatrlaa 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1391 QLPQL---QQLHVEHLEHDgLGLSAIQQliaqgNLFDSLLVVE------NYPDNQYLQQKLGDAAISKLTnrgyshypLA 1461
Cdd:PRK10252  319 QLKKMrrhQRYDAEQIVRD-SGRAAGDE-----PLFGPVLNIKvfdyqlDFPGVQAQTHTLATGPVNDLE--------LA 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1462 LLVIPDHQIELLLE---QRGVIDQPEHFLERMIQLIEIALNEPETSLSHYRLQLAEEHDLIQKTNQTQYYVRQSTLQQLL 1538
Cdd:PRK10252  385 LFPDEHGGLSIEILanpQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALV 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1539 REQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPT 1618
Cdd:PRK10252  465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1619 ERIKFMLQDAKSKLVIGEQKDLAAIVH-PSIATFAFNELF---DETKVDLSSykttvitPQHPAYLIYTSGTTGQPKGVM 1694
Cdd:PRK10252  545 DRLKMMLEDARPSLLITTADQLPRFADvPDLTSLCYNAPLapqGAAPLQLSQ-------PHHTAYIIFTSGSTGRPKGVM 617
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVP 1774
Cdd:PRK10252  618 VGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVP 697
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1775 SMLAVFENAATEilSSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATlglhPEE---- 1850
Cdd:PRK10252  698 SMLAAFVASLTP--EGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAF----GEElaav 771
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1851 --SCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADG 1928
Cdd:PRK10252  772 rgSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDG 851
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1929 SIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD-VVVHAISSEQNKANV----QLVAYL--QTTAPVDIDQLKKQLAK 2001
Cdd:PRK10252  852 AVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEqAVTHACVINQAAATGgdarQLVGYLvsQSGLPLDTSALQAQLRE 931
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2002 HLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTpSNTEKQYATSAFEHELTRIFQQILNTDQNiGVNEDFFAIGGHS 2081
Cdd:PRK10252  932 RLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELK-AQVPGRAPKTGTETIIAAAFSSLLGCDVV-DADADFFALGGHS 1009
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2082 ILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQErlAEVEQTGMQPILPIRSGSGHPLFCFYPGSGSAWQYTVL 2161
Cdd:PRK10252 1010 LLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEE--DESRRLGFGTILPLREGDGPTLFCFHPASGFAWQFSVL 1087
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2162 NRYLHSDLPIIGLQSPRPDGLLANSTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVAAKLTEQGEKVDYLGLL 2241
Cdd:PRK10252 1088 SRYLDPQWSIYGIQSPRPDGPMQTATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLL 1167
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2242 DTYPAEIHQWLDLSVEEMN----AEAEQEQLQFfndiLADADSALSEEtrrLQEDIFANYRDAVRLLKPYKMPHFDGELH 2317
Cdd:PRK10252 1168 DTWPPETQNWREKEANGLDpevlAEIDREREAF----LAAQQGSLSTE---LFTTIEGNYADAVRLLTTAHSVPFDGKAT 1240
                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 2318 LVVAEKDLLPYIQPEQQWSPLVKKLNIVRLSEAdHTDILSPQQLETLGPILNRMI 2372
Cdd:PRK10252 1241 LFVAERTLQEGMSPEQAWSPWIAELDVYRQDCA-HVDIISPEAFEKIGPILRATL 1294
PRK12467 PRK12467
peptide synthase; Provisional
152-2138 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1010.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  152 HHIMLDGFSMINLTKRIVELYQQLQEGKDLSVS--PFIGVNEVISER---QAYENSHQFkidqAFWKAYCEDLPSPISLS 226
Cdd:PRK12467  182 HHIISDGWSMRVLVEELVQLYSAYSQGREPSLPalPIQYADYAIWQRswlEAGERERQL----AYWQEQLGGEHTVLELP 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  227 THH-LAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNdMMMSLSLH-YIYKMTDKAELVNGIPFMRRLGSKAIRSTL 304
Cdd:PRK12467  258 TDRpRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLF-MVLLASFQtLLHRYSGQSDIRIGVPNANRNRVETERLIG 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  305 PTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSidihER--MYGPILNYKAFDQDLVIDGEKVK 382
Cdd:PRK12467  337 FFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQP----ERslSHSPLFQVMFNHQNTATGGRDRE 412
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  383 THHISTGPIDDFE-------FSFIVQDHELIIELRAdSQRYTQDeLFNHG--QRLTL----LLEQALIRPeqpcsnfnit 449
Cdd:PRK12467  413 GAQLPGLTVEELSwarhtaqFDLALDTYESAQGLWA-AFTYATD-LFEATtiERLAThwrnLLEAIVAEP---------- 480
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  450 tPQELTALTQSGIGPRVSHPEQYN---------NVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQ 520
Cdd:PRK12467  481 -RRRLGELPLLDAEERARELVRWNapateyapdCVHQLIEAQARQHPERPALVFGE----QVLSYAELNRQANRLAHVLI 555
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  521 ENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQL--PQNIQQLHLD 598
Cdd:PRK12467  556 AAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLpvPAGLRSLCLD 635
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  599 QEGVQTQIRKQDASDIPaenrkFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkpTIYWPVLEAVNerfpdrplR 678
Cdd:PRK12467  636 EPADLLCGYSGHNPEVA-----LDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCV---IAERLQLAADD--------S 699
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  679 AAHTHSFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLIlI 757
Cdd:PRK12467  700 MLMVSTFAFDLGVTELFGALAsGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALV-C 778
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  758 GGEAAPLAL---WQQLNAQPALFahNLYGPTEYTVDTFRAELKQTARPV----IGNPIGNTQAYVLDRHLQRCPTGVIGE 830
Cdd:PRK12467  779 GGEALQVDLlarVRALGPGARLI--NHYGPTETTVGVSTYELSDEERDFgnvpIGQPLANLGLYILDHYLNPVPVGVVGE 856
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  831 LYISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILT 909
Cdd:PRK12467  857 LYIGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQP 936
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  910 NVESAVVIAEPINNSHRLLGYCvVKDIELDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:PRK12467  937 GVREAVVLAQPGDAGLQLVAYL-VPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKP 1015
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  990 ---QIRAHSRMAETPEQQLLCQITASVLKLDAIGIDDDFFMTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMAp 1065
Cdd:PRK12467 1016 dasAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLAGFA- 1094
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1066 qlTRLDEQQAAVSKPLFSADLEQKvqekygknstiLPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALI 1144
Cdd:PRK12467 1095 --QAVAAQQQGAQPALPDVDRDQP-----------LPLSYAQERQWFLWQLEPGSAaYHIPQALRLKGPLDIEALERSFD 1161
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1145 TVLKRHPQLGGHFDSElAEEPVFIysLHPtqAWPVQFCSVTPDL-------LEQTIQEALQQPIHLDQ-PygLIRATLIQ 1216
Cdd:PRK12467 1162 ALVARHESLRTTFVQE-DGRTRQV--IHP--VGSLTLEEPLLLAadkdeaqLKVYVEAEARQPFDLEQgP--LLRVGLLR 1234
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1217 HAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAY----QQTNQQLPVLEHSYETVI----KALSGRDHETSKVIWQRDLAD 1288
Cdd:PRK12467 1235 LAADEHVLVLTLHHIVSDGWSMQVLVDELVALYaaysQGQSLQLPALPIQYADYAvwqrQWMDAGERARQLAYWKAQLGG 1314
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1289 LQPLIL--FNQAQQAVQetSYR-------LSAELGAKLQHKLRQQGITLnvFMQMI--WAMTLNIYAHREDIVFGTPVSG 1357
Cdd:PRK12467 1315 EQPVLElpTDRPRPAVQ--SHRgarlafeLPPALAEGLRALARREGVTL--FMLLLasFQTLLHRYSGQDDIRVGVPIAN 1390
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1358 RS-APINGLeqqIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLglsAIQQLI---------AQGNLFDSLL 1427
Cdd:PRK12467 1391 RNrAETEGL---IGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDL---PFEQLVealqperslSHSPLFQVMF 1464
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1428 vvenypdNQYLQQKLGDAAISKLTNRGYS------HYPLALLVIPDHQiELLLEQRGVIDQPEH-FLERM----IQLIEI 1496
Cdd:PRK12467 1465 -------NHQRDDHQAQAQLPGLSVESLSwesqtaQFDLTLDTYESSE-GLQASLTYATDLFEAsTIERLaghwLNLLQG 1536
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1497 ALNEPETSLSHYRL-QLAEEHDLIQKTNQT-QYYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQL 1574
Cdd:PRK12467 1537 LVADPERRLGELDLlDEAERRQILEGWNAThTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRL 1616
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1575 QRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIvhPSIATFAFN 1654
Cdd:PRK12467 1617 IALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL--PLPDGLRSL 1694
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1655 ELfDETKVDLSSYKTT----VITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVS 1730
Cdd:PRK12467 1695 VL-DQEDDWLEGYSDSnpavNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVS 1773
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1731 VWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEIlssaqRQSLPICRVFCSGEALPT 1810
Cdd:PRK12467 1774 VWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQV-----EHPLSLRRVVCGGEALEV 1848
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1811 ALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQL 1889
Cdd:PRK12467 1849 EALRPWLERLpDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGL 1928
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1890 AMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVH 1967
Cdd:PRK12467 1929 ARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVrEAVVI 2008
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1968 AISSEQNKanvQLVAYLQTTAP--VDID--------QLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHlt 2037
Cdd:PRK12467 2009 AQDGANGK---QLVAYVVPTDPglVDDDeaqvalraILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPD-- 2083
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2038 PSNTEKQYA--TSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPiGQLMSHVTIQRLAA 2115
Cdd:PRK12467 2084 ASELQQAYVapQSELEQRLAAIWQDVLGLEQ-VGLHDNFFELGGDSIISIQVVSRARQAGIRFTP-KDLFQHQTVQSLAA 2161
                        2090      2100
                  ....*....|....*....|....*.
gi 490930577 2116 LLLTQERLAEVEQ---TGMQPILPIR 2138
Cdd:PRK12467 2162 VAQEGDGTVSIDQgpvTGDLPLLPIQ 2187
PRK12316 PRK12316
peptide synthase; Provisional
53-2138 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 912.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   53 VDIPTFKKAIQIGLNEADTVIASY--SSDPSQPFIELNNQVQFQIEEFDFchLTPKKAQQRLWDWMPSDRQCAKSLKAGE 130
Cdd:PRK12316 1590 LDPDRFRAAWQATVDRHEILRSGFlwQDGLEQPLQVIHKQVELPFAELDW--RGREDLGQALDALAQAERQKGFDLTRAP 1667
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  131 tqLFRQVLFTT----HDKVYwyqRYHHIMLDGFSMINLTKRIVELYQ-QLQEGKDLSVSPFIGvnevISERQAYENShqf 205
Cdd:PRK12316 1668 --LLRLVLVRTgegrHHLIY---TNHHILMDGWSNAQLLGEVLQRYAgQPVAAPGGRYRDYIA----WLQRQDAAAS--- 1735
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  206 kidQAFWKAYCEDLPSPISLSTHHLAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAEL 285
Cdd:PRK12316 1736 ---EAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETV 1812
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  286 VNGipfmrrlGSKAIRST-LPTV--------NVLPVkfkVAEKDSWVSLA---QHVQEQLREIRPHQKYDAEQILRdlns 353
Cdd:PRK12316 1813 AFG-------ATVAGRPAeLPGIeqqiglfiNTLPV---IAAPRPDQSVAdwlQEVQALNLALREHEHTPLYDIQR---- 1878
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  354 idihermYGPILNYKAFDQDLVIDGEKVkTHHISTGPIDDFEFSFIVqDHE---------------LIIELRADSQRYTQ 418
Cdd:PRK12316 1879 -------WAGQGGEALFDSLLVFENYPV-AEALKQGAPAGLVFGRVS-NHEqtnypltlavtlgetLSLQYSYDRGHFDA 1949
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  419 DELFNHGQRLTLLLEQALIRPEQPCSNFNITTPQELTALTQSGIGPRVSHPEQYNnVLDIFYEQVKKYPERTAIVSGErp 498
Cdd:PRK12316 1950 AAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPG-VHQRIAEQAARAPEAIAVVFGD-- 2026
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  499 nlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFV 578
Cdd:PRK12316 2027 --QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  579 LTTQALAQQLP--QNIQQLHLDQEGvqtqirkqDASDIPAENRKFDF--QDVAYVIFTSGSTGRPKGVMNTHGSLLNLIl 654
Cdd:PRK12316 2105 LTQRHLLERLPlpAGVARLPLDRDA--------EWADYPDTAPAVQLagENLAYVIYTSGSTGLPKGVAVSHGALVAHC- 2175
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  655 shkptiywpvlEAVNERFPDRPL-RAAHTHSFSFDSSWLQVFW-MLWGQELHIFDENMRrDAFGLVQEIQQRQIDTLDLP 732
Cdd:PRK12316 2176 -----------QAAGERYELSPAdCELQFMSFSFDGAHEQWFHpLLNGARVLIRDDELW-DPEQLYDEMERHGVTILDFP 2243
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  733 PSFCAQmmtnglFVENQHH----PSL--ILIGGEAAPLALW-QQLNAQPALFAHNLYGPTEYTVDTF-----RAELKQTA 800
Cdd:PRK12316 2244 PVYLQQ------LAEHAERdgrpPAVrvYCFGGEAVPAASLrLAWEALRPVYLFNGYGPTEAVVTPLlwkcrPQDPCGAA 2317
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  801 RPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEH-GQRMYRTGDLVRWNSAGKL 879
Cdd:PRK12316 2318 YVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsGERLYRTGDLARYRADGVV 2397
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  880 EFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIeldektSEQLSQQYLSQLRQNLP 959
Cdd:PRK12316 2398 EYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDA------AEDLLAELRAWLAARLP 2471
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  960 EYMVPSALTVMSEFPRNVSGKVDKKALPKPQIRAHSRMAETPE---QQLLCQITASVLKLDAIGIDDDFFMTGGDSISAI 1036
Cdd:PRK12316 2472 AYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQeglEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLAT 2551
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1037 MLCTQLRQ-RGYSLRPSDVFQFKTVAAMApqlTRLDEQQAAVSKPLFSADLEQKvqekygknstiLPLLPLQKGMLFLSQ 1115
Cdd:PRK12316 2552 QVVSRVRQdLGLEVPLRILFERPTLAAFA---ASLESGQTSRAPVLQKVTRVQP-----------LPLSHAQQRQWFLWQ 2617
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1116 VENQS-NYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQAWPVQFCSVTPDLLEQTIQ 1194
Cdd:PRK12316 2618 LEPESaAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVA 2697
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1195 EALQQPIHLdQPYGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQ--QLPVLEHSYETVIKALSG 1272
Cdd:PRK12316 2698 EEIQRPFDL-ARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRgeQPTLPPLPLQYADYAAWQ 2776
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1273 RDHETSK------VIWQRDLADLQPLILF-------NQAQQAVQETSYRLSAELGAKLQHKLRQQGITLNVFMQMIWAMT 1339
Cdd:PRK12316 2777 RAWMDSGegarqlDYWRERLGGEQPVLELpldrprpALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVL 2856
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1340 LNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGL----SAIQQ 1415
Cdd:PRK12316 2857 LHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFeqlvEALQP 2934
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1416 LIAQGN--LFDSLLVVENYPDNQYLQQKLGDAAISKLTNRGYSHYPLALLVIPDHQIELLLEQRGVIDQP--EHFLERMI 1491
Cdd:PRK12316 2935 ERSLSHspLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARtvERLARHWQ 3014
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1492 QLIEIALNEPETSLSHYRLQLAEEHDLI-QKTNQTQ-YYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCA 1569
Cdd:PRK12316 3015 NLLRGMVENPQRSVDELAMLDAEERGQLlEAWNATAaEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANR 3094
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQkdlaaivHPSIA 1649
Cdd:PRK12316 3095 LAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS-------HLRLP 3167
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1650 TFAFNE--LFDETKVDLSSYKTTV-ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCT 1726
Cdd:PRK12316 3168 LAQGVQvlDLDRGDENYAEANPAIrTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS 3247
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1727 FDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaateILSSAQRQSLPICRVFCSGE 1806
Cdd:PRK12316 3248 FDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAF------LEEEDAHRCTSLKRIVCGGE 3321
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1807 ALPTALAKSFTEHFSceLHNLYGPTEAAVDVSYMDATlglHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAG 1886
Cdd:PRK12316 3322 ALPADLQQQVFAGLP--LYNLYGPTEATITVTHWQCV---EEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGG 3396
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1887 HQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVV 1965
Cdd:PRK12316 3397 EGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVrEAV 3476
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1966 VHAISSEqnkanvQLVAYLQTTAPVDI--DQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEK 2043
Cdd:PRK12316 3477 VLAVDGR------QLVAYVVPEDEAGDlrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDY 3550
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2044 QYATSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPiGQLMSHVTIQRLAALLLTQERL 2123
Cdd:PRK12316 3551 VAPVNELERRLAAIWADVLKLEQ-VGLTDNFFELGGDSIISLQVVSRARQAGIRFTP-KDLFQHQTIQGLARVARVGGGV 3628
                        2170
                  ....*....|....*...
gi 490930577 2124 AeVEQ---TGMQPILPIR 2138
Cdd:PRK12316 3629 A-VDQgpvSGETLLLPIQ 3645
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1097-2338 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: 785.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1097 NSTILPLLPLQKGMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQA 1176
Cdd:COG1020    15 AAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1177 WPVQFCSVTPDL----LEQTIQEALQQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ- 1251
Cdd:COG1020    95 PVVVLLVDLEALaeaaAEAAAAAEALAPFDLLRG-PLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAa 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1252 -TNQQLPVLE------HSYETVIKALSGRDHETSKVIWQRDLADLQPLILFNQAQQAVQETSYR-------LSAELGAKL 1317
Cdd:COG1020   174 yAGAPLPLPPlpiqyaDYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRgarvsfrLPAELTAAL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1318 QHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQ 1397
Cdd:COG1020   254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRE 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1398 LHVEHLEHDGLGLSAIQQLI------AQGNLFDSLLVVENYPDNQylqQKLGDAAISKLT-NRGYSHYPLALLVIP-DHQ 1469
Cdd:COG1020   332 TLLAAYAHQDLPFERLVEELqperdlSRNPLFQVMFVLQNAPADE---LELPGLTLEPLElDSGTAKFDLTLTVVEtGDG 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1470 IELLLE-QRGVIDQP--EHFLERMIQLIEIALNEPETSLSHYRLQLAEEHD-LIQKTNQTQ-YYVRQSTLQQLLREQARI 1544
Cdd:COG1020   409 LRLTLEyNTDLFDAAtiERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQqLLAEWNATAaPYPADATLHELFEAQAAR 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1545 TPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFM 1624
Cdd:COG1020   489 TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYM 568
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1625 LQDAKSKLVIGEQKDLAAIVHPSIATFAFNELfdetkvDLSSYKTT----VITPQHPAYLIYTSGTTGQPKGVMVSHQAI 1700
Cdd:COG1020   569 LEDAGARLVLTQSALAARLPELGVPVLALDAL------ALAAEPATnppvPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL 642
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVF 1780
Cdd:COG1020   643 VNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRAL 722
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1781 ENAATEILSSAQrqslpicRVFCSGEALPTALAKSFTEHFS-CELHNLYGPTEAAVDVSYMDATLGLHPEEScVAIGYPV 1859
Cdd:COG1020   723 LDAAPEALPSLR-------LVLVGGEALPPELVRRWRARLPgARLVNLYGPTETTVDSTYYEVTPPDADGGS-VPIGRPI 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1860 WNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFT-AGQRMYRTGDIARWHADGSIQYIGRADD 1938
Cdd:COG1020   795 ANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfPGARLYRTGDLARWLPDGNLEFLGRADD 874
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1939 QLKIRGQRIELGEIEQQLRLISGL-DVVVHAIssEQNKANVQLVAYL--QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLV 2015
Cdd:COG1020   875 QVKIRGFRIELGEIEAALLQHPGVrEAVVVAR--EDAPGDKRLVAYVvpEAGAAAAAALLRLALALLLPPYMVPAAVVLL 952
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2016 EQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSAFEHELTRIFQQILNTDqnIGVNEDFFAIGGHSILVMKLAIEIRKVF 2095
Cdd:COG1020   953 LPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVV--VGDDDFFFFGGGLGLLLLLALARAARLL 1030
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2096 KRTIPIGQLMSHVTIQRLAALLLTQERLAEVEQTGMQPILPIRsgsghPLFCFYPGSGSAWQYTVLNRYLHSDLPIIGLQ 2175
Cdd:COG1020  1031 LLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLP-----PLLLSLLALLLALLLLLALLALLALLLLLLLL 1105
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2176 SPRPDGLLANSTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVAAKLTEQGEKVDylgLLDTYPAEIHQWLDLS 2255
Cdd:COG1020  1106 LLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAE---LLAAAALLLLLALLLL 1182
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2256 VEEMNAEAEQEQLQFFNDILADADSALSEETRRLQEDIFANYRDAVRLLKPYKMPHFDGELHLVVAEKDLLPYIQPEQQW 2335
Cdd:COG1020  1183 ALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLAL 1262

                  ...
gi 490930577 2336 SPL 2338
Cdd:COG1020  1263 ALA 1265
PRK05691 PRK05691
peptide synthase; Validated
152-2138 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 773.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  152 HHIMLDGFSMINLTKRIVELYQQLQEGKDLSVSPF-IGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHH- 229
Cdd:PRK05691  808 HHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLpLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHp 887
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  230 LAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPfmrrlgsKAIRSTLPT--- 306
Cdd:PRK05691  888 RSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVP-------NANRPRLETqgl 960
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  307 ----VNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSidihERMYGP---ILNYKAFDQDLV---- 375
Cdd:PRK05691  961 vgffINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQ----AREQGLfqvMFNHQQRDLSALrrlp 1036
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  376 -IDGEKVKTHhistgpidDFEFSFIVQ-----DHELIIELRADsqrYTqDELFNH------GQRLTLLLEQALIRPEQPC 443
Cdd:PRK05691 1037 gLLAEELPWH--------SREAKFDLQlhseeDRNGRLTLSFD---YA-AELFDAatierlAEHFLALLEQVCEDPQRAL 1104
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  444 SNFNITTPQELTALTQSGIGP----RVSHPEQYNnvldifyEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFL 519
Cdd:PRK05691 1105 GDVQLLDAAERAQLAQWGQAPcapaQAWLPELLN-------EQARQTPERIALVWDG----GSLDYAELHAQANRLAHYL 1173
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  520 QENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQ-------NI 592
Cdd:PRK05691 1174 RDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQaegvsaiAL 1253
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  593 QQLHLDQEGVQtqirkqdasdipAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIywpvleAVNERf 672
Cdd:PRK05691 1254 DSLHLDSWPSQ------------APGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATY------ALDDS- 1314
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  673 pDRPLRAAhthSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFCaQMMTNGLFVENQHH 751
Cdd:PRK05691 1315 -DVLMQKA---PISFDVSVWECFWpLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLL-QLFIDEPLAAACTS 1389
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  752 PSLILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVDT--FRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVI 828
Cdd:PRK05691 1390 LRRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAINVthWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVA 1469
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  829 GELYISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSI 907
Cdd:PRK05691 1470 GELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA 1549
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  908 LTNVESAVVIAEPINNSHRLLGYCVVkdieldEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:PRK05691 1550 QPGVAQAAVLVREGAAGAQLVGYYTG------EAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALP 1623
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  988 KPQIRAHSRMA-ETPEQQLLCQITASVLKLDAIGIDDDFFMTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMAP 1065
Cdd:PRK05691 1624 EPVWQQREHVEpRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFEASELGAFAE 1703
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1066 QLTRLDEQQAAVSK-PLFSADLEQKVqekygknstilPLLPLQKGMLFLSQVENQS-NYNAFTRLSLNGDIDPVRLQQAL 1143
Cdd:PRK05691 1704 QVARIQAAGERNSQgAIARVDRSQPV-----------PLSYSQQRMWFLWQMEPDSpAYNVGGMARLSGVLDVDRFEAAL 1772
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1144 ITVLKRHPQLGGHFDSElaeEPVFIYSLHPTQAWPVQ---FCSVTPDLLEQTIQEALQQPIHldQPYGL-----IRATLI 1215
Cdd:PRK05691 1773 QALILRHETLRTTFPSV---DGVPVQQVAEDSGLRMDwqdFSALPADARQQRLQQLADSEAH--QPFDLergplLRACLV 1847
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1216 QHAPEQSELLIMVHHLLTDGWSTPLFLQD-------FIKAYQQTNQQLPVLEHSYETVIKA-LSGRDHETSKVIWQRDLA 1287
Cdd:PRK05691 1848 KAAEREHYFVLTLHHIVTEGWAMDIFARElgalyeaFLDDRESPLEPLPVQYLDYSVWQRQwLESGERQRQLDYWKAQLG 1927
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1288 DLQPLILF--NQAQQAVQETS---YR--LSAELGAKLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSA 1360
Cdd:PRK05691 1928 NEHPLLELpaDRPRPPVQSHRgelYRfdLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIR 2007
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1361 PINglEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLG----LSAIQ--QLIAQGNLFDSLLVVENYPD 1434
Cdd:PRK05691 2008 PES--EGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPfdhlVEALQppRSAAYNPLFQVMCNVQRWEF 2085
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1435 NQylQQKLGDAAISKLTNRGYS-HYPLALLVIP-DHQIELLLE-QRGVIDQP------EHFLermiQLIEIALNEPETSL 1505
Cdd:PRK05691 2086 QQ--SRQLAGMTVEYLVNDARAtKFDLNLEVTDlDGRLGCCLTySRDLFDEPriarmaEHWQ----NLLEALLGDPQQRL 2159
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1506 SHY-RLQLAEEHDLIQKTNQTQY-YVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGD 1583
Cdd:PRK05691 2160 AELpLLAAAEQQQLLDSLAGEAGeARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQV 2239
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1584 IVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAI--VHPSIATFAfnelFDETK 1661
Cdd:PRK05691 2240 RVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALgeLPAGVARWC----LEDDA 2315
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1662 VDLSSYKTT----VITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWS 1737
Cdd:PRK05691 2316 AALAAYSDAplpfLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVP 2395
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1738 YLVGARLVIAPiDAHRDPLALLSLIQKYQVTTLHFVPSmlavFENAATEILSSaQRQSLPICRVFCSGEALPTALAKSFT 1817
Cdd:PRK05691 2396 LLCGARVVLRA-QGQWGAEEICQLIREQQVSILGFTPS----YGSQLAQWLAG-QGEQLPVRMCITGGEALTGEHLQRIR 2469
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1818 EHFSCEL-HNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHR 1896
Cdd:PRK05691 2470 QAFAPQLfFNAYGPTETVVMPLACLAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDR 2549
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1897 ADLTASRFVANPFTA-GQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQN 1974
Cdd:PRK05691 2550 PGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVrEAVVLALDTPSG 2629
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1975 KanvQLVAYLQT-TAPVDIDQ-------LKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYA 2046
Cdd:PRK05691 2630 K---QLAGYLVSaVAGQDDEAqaalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAP 2706
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2047 TSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPiGQLMSHVTIQRLAAlLLTQERLAEV 2126
Cdd:PRK05691 2707 RSELEQQLAQIWREVLNVER-VGLGDNFFELGGDSILSIQVVSRARQLGIHFSP-RDLFQHQTVQTLAA-VATHSEAAQA 2783
                        2090
                  ....*....|....*
gi 490930577 2127 EQ---TGMQPILPIR 2138
Cdd:PRK05691 2784 EQgplQGASGLTPIQ 2798
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
17-1073 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 727.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   17 ARFELASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELNNQVQFQIE 96
Cdd:PRK10252    6 QHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   97 EF-DFCHLTPKKAQQRlwDWMPSDRQCAKSLKAGETqLFRQVLFTTHDK-VYWYQRYHHIMLDGFSMINLTKRIVELYQQ 174
Cdd:PRK10252   86 EIiDLRTQPDPHAAAQ--ALMQADLQQDLRVDSGKP-LVFHQLIQLGDNrWYWYQRYHHLLVDGFSFPAITRRIAAIYCA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  175 LQEGKDLSVSPFIGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHHLAAKTTAT-FVKHQLRFSTGILEQI 253
Cdd:PRK10252  163 WLRGEPTPASPFTPFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASAdILRLKLEFTDGAFRQL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  254 QALAAQTKLAlnDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQL 333
Cdd:PRK10252  243 AAQASGVQRP--DLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  334 REIRPHQKYDAEQILRDLNSIDIHERMYGPILNYKAFDQDLVIDGEKVKTHHISTGPIDDFEFS-FIVQDHELIIELRAD 412
Cdd:PRK10252  321 KKMRRHQRYDAEQIVRDSGRAAGDEPLFGPVLNIKVFDYQLDFPGVQAQTHTLATGPVNDLELAlFPDEHGGLSIEILAN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  413 SQRYTQDELFNHGQRLTLLLEQALIRPEQPCSNFNITTPQELTALTQsgiGPRVSHPEQYNNVLDIFYEQVKKYPERTAI 492
Cdd:PRK10252  401 PQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQ---VNATAVEIPETTLSALVAQQAAKTPDAPAL 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  493 VSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCED 572
Cdd:PRK10252  478 ADAR----YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLED 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  573 ANPLFVLTTQALAQQLPqniqqlHLDQEGVQTQIRKQDASDIPAENRKFDfQDVAYVIFTSGSTGRPKGVMNTHGSLLNL 652
Cdd:PRK10252  554 ARPSLLITTADQLPRFA------DVPDLTSLCYNAPLAPQGAAPLQLSQP-HHTAYIIFTSGSTGRPKGVMVGQTAIVNR 626
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  653 ILshkptiyWpvleaVNERFPDRPL-RAAHTHSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAFGLVQEIQQRQIDTLD 730
Cdd:PRK10252  627 LL-------W-----MQNHYPLTADdVVLQKTPCSFDVSVWEFFWpFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTH 694
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  731 LPPSFCAQMMtNGLFVENQHHPSLIL----IGGEAAPLAL---WQQLNAQPAlfaHNLYGPTEYTVD-----TFRAELKQ 798
Cdd:PRK10252  695 FVPSMLAAFV-ASLTPEGARQSCASLrqvfCSGEALPADLcreWQQLTGAPL---HNLYGPTEAAVDvswypAFGEELAA 770
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  799 -TARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSA 876
Cdd:PRK10252  771 vRGSSVpIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDD 850
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  877 GKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINN-------SHRLLGYCVVKDIE-LDektSEQLsq 948
Cdd:PRK10252  851 GAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQaaatggdARQLVGYLVSQSGLpLD---TSAL-- 925
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  949 qyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQI--RAHSRMAETPEQQLLCQITASVLKLDAIGIDDDFF 1026
Cdd:PRK10252  926 --QAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELkaQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFF 1003
                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*...
gi 490930577 1027 MTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMApqlTRLDEQ 1073
Cdd:PRK10252 1004 ALGGHSLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLA---TLLDAE 1048
PRK12467 PRK12467
peptide synthase; Provisional
1039-2245 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 722.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1039 CTQLRQRGYSlrPSDvfqFKTVAAMAPQLTRLdeqqaavskPLFSADLEQkvqekygknstILPLLPLQKGMLFLSQVEN 1118
Cdd:PRK12467 2610 CCSNDQRGVT--PSD---FPLAGLSQEQLDRL---------PVAVGDIED-----------IYPLSPMQQGMLFHTLYEG 2664
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1119 QS-NYNAFTRLSLNGdIDPVRLQQALITVLKRHPQLGGHF--DSELaEEPVFIysLHPTQAWPVQFC-----SVTPDLLE 1190
Cdd:PRK12467 2665 GAgDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFlwDGEL-EEPLQV--VYKQARLPFSRLdwrdrADLEQALD 2740
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1191 QTIQEALQQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYqqTNQQLPVLEHSYETVIKAL 1270
Cdd:PRK12467 2741 ALAAADRQQGFDLLSA-PLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRY--FGQPPPAREGRYRDYIAWL 2817
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1271 SGRDHETSKVIWQRDLADLQPLILFNQAQQ-------AVQETSYR-LSAELGAKLQHKLRQQGITLNVFMQMIWAMTLNI 1342
Cdd:PRK12467 2818 QAQDAEASEAFWKEQLAALEEPTRLARALYpapaeavAGHGAHYLhLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQR 2897
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1343 YAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGLSAIQQLIAQGN- 1421
Cdd:PRK12467 2898 FTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGe 2977
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1422 -LFDSLLVVENYPDNQYLQQKL-GDAAISKLTNRGYSHYPLALLVIPDHQIEL-LLEQRGVIDQP--EHFLERMIQLIEI 1496
Cdd:PRK12467 2978 aLFDSILVFENYPISEALKQGApSGLRFGAVSSREQTNYPLTLAVGLGDTLELeFSYDRQHFDAAaiERLAESFDRLLQA 3057
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1497 ALNEPETSLSHYRLQLAEEHDLI--QKTNQTQYYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQL 1574
Cdd:PRK12467 3058 MLNNPAARLGELPTLAAHERRQVlhAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRL 3137
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1575 QRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHPsiatfAFN 1654
Cdd:PRK12467 3138 IAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAP-----AGD 3212
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1655 ELFDETKVDLSSYK----TTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVS 1730
Cdd:PRK12467 3213 TALTLDRLDLNGYSennpSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGA 3292
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1731 VWEFFWSYLVGARLVIAPIDaHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaateiLSSAQRQSL-PICRVFCSGEALP 1809
Cdd:PRK12467 3293 QERFLWTLICGGCLVVRDND-LWDPEELWQAIHAHRISIACFPPAYLQQF-------AEDAGGADCaSLDIYVFGGEAVP 3364
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1810 -TALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQ 1888
Cdd:PRK12467 3365 pAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVG 3444
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1889 LAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVV 1966
Cdd:PRK12467 3445 LARGYHQRPSLTAERFVADPFsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVrEAVV 3524
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1967 HAISSEQNKanvQLVAYLQTTAPVD--IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNtEKQ 2044
Cdd:PRK12467 3525 LARDGAGGK---QLVAYVVPADPQGdwRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSR-EYV 3600
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2045 YATSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLltqerla 2124
Cdd:PRK12467 3601 APRSEVEQQLAAIWADVLGVEQ-VGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS------- 3672
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2125 EVEQTGMQPILPI--RSGSGHPLFCFYPGSGSAWQYTVLNRYLHSDLPIIGLQSPR--PDGllANSTDMDELVEKQLEIM 2200
Cdd:PRK12467 3673 PLGDVPVNLLLDLnrLETGFPALFCRHEGLGTVFDYEPLAVILEGDRHVLGLTCRHllDDG--WQDTSLQAMAVQYADYI 3750
                        1210      1220      1230      1240
                  ....*....|....*....|....*....|....*....|....*
gi 490930577 2201 RKQQPTGPYTLLGYSLGGTVAYAVAAKLTEQGEKVDYLGLLDTYP 2245
Cdd:PRK12467 3751 LWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDNTL 3795
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
133-1340 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: 621.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  133 LFRQVLFTTHDKVYW-YQRYHHIMLDGFSMINLTKRIVELYQQLQEGKDLSVSP-FIGVNEVISERQAYENSHQFKIDQA 210
Cdd:COG1020   130 LLRLLLLLLLLLLLLlLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPlPIQYADYALWQREWLQGEELARQLA 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  211 FWKAYCEDLPSPISLSTHHL-AAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGI 289
Cdd:COG1020   210 YWRQQLAGLPPLLELPTDRPrPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGT 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  290 PFMRRLGSkAIRSTL-PTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSIDIHERM--YGPILN 366
Cdd:COG1020   290 PVAGRPRP-ELEGLVgFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNplFQVMFV 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  367 YKAFDQD-LVIDGEKVKTHHISTG-PIDDFEFSFIVQDHELIIELRADSQRYTQDELFNHGQRLTLLLEQALIRPEQPCS 444
Cdd:COG1020   369 LQNAPADeLELPGLTLEPLELDSGtAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLG 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  445 NFNITTPQELTALTQSGIGPRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGA 524
Cdd:COG1020   449 DLPLLTAAERQQLLAEWNATAAPYPAD-ATLHELFEAQAARTPDAVAVVFGD----QSLTYAELNARANRLAHHLRALGV 523
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  525 RKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQ-NIQQLHLDQEgvq 603
Cdd:COG1020   524 GPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPElGVPVLALDAL--- 600
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  604 tQIRKQDASDIPAENRKfdfQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHkptiywpvleavNERFPDRP-LRAAHT 682
Cdd:COG1020   601 -ALAAEPATNPPVPVTP---DDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM------------QRRYGLGPgDRVLQF 664
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  683 HSFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLfvENQHHPSLILIGGEA 761
Cdd:COG1020   665 ASLSFDASVWEIFGALLsGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP--EALPSLRLVLVGGEA 742
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  762 APLALWQQLNAQ-PALFAHNLYGPTEYTVDT----FRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGF 836
Cdd:COG1020   743 LPPELVRRWRARlPGARLVNLYGPTETTVDStyyeVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGA 822
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  837 GIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAV 915
Cdd:COG1020   823 GLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAV 902
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  916 VIAEPINNSHRLLGYCVVkdielDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQIRAHS 995
Cdd:COG1020   903 VVAREDAPGDKRLVAYVV-----PEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA 977
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  996 RMAETPEQQLLCQITASVLKL---DAIGIDDDFFMTGGDSISAIMLCTQLRQRGYSLRPSDVFQFKTVAAMAPQLTRLDE 1072
Cdd:COG1020   978 AAAAPPAEEEEEEAALALLLLlvvVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAA 1057
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1073 QQAAVSKPLFSADLEQKVQEKYGKNSTILPLLPLQKGMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQ 1152
Cdd:COG1020  1058 AAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPR 1137
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1153 LGGHFDSELAEEPVFIYSLHPTQAWPVQfcsvtpdLLEQTIQEALQQPIHLDQPYGLIRATLIQHAPEQSELLIMVHHLL 1232
Cdd:COG1020  1138 LRLLVALAAALALAALLALLLAAAAAAA-------ELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLL 1210
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1233 TDGWSTPLFLQDFIKAYQQTNQQLPVLEHSYETVI----------KALSGRDHETSKVIWQRDLADLQPLILFNQAQQAV 1302
Cdd:COG1020  1211 LLLLLLLLLLLLLLAAAAAALLALALLLALLALAAllalaalaalAAALLALALALLALALLLLALALLLPALARARAAR 1290
                        1210      1220      1230
                  ....*....|....*....|....*....|....*...
gi 490930577 1303 QETSYRLSAELGAKLQHKLRQQGITLNVFMQMIWAMTL 1340
Cdd:COG1020  1291 TARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
1537-2031 0e+00

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: 620.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:cd17646     3 LVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKDLAAIVHPSIATFAFNELFDETKVDLssyKTTVITPQHPAYLIYTSGTTGQPKGVMVS 1696
Cdd:cd17646    83 PADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATP---PLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1697 HQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSM 1776
Cdd:cd17646   160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1777 LAVFENAATeilsSAQRQSLPicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATlGLHPEEScVAIG 1856
Cdd:cd17646   240 LRVFLAEPA----AGSCASLR--RVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVR-GPAETPS-VPIG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1857 YPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRA 1936
Cdd:cd17646   312 RPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRS 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1937 DDQLKIRGQRIELGEIEQQLR---LISGLDVVVHaissEQNKANVQLVAYLQ---TTAPVDIDQLKKQLAKHLPAYMVPT 2010
Cdd:cd17646   392 DDQVKIRGFRVEPGEIEAALAahpAVTHAVVVAR----AAPAGAARLVGYVVpaaGAAGPDTAALRAHLAERLPEYMVPA 467
                         490       500
                  ....*....|....*....|.
gi 490930577 2011 HYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd17646   468 AFVVLDALPLTANGKLDRAAL 488
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
1546-2031 0e+00

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: 594.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIGEqkdlaaivhpsiatfafnelfdetkvdlssykttvitPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd05930    81 EDSGAKLVLTD-------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAAT 1785
Cdd:cd05930   124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1786 EILSSAQRqslpicRVFCSGEALPTALAKSFTEHFS-CELHNLYGPTEAAVDVSYMDATLGlHPEESCVAIGYPVWNTQL 1864
Cdd:cd05930   204 LAALPSLR------LVLVGGEALPPDLVRRWRELLPgARLVNLYGPTEATVDATYYRVPPD-DEEDGRVPIGRPIPNTRV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:cd05930   277 YVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRG 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1945 QRIELGEIEQQLRLISGL-DVVVHAIssEQNKANVQLVAY--LQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLS 2021
Cdd:cd05930   357 YRIELGEIEAALLAHPGVrEAAVVAR--EDGDGEKRLVAYvvPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLT 434
                         490
                  ....*....|
gi 490930577 2022 HNGKLDRKAL 2031
Cdd:cd05930   435 PNGKVDRKAL 444
PRK12316 PRK12316
peptide synthase; Provisional
1039-2120 8.75e-178

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 611.19  E-value: 8.75e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1039 CTQLRQRGysLRPSDVfqfktvaamapQLTRLDEQQAAvSKPLFSADLEQkvqekygknstILPLLPLQKGMLFLSQVEN 1118
Cdd:PRK12316 4066 CCDAERHG--VTPSDF-----------PLAGLDQARLD-ALPLPLGEIED-----------IYPLSPMQQGMLFHSLYEQ 4120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1119 QS-NYNAFTRLSLNGdIDPVRLQQALITVLKRHPQLGGHFDSELA-EEPVFIYSLHPTQAWPVQFCSVTPDL---LEQTI 1193
Cdd:PRK12316 4121 EAgDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGElGRPLQVVHKQVSLPFAELDWRGRADLqaaLDALA 4199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1194 QEALQQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYqqTNQQLPVLEHSYETVIKALSGR 1273
Cdd:PRK12316 4200 AAERERGFDLQRA-PLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY--SGRPPAQPGGRYRDYIAWLQRQ 4276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1274 DHETSKVIWQRDLADLQ-PLILFNQAQQA-------VQETSYRLSAELGAKLQHKLRQQGITLNVFMQMIWAMTLNIYAH 1345
Cdd:PRK12316 4277 DAAASEAFWREQLAALDePTRLAQAIARAdlrsangYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTG 4356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1346 REDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGLSAIQQLIAQGN--LF 1423
Cdd:PRK12316 4357 QDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGeaLF 4436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1424 DSLLVVENYPDNQYLQQKL-GDAAISKLTNRGYSHYPLALLVIPDHQIELLLE-QRGVIDQP--EHFLERMIQLIEIALN 1499
Cdd:PRK12316 4437 DSLLVFENYPVSEALQQGApGGLRFGEVTNHEQTNYPLTLAVGLGETLSLQFSyDRGHFDAAtiERLARHLTNLLEAMAE 4516
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1500 EPETSLSHYR-LQLAEEHDLIQKTNQTQY-YVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRA 1577
Cdd:PRK12316 4517 DPQRRLGELQlLEKAEQQRIVALWNRTDAgYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIAR 4596
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1578 GVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHPS-IATFAFNEl 1656
Cdd:PRK12316 4597 GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDgLASLALDR- 4675
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1657 fDETKVDLSSYKTTV-ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFF 1735
Cdd:PRK12316 4676 -DEDWEGFPAHDPAVrLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLY 4754
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1736 WSYLVGARLVIAPIDAHrDPLALLSLIQKYQVTTLHFVPSMLAVFENAAteilsSAQRQSLPICRVFCSGEAL-PTALAK 1814
Cdd:PRK12316 4755 HPLINGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLAEHA-----ERDGEPPSLRVYCFGGEAVaQASYDL 4828
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1815 SFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYL 1894
Cdd:PRK12316 4829 AWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYL 4908
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1895 HRADLTASRFVANPFTA-GQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRlisGLDVVVHAISSEQ 1973
Cdd:PRK12316 4909 ERPALTAERFVPDPFGApGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLR---EHPAVREAVVIAQ 4985
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1974 NKA-NVQLVAYL--QTTAPVDI--------DQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPhlTPSNTE 2042
Cdd:PRK12316 4986 EGAvGKQLVGYVvpQDPALADAdeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQP--DASLLQ 5063
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2043 KQYAT--SAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQ 2120
Cdd:PRK12316 5064 QAYVAprSELEQQVAAIWAEVLQLER-VGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAA 5142
PRK12316 PRK12316
peptide synthase; Provisional
1039-2135 1.37e-176

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 607.34  E-value: 1.37e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1039 CTQLRQRGYSlrPSDVfqfktvaamapQLTRLDEQQAAvSKPLFSADLEQkvqekygknstILPLLPLQKGMLFLSQVEN 1118
Cdd:PRK12316 1520 CCDERNRGVT--PSDF-----------PLAGLSQAQLD-ALPLPAGEIAD-----------IYPLSPMQQGMLFHSLYEQ 1574
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1119 QS-NYNAFTRLSLNGdIDPVRLQQALITVLKRHPQL--GGHFDSELaEEPVFIysLHPTQAWPvqfCSVTPDLLEQTIQE 1195
Cdd:PRK12316 1575 EAgDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILrsGFLWQDGL-EQPLQV--IHKQVELP---FAELDWRGREDLGQ 1647
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1196 ALQQPIHLDQPYG-------LIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYqqTNQQLPVLEHSYETVIK 1268
Cdd:PRK12316 1648 ALDALAQAERQKGfdltrapLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRY--AGQPVAAPGGRYRDYIA 1725
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1269 ALSGRDHETSKVIWQRDLADLQ-PLILFNQAQQAVQETSY-----RLSAELGAKLQHKLRQQGITLNVFMQMIWAMTLNI 1342
Cdd:PRK12316 1726 WLQRQDAAASEAFWKEQLAALEePTRLAQAARTEDGQVGYgdhqqLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQR 1805
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1343 YAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGLSAIQQLIAQGN- 1421
Cdd:PRK12316 1806 YTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGe 1885
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1422 -LFDSLLVVENYPDNQYLQQKL-GDAAISKLTNRGYSHYPLALLVIPDHQIELLLE-QRGVID--QPEHFLERMIQLIEI 1496
Cdd:PRK12316 1886 aLFDSLLVFENYPVAEALKQGApAGLVFGRVSNHEQTNYPLTLAVTLGETLSLQYSyDRGHFDaaAIERLDRHLLHLLEQ 1965
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1497 ALNEPETSLSHYRLQLAEEHDLIQK--TNQTQYYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQL 1574
Cdd:PRK12316 1966 MAEDAQAALGELALLDAGERQRILAdwDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRL 2045
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1575 QRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHP-SIATFAF 1653
Cdd:PRK12316 2046 RARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPaGVARLPL 2125
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1654 nelfdETKVDLSSYKTTV----ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDV 1729
Cdd:PRK12316 2126 -----DRDAEWADYPDTApavqLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDG 2200
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1730 SVWEFFWSYLVGARLVIAPiDAHRDPLALLSLIQKYQVTTLHFVPSMLAVF-ENAATEilssaqRQSLPICRVFCSGEAL 1808
Cdd:PRK12316 2201 AHEQWFHPLLNGARVLIRD-DELWDPEQLYDEMERHGVTILDFPPVYLQQLaEHAERD------GRPPAVRVYCFGGEAV 2273
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1809 PTALAKSFTEHFSCE-LHNLYGPTEAAVDVSYMDAtlglHPEESC----VAIGYPVWNTQLYILDQYLRPVPVGVDGELY 1883
Cdd:PRK12316 2274 PAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKC----RPQDPCgaayVPIGRALGNRRAYILDADLNLLAPGMAGELY 2349
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1884 LAGHQLAMGYLHRADLTASRFVANPFTA-GQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL 1962
Cdd:PRK12316 2350 LGGEGLARGYLNRPGLTAERFVPDPFSAsGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAV 2429
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1963 -DVVVHAISSEQNKanvQLVAYL--QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPS 2039
Cdd:PRK12316 2430 rEAVVVAQDGASGK---QLVAYVvpDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQL 2506
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2040 NTEKQYATSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLT 2119
Cdd:PRK12316 2507 RQAYVAPQEGLEQRLAAIWQAVLKVEQ-VGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLES 2585
                        1130
                  ....*....|....*....
gi 490930577 2120 QER---LAEVEQTGMQPIL 2135
Cdd:PRK12316 2586 GQTsraPVLQKVTRVQPLP 2604
PRK05691 PRK05691
peptide synthase; Validated
487-2145 2.42e-175

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 603.31  E-value: 2.42e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAI--VSGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAgAIPRSIDSVVVMLSVLNSGASFLPLdldYP-- 562
Cdd:PRK05691   23 PDRLALrfLADDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVL-LFPSGPDYVAAFFGCLYAGVIAVPA---YPpe 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  563 ------IDRMQMMCEDANPLFVLTTQALAQQLpQNIQQLHLDQEGVQTQIRKQDASdiPAEN-RKFDFQ--DVAYVIFTS 633
Cdd:PRK05691   99 sarrhhQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPELLCVDTLDPA--LAEAwQEPALQpdDIAFLQYTS 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  634 GSTGRPKGVMNTHGSLL-----------------NLILSHKP---------TIYWPVLEAV------NERFPDRPLRaah 681
Cdd:PRK05691  176 GSTALPKGVQVSHGNLVaneqlirhgfgidlnpdDVIVSWLPlyhdmgligGLLQPIFSGVpcvlmsPAYFLERPLR--- 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  682 thsfsfdssWLQVFWMLWG-------------------QELHIFDENMRRDAFGLVQEIQQrqiDTLDLppsFCAQMMTN 742
Cdd:PRK05691  253 ---------WLEAISEYGGtisggpdfayrlcservseSALERLDLSRWRVAYSGSEPIRQ---DSLER---FAEKFAAC 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  743 GlFVENQHHPS-------LILIGGE--AAPLALwqQLNAQPalFAHNLYGPTEYTVdtfraeLKQTARPVIGNPIgntqA 813
Cdd:PRK05691  318 G-FDPDSFFASyglaeatLFVSGGRrgQGIPAL--ELDAEA--LARNRAEPGTGSV------LMSCGRSQPGHAV----L 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  814 YVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVanpfEH-GQRMYRTGDLvRWNSAGKLEFMGRCDDQIKIR 892
Cdd:PRK05691  383 IVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFV----EHdGRTWLRTGDL-GFLRDGELFVTGRLKDMLIVR 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  893 GYRVEIGEVENAlsiltnVESAVviaePINNSHRLLGYCVVKD--------IELDEKTSEQLSQQYL-SQLRQNLPE--Y 961
Cdd:PRK05691  458 GHNLYPQDIEKT------VEREV----EVVRKGRVAAFAVNHQgeegigiaAEISRSVQKILPPQALiKSIRQAVAEacQ 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  962 MVPSALTVMS--EFPRNVSGKVDKKA---------------LPKPQiRAHSRMAETPEQQLLCQITA---SVLKLDAIGI 1021
Cdd:PRK05691  528 EAPSVVLLLNpgALPKTSSGKLQRSAcrlrladgsldsyalFPALQ-AVEAAQTAASGDELQARIAAiwcEQLKVEQVAA 606
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1022 DDDFFMTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMAPQLTRLDEQQAAVSKPLFSADLEQKvqekygknsti 1100
Cdd:PRK05691  607 DDHFFLLGGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAQAAIARLPRGQA----------- 675
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElaeEPVFIYSLHPTQAWPV 1179
Cdd:PRK05691  676 LPQSLAQNRLWLLWQLDPQSAaYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYER---DGVALQRIDAQGEFAL 752
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTpDLLE-------QTIQEA-LQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ 1250
Cdd:PRK05691  753 QRIDLS-DLPEaerearaAQIREEeARQPFDLEKgP--LLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYA 829
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1251 QTNQ----QLPVLEHSY----ETVIKALSGRDHETSKVIWQRDLADLQPLILFN-------QAQQAVQETSYRLSAELGA 1315
Cdd:PRK05691  830 AACQgqtaELAPLPLGYadygAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELAtdhprsaRQAHSAARYSLRVDASLSE 909
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1316 KLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRsaPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQL 1395
Cdd:PRK05691  910 ALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANR--PRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQV 987
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1396 QQLHVEHLEHDGLGLSAIQQLIAQGNLFDSLLVVENYP--DNQYLQQKLGDAAISKLTNRGYSHYPLALLVIPDHQIEL- 1472
Cdd:PRK05691  988 RQATLGAQAHQDLPFEQLVEALPQAREQGLFQVMFNHQqrDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEDRNGRLt 1067
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1473 --------LLEQRGVIDQPEHFLermiQLIEIALNEPETSLSHYRLQLAEEHDLIQKTNQTQYYVRQSTLQQLLREQARI 1544
Cdd:PRK05691 1068 lsfdyaaeLFDAATIERLAEHFL----ALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQ 1143
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1545 TPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFM 1624
Cdd:PRK05691 1144 TPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYM 1223
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1625 LQDAKSKLVIGEQKDLAAIVHPS-IATFAFNELfdetkvDLSSYKTTV----ITPQHPAYLIYTSGTTGQPKGVMVSHQA 1699
Cdd:PRK05691 1224 LADSGVELLLTQSHLLERLPQAEgVSAIALDSL------HLDSWPSQApglhLHGDNLAYVIYTSGSTGQPKGVGNTHAA 1297
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1700 IVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAV 1779
Cdd:PRK05691 1298 LAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQL 1377
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1780 F--ENAATEILSsaqrqslpICRVFCSGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGlhpEESCVAIG 1856
Cdd:PRK05691 1378 FidEPLAAACTS--------LRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVTHWQCQAE---DGERSPIG 1446
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1857 YPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGR 1935
Cdd:PRK05691 1447 RPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGR 1526
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1936 ADDQLKIRGQRIELGEIEQQLRLISGLD---VVVHaisseQNKANVQLVAYLQTTAPVDI--DQLKKQLAKHLPAYMVPT 2010
Cdd:PRK05691 1527 LDQQVKLRGFRVEPEEIQARLLAQPGVAqaaVLVR-----EGAAGAQLVGYYTGEAGQEAeaERLKAALAAELPEYMVPA 1601
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2011 HYMLVEQFPLSHNGKLDRKALPQP------HLTPSntekqyatSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILV 2084
Cdd:PRK05691 1602 QLIRLDQMPLGPSGKLDRRALPEPvwqqreHVEPR--------TELQQQIAAIWREVLGLPR-VGLRDDFFALGGHSLLA 1672
                        1770      1780      1790      1800      1810      1820
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 2085 MKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQErlAEVEQTGMQPILPIRSGSGHPL 2145
Cdd:PRK05691 1673 TQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQ--AAGERNSQGAIARVDRSQPVPL 1731
PRK12467 PRK12467
peptide synthase; Provisional
1101-2134 7.25e-171

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 589.44  E-value: 7.25e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQS-NYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElaeEPVFIYSLHPTQAWPV 1179
Cdd:PRK12467   50 IPLSYAQERQWFLWQLDPDSaAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQD---EEGFRQVIDASLSLTI 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTPD-------LLEQTIQEALQQPIHLdQPYGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQT 1252
Cdd:PRK12467  127 PLDDLANEqgraresQIEAYINEEVARPFDL-ANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAY 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1253 NQ----QLPVLEHSYETVikALSGR------DHETSKVIWQRDLADLQPLILF-----NQAQQAVQETSYRLS--AELGA 1315
Cdd:PRK12467  206 SQgrepSLPALPIQYADY--AIWQRswleagERERQLAYWQEQLGGEHTVLELptdrpRPAVPSYRGARLRVDlpQALSA 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1316 KLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSApiNGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQL 1395
Cdd:PRK12467  284 GLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNR--VETERLIGFFVNTQVLKAEVDPQASFLELLQQV 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1396 QQLHVEHLEHDGLGLSA-IQQLIAQGNLFDSLL--VVENY-PDNQYLQQKLGdAAISKLT------NRGYSHYPLALLVI 1465
Cdd:PRK12467  362 KRTALGAQAHQDLPFEQlVEALQPERSLSHSPLfqVMFNHqNTATGGRDREG-AQLPGLTveelswARHTAQFDLALDTY 440
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1466 PDHQ---IEL-----LLEQRGVIDQPEHFLErmiqLIEIALNEPETSLSHYRLQLAEEH-DLIQKTNQTQYYVRQSTLQQ 1536
Cdd:PRK12467  441 ESAQglwAAFtyatdLFEATTIERLATHWRN----LLEAIVAEPRRRLGELPLLDAEERaRELVRWNAPATEYAPDCVHQ 516
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:PRK12467  517 LIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEY 596
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKDLAAIVHP-SIATFAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMV 1695
Cdd:PRK12467  597 PQDRLAYMLDDSGVRLLLTQSHLLAQLPVPaGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAI 676
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1696 SHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPS 1775
Cdd:PRK12467  677 SHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPS 756
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 MLAVFenaateILSSAQRQSLPICRVFCSGEALPTAL-AKSFTEHFSCELHNLYGPTEAAVDVSYMDATlGLHPEESCVA 1854
Cdd:PRK12467  757 HLQAL------LQASRVALPRPQRALVCGGEALQVDLlARVRALGPGARLINHYGPTETTVGVSTYELS-DEERDFGNVP 829
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1855 IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYI 1933
Cdd:PRK12467  830 IGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYL 909
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1934 GRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEqnkANVQLVAYLQTTAPVD-------IDQLKKQLAKHLPA 2005
Cdd:PRK12467  910 GRMDHQVKIRGFRIELGEIEARLLAQPGVrEAVVLAQPGD---AGLQLVAYLVPAAVADgaehqatRDELKAQLRQVLPD 986
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2006 YMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVM 2085
Cdd:PRK12467  987 YMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVER-VGLTDNFFELGGHSLLAT 1065
                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*....
gi 490930577 2086 KLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQerlAEVEQTGMQPI 2134
Cdd:PRK12467 1066 QVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQ---QQGAQPALPDV 1111
PRK12316 PRK12316
peptide synthase; Provisional
1101-2139 7.48e-170

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 586.54  E-value: 7.48e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQAWPV 1179
Cdd:PRK12316   50 DRLSYAQQRMWFLWQLEPQSGaYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFE 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTPDLLEQTIQEALQ----QPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ--QT 1252
Cdd:PRK12316  130 DCSGLPEAEQEARLRDEAQreslQPFDLCEgP--LLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSayAT 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1253 NQ--QLPVLEHSYETVikALSGR------DHETSKVIWQRDLADLQPLILF-----NQAQQAVQETSYRLSAE--LGAKL 1317
Cdd:PRK12316  208 GAepGLPALPIQYADY--ALWQRswleagEQERQLEYWRAQLGEEHPVLELptdhpRPAVPSYRGSRYEFSIDpaLAEAL 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1318 QHKLRQQGITLnvFMQMI--WAMTLNIYAHREDIVFGTPVSGRS-APINGLeqqIGLFLNTIPVRVKLNMQQTLWEQLPQ 1394
Cdd:PRK12316  286 RGTARRQGLTL--FMLLLgaFNVLLHRYSGQTDIRVGVPIANRNrAEVEGL---IGFFVNTQVLRSVFDGRTRVATLLAG 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1395 LQQlHVehlehdgLGLSAIQQLIAQgNLFDSLLVVENYPDNQYLQQKLGD----AAISKLTnrGYSHYPLALLVIPDH-- 1468
Cdd:PRK12316  361 VKD-TV-------LGAQAHQDLPFE-RLVEALKVERSLSHSPLFQVMYNHqplvADIEALD--TVAGLEFGQLEWKSRtt 429
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1469 QIELLL---EQRGVIDQPEHF---------LERM----IQLIEIALNEPETSLSHYRLQLAEEH-DLIQKTNQT-QYYVR 1530
Cdd:PRK12316  430 QFDLTLdtyEKGGRLHAALTYatdlfeartVERMarhwQNLLRGMVENPQARVDELPMLDAEERgQLVEGWNATaAEYPL 509
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1531 QSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYL 1610
Cdd:PRK12316  510 QRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYV 589
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1611 PIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIvhpSIATFAFNELFDETKVDLSSYKT----TVITPQHPAYLIYTSGT 1686
Cdd:PRK12316  590 PLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL---PLAAGVQVLDLDRPAAWLEGYSEenpgTELNPENLAYVIYTSGS 666
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1687 TGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQ 1766
Cdd:PRK12316  667 TGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREG 746
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1767 VTTLHFVPSMLAVFENAAteilssAQRQSLPICRVFCSGEALPTALAKS-FTEHFSCELHNLYGPTEAAVDVSYMDATlg 1845
Cdd:PRK12316  747 VDTLHFVPSMLQAFLQDE------DVASCTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAAIDVTHWTCV-- 818
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1846 lhpEE--SCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIAR 1923
Cdd:PRK12316  819 ---EEggDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLAR 895
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1924 WHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEqnkanvQLVAY--LQTTAPVDIDQLKKQLA 2000
Cdd:PRK12316  896 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVrEAAVLAVDGK------QLVGYvvLESEGGDWREALKAHLA 969
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2001 KHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSAFEHELTRIFQQILNTdQNIGVNEDFFAIGGH 2080
Cdd:PRK12316  970 ASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGV-ERVGLDDNFFELGGD 1048
                        1050      1060      1070      1080      1090      1100
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 2081 SILVMKLAIEIRKVFKRTIPiGQLMSHVTIQRLaALLLTQERLAEVEQ---TGMQPILPIRS 2139
Cdd:PRK12316 1049 SIVSIQVVSRARQAGIQLSP-RDLFQHQTIRSL-ALVAKAGQATAADQgpaSGEVALAPVQR 1108
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
487-986 2.13e-158

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: 497.05  E-value: 2.13e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd05930     1 PDAVAVVDGD----QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  567 QMMCEDANPLFVLTTQalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd05930    77 AYILEDSGAKLVLTDP-----------------------------------------DDLAYVIYTSGSTGKPKGVMVEH 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  647 GSLLNLILSHkptiywpvleavNERFPDRP-LRAAHTHSFSFDSSWLQVFWML-WGQELHIFDENMRRDAFGLVQEIQQR 724
Cdd:cd05930   116 RGLVNLLLWM------------QEAYPLTPgDRVLQFTSFSFDVSVWEIFGALlAGATLVVLPEEVRKDPEALADLLAEE 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  725 QIDTLDLPPSFCAQMMTNGlfvENQHHPSL--ILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVD-TF---RAELK 797
Cdd:cd05930   184 GITVLHLTPSLLRLLLQEL---ELAALPSLrlVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDaTYyrvPPDDE 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  798 QTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAG 877
Cdd:cd05930   261 EDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDG 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  878 KLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYCVVKDieldekTSEQLSQQYLSQLRQ 956
Cdd:cd05930   341 NLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEkRLVAYVVPDE------GGELDEEELRAHLAE 414
                         490       500       510
                  ....*....|....*....|....*....|
gi 490930577  957 NLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05930   415 RLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
1546-2031 6.99e-156

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: 491.42  E-value: 6.99e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIGEQKDLAAIVHPSIATFAFNElfdETKVDLSSYKTTViTPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVLLLALA---AAAAAPAAPRTPV-SPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPsmlavfenAAT 1785
Cdd:cd12116   157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATP--------ATW 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1786 EILSSAQRQSLPICRVFCSGEALPTALAKSFTEHfSCELHNLYGPTEAAVDVSYMDATLGLHPeescVAIGYPVWNTQLY 1865
Cdd:cd12116   229 RMLLDAGWQGRAGLTALCGGEALPPDLAARLLSR-VGSLWNLYGPTETTIWSTAARVTAAAGP----IPIGRPLANTQVY 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1866 ILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:cd12116   304 VLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRG 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1945 QRIELGEIEQQLRLISGLD---VVVHaisseQNKANVQLVAY--LQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFP 2019
Cdd:cd12116   384 HRIELGEIEAALAAHPGVAqaaVVVR-----EDGGDRRLVAYvvLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALP 458
                         490
                  ....*....|..
gi 490930577 2020 LSHNGKLDRKAL 2031
Cdd:cd12116   459 LTANGKLDRKAL 470
NRPS_MxcG NF038078
myxochelin non-ribosomal peptide synthetase MxcG;
15-1079 4.50e-155

myxochelin non-ribosomal peptide synthetase MxcG;


Pssm-ID: 468336 [Multi-domain]  Cd Length: 1444  Bit Score: 521.59  E-value: 4.50e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   15 QPARFELASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELNNQVQFQ 94
Cdd:NF038078    1 QEARWPLSAAQHGIWLGQQLDLASPVYNAGECIEIRGPVDPAVFEAALRQAVGEAEALHMRFVPGEEGPRQLLDPSADWP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   95 IEEFDFCHLT-PKKAQQrlwDWMPSDrqCAKSLKAGETQLFRQVLFTTH-DKVYWYQRYHHIMLDGFSMINLTKRIVELY 172
Cdd:NF038078   81 LHRVDVSGTPdPWAAAQ---AWMRED--LARTVDLSRGPLFAEALFKAApDRFFWYQRAHHIALDGFGFSLLARRVAELY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  173 QQLQEGKDlSVSPFIGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSThhlAAKTTATFVKHQLRFSTGILEQ 252
Cdd:NF038078  156 TARVTGRP-ATGGFGSLRAVLDEDAAYRAGPQCELDRAFWMERFADRPTPVSLAE---PAPMSRSFVRQTRHLSPSEMER 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  253 IQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQ 332
Cdd:NF038078  232 LQAVARQAGLSWPDLVLAATAAWLHRRTGAPEVVLGLPVMGRLGSAALRVPCMAMNIVPLRVPVRPGAGLLALARGVAAE 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  333 LREIRPHQKYDAEQILRDLNSIDIHERMYGPILNYKAFDQDLVIDGEKVKTHHISTGPIDDFEFSFIVQD--HELIIELR 410
Cdd:NF038078  312 LRAIRPHLRYRYEQLRRDLKLVGGQRRLFGPVVNIMPFDYALRFAGMPAIAHNISAGPVEDLSIGVYARSdgRGPRVDFD 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  411 ADSQRYTQDELFNHGQRLTLLLEQALIRPEQPCSNFNITTP-------QELTALTQSGIGPRVSHPeqynnVLDIFYEQV 483
Cdd:NF038078  392 ANPACYSADELDAHQREFLQLLEALLAAPEQAVARALIPGAaapapaaSRPGSLLDGGPLPAPARP-----VLELIAERA 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  484 KKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPI 563
Cdd:NF038078  467 REQPDAIAVEHGPR----RMTYRELLLAARALAARLVAAGARPDTLVAVMLPRSIDAIVASLGVLFSGAGYLPLDPFGPS 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  564 DRMQMMCEDANPLFVLTTQALA---QQLPQNIQQLHLDQEGVQTQIRKQDASDIPAENRkfdfqdVAYVIFTSGSTGRPK 640
Cdd:NF038078  543 SRTAAILADAAPALIVTSSEHAptaKAGPQAPGALVVRRLEEAVPSPAPEAPPRPADER------LAYVIYTSGSTGQPN 616
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  641 GVMNTHGSLLNLILShkPTIYWPVleavneRFPDRPLRAAHTHsfsFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQ 719
Cdd:NF038078  617 GVQISRGALAHFVAG--ATQRYGV------RRDDRVLQFAPLH---FDASVEEIFLTLCaGARLVLRTDEMLQSVPRLLD 685
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  720 EIQQRQIDTLDLPPSF---CAQMMTNGLFVenqhHPS---LILIGGEAA-P--LALWQQlNAQPALFAHNLYGPTEYTVD 790
Cdd:NF038078  686 ACAEHGITVLDLPTAFwheLAYSVSTGAAR----LPSslrTVIIGGEAAlPerVARWRA-AVGPRVRLLNTYGPTEATVV 760
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  791 TFRAELKQTARPV-------IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVA-NPFEHGQ 862
Cdd:NF038078  761 ATVATLSGGGAAGdegdevpIGRPLPGVRAALLDAQGRLVAPGAEGELYLLGGGLARGYLGRPELDAARFTTlEALPGRP 840
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  863 RMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIAEPINNSHRLLGYCVVKDIeldEK 941
Cdd:NF038078  841 RAYRTGDLVRLREDGQLVFVGRVDDEFKISGHRIDPAEVETVLLGHPGVrEAAVVGQVLPGGTRRLCAHVVADAP---AP 917
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  942 TSEQLSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQI---RAHSRMAETPEQQLLCQITASVLKLDA 1018
Cdd:NF038078  918 SAAELRR----HLLSALPAPMVPGAFVFAERLPRTSTGKIDRAALRRAGPaeeSATSAAAATALERVVLRVWEQVLGVSG 993
                        1050      1060      1070      1080      1090      1100
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1019 IGIDDDFFMTGGDSISAIMLCTQLR-QRGYSLRPSDVFQFKTVAAMAPQLtrldEQQAAVSK 1079
Cdd:NF038078  994 LSAQDDFFELGGQSLQSIQVANRLGvALGREVPVATVFRHPTAAGLAQAL----EHGASVAA 1051
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
1538-2032 1.86e-146

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: 465.28  E-value: 1.86e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1538 LREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHP 1617
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1618 TERIKFMLQDAKSKLVIGEQKDLAAIVHPSIATFAFNELFDETKVDLSsyKTTVITPQHPAYLIYTSGTTGQPKGVMVSH 1697
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAE--PDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1698 QAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLhFVPsml 1777
Cdd:cd17651   159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRV-FLP--- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1778 AVFENAATEILSSAQRQSLPICRVFCSGEALPT--ALAKSFTEHFSCELHNLYGPTEAAVDVSY-MDATLGLHPEEscVA 1854
Cdd:cd17651   235 TVALRALAEHGRPLGVRLAALRYLLTGGEQLVLteDLREFCAGLPGLRLHNHYGPTETHVVTALsLPGDPAAWPAP--PP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1855 IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIG 1934
Cdd:cd17651   313 IGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLG 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1935 RADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKAnvQLVAYL--QTTAPVDIDQLKKQLAKHLPAYMVPTH 2011
Cdd:cd17651   393 RADDQVKIRGFRIELGEIEAALARHPGVrEAVVLAREDRPGEK--RLVAYVvgDPEAPVDAAELRAALATHLPEYMVPSA 470
                         490       500
                  ....*....|....*....|.
gi 490930577 2012 YMLVEQFPLSHNGKLDRKALP 2032
Cdd:cd17651   471 FVLLDALPLTPNGKLDRRALP 491
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
1536-2034 2.17e-146

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: 465.26  E-value: 2.17e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1536 QLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQ 1615
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1616 HPTERIKFMLQDAKSKLVIGEQKdlaaiVHPSIATFAFNELFDETkvDLSSYKTT----VITPQHPAYLIYTSGTTGQPK 1691
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSH-----LQPPIAFIGLIDLLDED--TIYHEESEnlepVSKSDDLAYVIYTSGSTGKPK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1692 GVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLH 1771
Cdd:cd17655   154 GVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIID 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1772 FVPSMLAVFENAAteilssaQRQSLPICRVFCSGEALPTALAKSFTEHF--SCELHNLYGPTEAAVDVSYMDATLGLHPE 1849
Cdd:cd17655   234 LTPAHLKLLDAAD-------DSEGLSLKHLIVGGEALSTELAKKIIELFgtNPTITNAYGPTETTVDASIYQYEPETDQQ 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 EScVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGS 1929
Cdd:cd17655   307 VS-VPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGN 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD-VVVHAISSEQNkaNVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMV 2008
Cdd:cd17655   386 IEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKeAVVIARKDEQG--QNYLCAYIVSEKELPVAQLREFLARELPDYMI 463
                         490       500
                  ....*....|....*....|....*.
gi 490930577 2009 PTHYMLVEQFPLSHNGKLDRKALPQP 2034
Cdd:cd17655   464 PSYFIKLDEIPLTPNGKVDRKALPEP 489
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
1536-2031 4.97e-143

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: 455.51  E-value: 4.97e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1536 QLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQ 1615
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1616 HPTERIKFMLQDAKSKLVIGEQKDLAAIVHPSIATFAFNELFDETKVDLSsyktTVITPQHPAYLIYTSGTTGQPKGVMV 1695
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPA----VPVSPDDLAYVMYTSGSTGRPKGVAV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1696 SHQAIVNriLWMQSEY-PLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVP 1774
Cdd:cd12117   157 THRGVVR--LVKNTNYvTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1775 SMLAVFENAATEILSSAqRQslpicrVFCSGEALPTALAKSFTEHfsC---ELHNLYGPTEAAVDVSY--MDAtlgLHPE 1849
Cdd:cd12117   235 ALFNQLADEDPECFAGL-RE------LLTGGEVVSPPHVRRVLAA--CpglRLVNGYGPTENTTFTTShvVTE---LDEV 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 ESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGS 1929
Cdd:cd12117   303 AGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGR 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAIssEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMV 2008
Cdd:cd12117   383 LEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVrEAVVVVR--EDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMV 460
                         490       500
                  ....*....|....*....|...
gi 490930577 2009 PTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd12117   461 PAAFVVLDELPLTANGKVDRRAL 483
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1569-1966 1.63e-138

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: 439.39  E-value: 1.63e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1569 ALAQQLQ-RAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQK--DLAAIVH 1645
Cdd:TIGR01733   11 RLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSAlaSRLAGLV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1646 PSIATFAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPC 1725
Cdd:TIGR01733   91 LPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASL 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1726 TFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLS-LIQKYQVTTLHFVPSMLAVfenaateiLSSAQRQSLPICR-VFC 1803
Cdd:TIGR01733  171 SFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaLIAEHPVTVLNLTPSLLAL--------LAAALPPALASLRlVIL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1804 SGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGEL 1882
Cdd:TIGR01733  243 GGEALTPALVDRWRARGpGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGEL 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1883 YLAGHQLAMGYLHRADLTASRFVANPF--TAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLIS 1960
Cdd:TIGR01733  323 YIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHP 402

                   ....*.
gi 490930577  1961 GLDVVV 1966
Cdd:TIGR01733  403 GVREAV 408
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
1546-2031 1.82e-136

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: 435.20  E-value: 1.82e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIGEqkdlaaivhpsiatfafnelfdetkvdlssykttvitPQHPAYLIYTSGTTGQPKGVMVSHqAIVNRIL 1705
Cdd:cd17643    81 ADSGPSLLLTD-------------------------------------PDDLAYVIYTSGSTGRPKGVVVSH-ANVLALF 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 W-MQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaa 1784
Cdd:cd17643   123 AaTQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQL---- 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1785 TEILSSAQRQSLPICRVFCSGEALPTALAKSFTEHF---SCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWN 1861
Cdd:cd17643   199 VEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFgldRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPG 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1862 TQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFT-AGQRMYRTGDIARWHADGSIQYIGRADDQL 1940
Cdd:cd17643   279 LRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQV 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1941 KIRGQRIELGEIEQQLRLISGL-DVVVhaISSEQNKANVQLVAYL--QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQ 2017
Cdd:cd17643   359 KIRGFRIELGEIEAALATHPSVrDAAV--IVREDEPGDTRLVAYVvaDDGAAADIAELRALLKELLPDYMVPARYVPLDA 436
                         490
                  ....*....|....
gi 490930577 2018 FPLSHNGKLDRKAL 2031
Cdd:cd17643   437 LPLTVNGKLDRAAL 450
PRK12316 PRK12316
peptide synthase; Provisional
124-1317 1.87e-135

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 477.53  E-value: 1.87e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  124 KSLKAGETqlfRQVLFTThdkvywyqrYHHIMLDGFSMINLTKRIVELYQQLQEGK--DLSVSPFIGVNEVISER---QA 198
Cdd:PRK12316  166 RLLRLGEE---EHVLLLT---------LHHIVSDGWSMNVLIEEFSRFYSAYATGAepGLPALPIQYADYALWQRswlEA 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  199 YENSHQFkidqAFWKAYCEDLPSPISLSTHH-LAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIY 277
Cdd:PRK12316  234 GEQERQL----EYWRAQLGEEHPVLELPTDHpRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLH 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  278 KMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSidih 357
Cdd:PRK12316  310 RYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKV---- 385
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  358 ER--MYGPILNYKAFDQDLVIDGEKVKT-HHISTGPID----DFEFSFIVQDHELIIELRAdSQRYTQDeLFN------- 423
Cdd:PRK12316  386 ERslSHSPLFQVMYNHQPLVADIEALDTvAGLEFGQLEwksrTTQFDLTLDTYEKGGRLHA-ALTYATD-LFEartverm 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  424 --HGQRLtllLEQALIRPEQPCSNFNITTPQELTALTQSGIGPRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErpnlQ 501
Cdd:PRK12316  464 arHWQNL---LRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQ-RGVHRLFEEQVERTPEAPALAFGE----E 535
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  502 HLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTT 581
Cdd:PRK12316  536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ 615
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  582 QALAQQLP--QNIQQLHLDQEGVQTQIRKQDASDIPAenrkfDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPT 659
Cdd:PRK12316  616 SHLGRKLPlaAGVQVLDLDRPAAWLEGYSEENPGTEL-----NPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQA 690
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  660 IYWPVLEAVNERFPdrplraahthsFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSfcaq 738
Cdd:PRK12316  691 YGLGVGDTVLQKTP-----------FSFDVSVWEFFWPLMsGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPS---- 755
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  739 mMTNGLF----VENQHHPSLILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVD----TFRAELKQTarPVIGNPIG 809
Cdd:PRK12316  756 -MLQAFLqdedVASCTSLRRIVCSGEALPADAQEQVFAKlPQAGLYNLYGPTEAAIDvthwTCVEEGGDS--VPIGRPIA 832
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  810 NTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQI 889
Cdd:PRK12316  833 NLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQV 912
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  890 KIRGYRVEIGEVENALSILTNVESAVVIAEpinNSHRLLGYCVVKDIELDekTSEQLSQqylsQLRQNLPEYMVPSALTV 969
Cdd:PRK12316  913 KLRGLRIELGEIEARLLEHPWVREAAVLAV---DGKQLVGYVVLESEGGD--WREALKA----HLAASLPEYMVPAQWLA 983
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  970 MSEFPRNVSGKVDKKALPKPQIRAHSRMAETPE---QQLLCQITASVLKLDAIGIDDDFFMTGGDSISAIMLCTQLRQRG 1046
Cdd:PRK12316  984 LERLPLTPNGKLDRKALPAPEASVAQQGYVAPRnalERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAG 1063
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1047 YSLRPSDVFQFKTVAAMAPQLTRldEQQAAVSKplfsadleqkvqekyGKNSTILPLLPLQKgMLFLSQVENQSNYNAFT 1126
Cdd:PRK12316 1064 IQLSPRDLFQHQTIRSLALVAKA--GQATAADQ---------------GPASGEVALAPVQR-WFFEQAIPQRQHWNQSL 1125
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1127 RLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAE------EPVFIYSLhptqaWPVQFCSVTPdlLEQTIQEAlQQP 1200
Cdd:PRK12316 1126 LLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGwqqayaAPQAGEVL-----WQRQAASEEE--LLALCEEA-QRS 1197
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1201 IHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQQLPVLEHSYETVIKALSGrdHETSK 1279
Cdd:PRK12316 1198 LDLEQgP--LLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWARRLHE--HAGAR 1273
                        1210      1220      1230      1240
                  ....*....|....*....|....*....|....*....|....*..
gi 490930577 1280 V----IWQRDLADLQPLILFNQAQQAVQ-----ETSYRLSAELGAKL 1317
Cdd:PRK12316 1274 AeeldYWQAQLEDAPHELPCENPDGALEnrherKLELRLDAERTRQL 1320
PRK12467 PRK12467
peptide synthase; Provisional
152-1324 2.96e-134

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 473.49  E-value: 2.96e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  152 HHIMLDGFSMINLTKRIVELYQQLQEGKDLSVS--PFIGVNEVISERQAYENSHQFKiDQAFWKAYC----------EDL 219
Cdd:PRK12467 1247 HHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPalPIQYADYAVWQRQWMDAGERAR-QLAYWKAQLggeqpvlelpTDR 1325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  220 PSPISLSthHLAAKttatfvkHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKA 299
Cdd:PRK12467 1326 PRPAVQS--HRGAR-------LAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAET 1396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  300 IRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSidihERMYG--PILNYkAFDQDLVID 377
Cdd:PRK12467 1397 EGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQP----ERSLShsPLFQV-MFNHQRDDH 1471
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  378 GEKVKTHHIStgpIDDFEFSFIVQDHELIIELRADSQ------RYTQDeLFNHG--QRLTL----LLEQALIRPEQPCSN 445
Cdd:PRK12467 1472 QAQAQLPGLS---VESLSWESQTAQFDLTLDTYESSEglqaslTYATD-LFEAStiERLAGhwlnLLQGLVADPERRLGE 1547
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  446 FNITTPQELTALTQSGIGPRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGAR 525
Cdd:PRK12467 1548 LDLLDEAERRQILEGWNATHTGYPLA-RLVHQLIEDQAAATPEAVALVFGE----QELTYGELNRRANRLAHRLIALGVG 1622
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  526 KQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLP--QNIQQLHLDQEgvQ 603
Cdd:PRK12467 1623 PEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPlpDGLRSLVLDQE--D 1700
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  604 TQIRKQDASDiPAENrkFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLilshkptiywpvLEAVNERFPdrpLRAA--- 680
Cdd:PRK12467 1701 DWLEGYSDSN-PAVN--LAPQNLAYVIYTSGSTGRPKGAGNRHGALVNR------------LCATQEAYQ---LSAAdvv 1762
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  681 -HTHSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIG 758
Cdd:PRK12467 1763 lQFTSFAFDVSVWELFWpLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCG 1842
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  759 GEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVDTF-----RAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELY 832
Cdd:PRK12467 1843 GEALEVEALRPWLERlPDTGLFNLYGPTETAVDVThwtcrRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELY 1922
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  833 ISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV 911
Cdd:PRK12467 1923 LGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGV 2002
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  912 ESAVVIAEPINNSHRLLGYCVVKDIEL-DEKTSEQLSQQYLSQ-LRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:PRK12467 2003 REAVVIAQDGANGKQLVAYVVPTDPGLvDDDEAQVALRAILKNhLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP 2082
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  990 QIRAHSRMAETPE---QQLLCQITASVLKLDAIGIDDDFFMTGGDSISAIMLCTQLRQRGYSLRPSDVFQFKTVAAMApq 1066
Cdd:PRK12467 2083 DASELQQAYVAPQselEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLA-- 2160
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1067 lTRLDEQQAAVSkplfsadLEQkvqekyGKNSTILPLLPLQKgMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITV 1146
Cdd:PRK12467 2161 -AVAQEGDGTVS-------IDQ------GPVTGDLPLLPIQQ-MFFADDIPERHHWNQSVLLEPREALDAELLEAALQAL 2225
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1147 LKRHPQL------------GGHFDSELAEEPVFiyslhptqaWPVQFCSVtpDLLEQTIQEALQQpihLDQPYG-LIRAT 1213
Cdd:PRK12467 2226 LVHHDALrlgfvqedggwsAMHRAPEQERRPLL---------WQVVVADK--EELEALCEQAQRS---LDLEEGpLLRAV 2291
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1214 LIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQQLPVLEHSYETVIKALSGR--DHETSKVI------WQRD 1285
Cdd:PRK12467 2292 LATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERlqTYAASAALadelgyWQAQ 2371
                        1210      1220      1230      1240
                  ....*....|....*....|....*....|....*....|.
gi 490930577 1286 LADLQPLILFNQAQQAVQeTSYRLSA--ELGAKLQHKLRQQ 1324
Cdd:PRK12467 2372 LQGASTELPCDHPQGGLQ-RRHAASVttHLDSEWTRRLLQE 2411
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
1546-2032 1.46e-133

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: 426.28  E-value: 1.46e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVigeqkdlaaivhpsiatfafnelfdetkvdlssykttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd17652    81 ADARPALL-------------------------------------LTTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAAt 1785
Cdd:cd17652   124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDD- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1786 eilssaqrqsLPICRVFCS-GEALPTALAKSFTEHfsCELHNLYGPTEAAVDVSYMDATlglhPEESCVAIGYPVWNTQL 1864
Cdd:cd17652   203 ----------LPDLRTLVVaGEACPAELVDRWAPG--RRMINAYGPTETTVCATMAGPL----PGGGVPPIGRPVPGTRV 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:cd17652   267 YVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIR 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1944 GQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYL--QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLS 2021
Cdd:cd17652   347 GFRIELGEVEAALTEHPGVAEAV-VVVRDDRPGDKRLVAYVvpAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLT 425
                         490
                  ....*....|.
gi 490930577 2022 HNGKLDRKALP 2032
Cdd:cd17652   426 PNGKLDRRALP 436
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
477-986 5.68e-132

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: 423.54  E-value: 5.68e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  477 DIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDR----SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  557 LDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQniqqlhldQEGVQTQIRKQDASDIPAENRKFDFQDVAYVIFTSGST 636
Cdd:cd12117    77 LDPELPAERLAFMLADAGAKVLLTDRSLAGRAGG--------LEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGST 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  637 GRPKGVMNTHGSLLNLILSHkptiyWPVLEAVNERFpdrplraAHTHSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAF 715
Cdd:cd12117   149 GRPKGVAVTHRGVVRLVKNT-----NYVTLGPDDRV-------LQTSPLAFDASTFEIWGaLLNGARLVLAPKGTLLDPD 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  716 GLVQEIQQRQIDTLdlppsfcaqMMTNGLFveNQ---HHPSL------ILIGGEAAPLALWQQ-LNAQPALFAHNLYGPT 785
Cdd:cd12117   217 ALGALIAEEGVTVL---------WLTAALF--NQladEDPECfaglreLLTGGEVVSPPHVRRvLAACPGLRLVNGYGPT 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  786 EYTVDT--FR-AELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHG 861
Cdd:cd12117   286 ENTTFTtsHVvTELDEVAGSIpIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPG 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  862 QRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINN-SHRLLGYcVVKDIELDe 940
Cdd:cd12117   366 ERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGgDKRLVAY-VVAEGALD- 443
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 490930577  941 ktSEQLSqqylSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd12117   444 --AAELR----AFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
477-986 4.30e-131

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: 421.30  E-value: 4.30e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  477 DIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:cd17646     2 ALVAEQAARTPDAPAVVDEGR----TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  557 LDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQniqqLHLDQEGVQTQIRKQDASDIPAENRKfdfQDVAYVIFTSGST 636
Cdd:cd17646    78 LDPGYPADRLAYMLADAGPAVVLTTADLAARLPA----GGDVALLGDEALAAPPATPPLVPPRP---DNLAYVIYTSGST 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  637 GRPKGVMNTHGSLLNLILshkptiyWpvleaVNERFP----DRPLRAAhthSFSFDSSWLQVFW-MLWGQELHIFDENMR 711
Cdd:cd17646   151 GRPKGVMVTHAGIVNRLL-------W-----MQDEYPlgpgDRVLQKT---PLSFDVSVWELFWpLVAGARLVVARPGGH 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  712 RDAFGLVQEIQQRQIDTLDLPPSfcaqMMtnGLFVEN---QHHPSL--ILIGGEAAPLALWQQLNAQPALFAHNLYGPTE 786
Cdd:cd17646   216 RDPAYLAALIREHGVTTCHFVPS----ML--RVFLAEpaaGSCASLrrVFCSGEALPPELAARFLALPGAELHNLYGPTE 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  787 YTVDT--FRAELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQR 863
Cdd:cd17646   290 AAIDVthWPVRGPAETPSVpIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSR 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  864 MYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYCVVKDIELDEKT 942
Cdd:cd17646   370 MYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAaRLVGYVVPAAGAAGPDT 449
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 490930577  943 SEqlsqqYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17646   450 AA-----LRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
PRK05691 PRK05691
peptide synthase; Validated
1100-2117 4.97e-130

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 460.02  E-value: 4.97e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIysLHPTQAWP 1178
Cdd:PRK05691 3257 VYPLTPMQEGLLLHTLLEPGTGlYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQV--IHKPGRTP 3334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1179 VQFC---SVTPDLLEQTIQEALQQPIH-----LDQPYGLIRatLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ 1250
Cdd:PRK05691 3335 IDYLdwrGLPEDGQEQRLQALHKQEREagfdlLNQPPFHLR--LIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYT 3412
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1251 Q----TNQQLPVLEHsYETVIKALSGRDHETSKVIWQRDLADLQ---------PLI---LFNQAQQAVQETSYRLSAELG 1314
Cdd:PRK05691 3413 AlgegREAQLPVPPR-YRDYIGWLQRQDLAQARQWWQDNLRGFErptpipsdrPFLrehAGDSGGMVVGDCYTRLDAADG 3491
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1315 AKLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKL---NMQQTLWEQ 1391
Cdd:PRK05691 3492 ARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLpaaGQRCSVRQW 3571
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1392 LPQLQQLHVEHLEHDGLGLSAIQQL--IAQGN-LFDSLLVVENYP-DNQYLQQKLGDAAISKlTNRGYSHYPLALLVIP- 1466
Cdd:PRK05691 3572 LQGLLDSNMELREYEYLPLVAIQECseLPKGQpLFDSLFVFENAPvEVSVLDRAQSLNASSD-SGRTHTNFPLTAVCYPg 3650
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1467 -DHQIELLLEQRgVIDQPEhfLERMI---QLIEIALNEP-ETSLSHYRLQLAEEHD-LIQKTNQTQ--YYVRQSTLQqLL 1538
Cdd:PRK05691 3651 dDLGLHLSYDQR-YFDAPT--VERLLgefKRLLLALVQGfHGDLSELPLLGEQERDfLLDGCNRSErdYPLEQSYVR-LF 3726
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1539 REQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPT 1618
Cdd:PRK05691 3727 EAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPA 3806
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1619 ERIKFMLQDAKSKLVI--GEQKDLAAIVHPSIATFAFNEL--FDETKVDLSSYKTTVI--TPQHPAYLIYTSGTTGQPKG 1692
Cdd:PRK05691 3807 QRLQRIIELSRTPVLVcsAACREQARALLDELGCANRPRLlvWEEVQAGEVASHNPGIysGPDNLAYVIYTSGSTGLPKG 3886
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1693 VMVSHQAIVNRILwmqSEYP---LSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTT 1769
Cdd:PRK05691 3887 VMVEQRGMLNNQL---SKVPylaLSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITV 3963
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1770 LHFVPSMLavfenaaTEILSSaQRQSLPICR-VFCSGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSY----MDAT 1843
Cdd:PRK05691 3964 LESVPSLI-------QGMLAE-DRQALDGLRwMLPTGEAMPPELARQWLQRYpQIGLVNAYGPAECSDDVAFfrvdLAST 4035
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1844 LGlhpeeSCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTA-GQRMYRTGDIA 1922
Cdd:PRK05691 4036 RG-----SYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGApGERLYRTGDLA 4110
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1923 RWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKanvQLVAYLQTTAPVD-----IDQLK 1996
Cdd:PRK05691 4111 RRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVrEAAVAVQEGVNGK---HLVGYLVPHQTVLaqgalLERIK 4187
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1997 KQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYA-TSAFEHELTRIFQQILNTDQnIGVNEDFF 2075
Cdd:PRK05691 4188 QRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLApRNELEQTLATIWADVLKVER-VGVHDNFF 4266
                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|..
gi 490930577 2076 AIGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALL 2117
Cdd:PRK05691 4267 ELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI 4308
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
1546-2032 3.51e-129

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: 414.46  E-value: 3.51e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIGEqkdlaaivhpsiatfafnelfdetkvdlssykttviTPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd17649    81 EDSGAGLLLTH------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaAT 1785
Cdd:cd17649   125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQL---AE 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1786 EILSSAQRQSLPIcRVFCS-GEAL-PTALAKSFTEHfsCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQ 1863
Cdd:cd17649   202 EADRTGDGRPPSL-RLYIFgGEALsPELLRRWLKAP--VRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRS 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1864 LYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGRADDQLKI 1942
Cdd:cd17649   279 AYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKI 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1943 RGQRIELGEIEQQLRLISG-LDVVVHAISSEQNKanvQLVAYL----QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQ 2017
Cdd:cd17649   359 RGFRIELGEIEAALLEHPGvREAAVVALDGAGGK---QLVAYVvlraAAAQPELRAQLRTALRASLPDYMVPAHLVFLAR 435
                         490
                  ....*....|....*
gi 490930577 2018 FPLSHNGKLDRKALP 2032
Cdd:cd17649   436 LPLTPNGKLDRKALP 450
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
479-987 1.97e-128

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: 413.66  E-value: 1.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  479 FYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLD 558
Cdd:cd17651     1 FERQAARTPDAPALVAEGR----RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  559 LDYPIDRMQMMCEDANPLFVLTTQALAQQLPQniqqlhlDQEGVQTQIRKQDASDIPAENR-KFDFQDVAYVIFTSGSTG 637
Cdd:cd17651    77 PAYPAERLAFMLADAGPVLVLTHPALAGELAV-------ELVAVTLLDQPGAAAGADAEPDpALDADDLAYVIYTSGSTG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  638 RPKGVMNTHGSLLNLILSHkptiywpvleavNERFP-DRPLRAAHTHSFSFDSSWLQVFWML-WGQELHIFDENMRRDAF 715
Cdd:cd17651   150 RPKGVVMPHRSLANLVAWQ------------ARASSlGPGARTLQFAGLGFDVSVQEIFSTLcAGATLVLPPEEVRTDPP 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  716 GLVQEIQQRQIDTLDLPPSFcAQMMTNGLFVENQHHPSL--ILIGGEAAPL--ALWQQLNAQPALFAHNLYGPTEYTVDT 791
Cdd:cd17651   218 ALAAWLDEQRISRVFLPTVA-LRALAEHGRPLGVRLAALryLLTGGEQLVLteDLREFCAGLPGLRLHNHYGPTETHVVT 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  792 FRaELKQ-----TARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYR 866
Cdd:cd17651   297 AL-SLPGdpaawPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYR 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  867 TGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP-INNSHRLLGYcVVKDIELDEKTSEq 945
Cdd:cd17651   376 TGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREdRPGEKRLVAY-VVGDPEAPVDAAE- 453
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 490930577  946 LSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17651   454 LRA----ALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
487-986 5.00e-128

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: 411.68  E-value: 5.00e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd12116     1 PDATAVRDDDRS----LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  567 QMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDASDIPAenrkfdfqDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd12116    77 RYILEDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPD--------DLAYVIYTSGSTGRPKGVVVSH 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  647 GSLLNLilshkptiywpvLEAVNERF---PDRPLRAAHThsFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQEIQ 722
Cdd:cd12116   149 RNLVNF------------LHSMRERLglgPGDRLLAVTT--YAFDISLLELLLPLLaGARVVIAPRETQRDPEALARLIE 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  723 QRQIDTLDLPPSfCAQMMtngLFVENQHHPSL-ILIGGEAAPLALWQQLNAQPALfAHNLYGPTEYTVDTFRAELKQTAR 801
Cdd:cd12116   215 AHSITVMQATPA-TWRML---LDAGWQGRAGLtALCGGEALPPDLAARLLSRVGS-LWNLYGPTETTIWSTAARVTAAAG 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  802 PV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEH-GQRMYRTGDLVRWNSAGKL 879
Cdd:cd12116   290 PIpIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpGSRLYRTGDLVRRRADGRL 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  880 EFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIE-LDEktsEQLSQqylsQLRQNL 958
Cdd:cd12116   370 EYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAaPDA---AALRA----HLRATL 442
                         490       500
                  ....*....|....*....|....*...
gi 490930577  959 PEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd12116   443 PAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
1534-2031 4.88e-127

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: 407.86  E-value: 4.88e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHPTERIKFMLQDAKSKLVIgeqkdlaaivhpsiatfafnelfdetkvdlssykttvITPQHPAYLIYTSGTTGQPKGV 1693
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVL-------------------------------------TDPDDLAYVIYTSGSTGRPKGV 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1694 MVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIApidahRDPLALLSLIQKYQVTTLHFV 1773
Cdd:cd12115   124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINTV 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1774 PSmlavfenAATEILS-SAQRQSLpicRVFC-SGEALPTALAKSFTEHFSCE-LHNLYGPTEaavDVSYMDAT-LGLHPE 1849
Cdd:cd12115   199 PS-------AAAELLRhDALPASV---RVVNlAGEPLPRDLVQRLYARLQVErVVNLYGPSE---DTTYSTVApVPPGAS 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 EScVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGS 1929
Cdd:cd12115   266 GE-VSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGL 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD---VVVHaissEQNKANVQLVAYLQTTAP--VDIDQLKKQLAKHLP 2004
Cdd:cd12115   345 LEFLGRADNQVKVRGFRIELGEIEAALRSIPGVReavVVAI----GDAAGERRLVAYIVAEPGaaGLVEDLRRHLGTRLP 420
                         490       500
                  ....*....|....*....|....*..
gi 490930577 2005 AYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd12115   421 AYMVPSRFVRLDALPLTPNGKIDRSAL 447
PRK12316 PRK12316
peptide synthase; Provisional
152-1324 1.85e-126

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 448.64  E-value: 1.85e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  152 HHIMLDGFSMINLTKRIVELYQQLQEGKDLSVSPF-IGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHHL 230
Cdd:PRK12316 2731 HHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLpLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRP 2810
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  231 -AAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNV 309
Cdd:PRK12316 2811 rPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNT 2890
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  310 LPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQIL------RDLNSIDIHERMYGPILNYKAFDQDLVIDGEKVKT 383
Cdd:PRK12316 2891 QVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVealqpeRSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAW 2970
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  384 HHISTGPidDFEFSFIVQDHELIIELRADSQRYTQDELFNHGQRLTLLLEQALIRPEQPCSNFNITTPQELTALTQSGIG 463
Cdd:PRK12316 2971 DGAATQF--DLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNA 3048
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  464 PRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVV 543
Cdd:PRK12316 3049 TAAEYPLE-RGVHRLFEEQVERTPDAVALAFGE----QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVG 3123
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  544 MLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDASDIPaenrkfdf 623
Cdd:PRK12316 3124 LLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMP-------- 3195
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  624 QDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiywpVLEAVNERFPDRPLRAAhthSFSFDSSWLQVFWMLW-GQE 702
Cdd:PRK12316 3196 ENLAYVIYTSGSTGKPKGVGIRHSALSNHLCW--------MQQAYGLGVGDRVLQFT---TFSFDVFVEELFWPLMsGAR 3264
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  703 LHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNglfVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFahN 780
Cdd:PRK12316 3265 VVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEE---EDAHRCTSLkrIVCGGEALPADLQQQVFAGLPLY--N 3339
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  781 LYGPTEYTVDT--FRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF 858
Cdd:PRK12316 3340 LYGPTEATITVthWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF 3419
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  859 EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEpinNSHRLLGYCVVKDIEL 938
Cdd:PRK12316 3420 VPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV---DGRQLVAYVVPEDEAG 3496
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  939 DektseqLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP---QIRAHSRMAETPEQQLLCQITASVLK 1015
Cdd:PRK12316 3497 D------LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPdaaLLQQDYVAPVNELERRLAAIWADVLK 3570
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1016 LDAIGIDDDFFMTGGDSISAIMLCTQLRQRGYSLRPSDVFQFKTVAAMAPqLTRLDEQQAAVSKPLfsadleqkvqekyg 1095
Cdd:PRK12316 3571 LEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLAR-VARVGGGVAVDQGPV-------------- 3635
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1096 knSTILPLLPLQKGmLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQ 1175
Cdd:PRK12316 3636 --SGETLLLPIQQQ-FFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGG 3712
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1176 AWPVQFCSVTPDLLEQTIQEAlQQPIHL-DQPygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQ 1254
Cdd:PRK12316 3713 ALLWRAELDDAEELERLGEEA-QRSLDLaDGP--LLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQ 3789
                        1130      1140      1150      1160      1170      1180      1190
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1255 ----QLPVLEHSYETVIKALSGRDHETSK----VIWQRDLADLQPLILFNQAQQAVQETSYR-LSAELGAKLQHKLRQQ 1324
Cdd:PRK12316 3790 geapRLPAKTSSFKAWAERLQEHARGEALkaelAYWQEQLQGVSSELPCDHPQGALQNRHAAsVQTRLDRELTRRLLQQ 3868
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
479-989 2.37e-126

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: 407.87  E-value: 2.37e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  479 FYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLD 558
Cdd:cd17655     3 FEEQAEKTPDHTAVVFED----QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  559 LDYPIDRMQMMCEDANPLFVLTTQALAQQLpQNIQQLHLDQEGvqtQIRKQDASDIPAENRkfdFQDVAYVIFTSGSTGR 638
Cdd:cd17655    79 PDYPEERIQYILEDSGADILLTQSHLQPPI-AFIGLIDLLDED---TIYHEESENLEPVSK---SDDLAYVIYTSGSTGK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  639 PKGVMNTHGSLLNLILSHKPTIYwpvleavnerfPDRPLRAAHTHSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAFGL 717
Cdd:cd17655   152 PKGVMIEHRGVVNLVEWANKVIY-----------QGEHLRVALFASISFDASVTEIFAsLLSGNTLYIVRKETVLDGQAL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  718 VQEIQQRQIDTLDLPPSFCAQMMTNGLFVE-NQHHpslILIGGEAAPLALWQQL----NAQPALFahNLYGPTEYTVDT- 791
Cdd:cd17655   221 TQYIRQNRITIIDLTPAHLKLLDAADDSEGlSLKH---LIVGGEALSTELAKKIielfGTNPTIT--NAYGPTETTVDAs 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  792 ---FRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTG 868
Cdd:cd17655   296 iyqYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  869 DLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP-INNSHRLLGYcVVKDIELdekTSEQLS 947
Cdd:cd17655   376 DLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKdEQGQNYLCAY-IVSEKEL---PVAQLR 451
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 490930577  948 QqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:cd17655   452 E----FLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489
PRK12316 PRK12316
peptide synthase; Provisional
53-1072 1.26e-122

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 436.31  E-value: 1.26e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   53 VDIPTFKKAIQIGLNEADTVIASY--SSDPSQPFIELNNQVQFQIEEFDFCHLTPKKAQqrLWDWMPSDRQCAKSLKagE 130
Cdd:PRK12316 4136 LDVERFRAAWQAALDRHDVLRSGFvwQGELGRPLQVVHKQVSLPFAELDWRGRADLQAA--LDALAAAERERGFDLQ--R 4211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  131 TQLFRQVLFTT----HDKVYwyqRYHHIMLDGFSMINLTKRIVELYQQLQEGK-DLSVSPFIGvnevISERQAYENShqf 205
Cdd:PRK12316 4212 APLLRLVLVRTaegrHHLIY---TNHHILMDGWSNSQLLGEVLERYSGRPPAQpGGRYRDYIA----WLQRQDAAAS--- 4281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  206 kidQAFWKAYCEDLPSPISLSTHHLAAK--TTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKA 283
Cdd:PRK12316 4282 ---EAFWREQLAALDEPTRLAQAIARADlrSANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQD 4358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  284 ELVNGIPFMRRLGS-KAIRSTLPT-VNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRD--------LNS 353
Cdd:PRK12316 4359 TVAFGATVAGRPAElPGIEGQIGLfINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWagqggealFDS 4438
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  354 IDIHERMygPILNY--KAFDQDLVIDgeKVKTHHISTGPIDdfeFSFIVQDhELIIELRADSQRYTQDELFNHGQRLTLL 431
Cdd:PRK12316 4439 LLVFENY--PVSEAlqQGAPGGLRFG--EVTNHEQTNYPLT---LAVGLGE-TLSLQFSYDRGHFDAATIERLARHLTNL 4510
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  432 LEQALIRPEQPCSNFNITTPQELTALTQSGIGPRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVK 511
Cdd:PRK12316 4511 LEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPAT-RCVHQLVAERARMTPDAVAVVFDE----EKLTYAELNRR 4585
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  512 VNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLP-- 589
Cdd:PRK12316 4586 ANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPip 4665
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  590 QNIQQLHLDQEGvqtqirkqDASDIPAEN--RKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiywpVLEA 667
Cdd:PRK12316 4666 DGLASLALDRDE--------DWEGFPAHDpaVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHA--------TGER 4729
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  668 VNERFPDRPLraaHTHSFSFDSSWLQVFWMLW-GQELHIFDENMRrDAFGLVQEIQQRQIDTLDLPPSFCaQMMTNGlFV 746
Cdd:PRK12316 4730 YELTPDDRVL---QFMSFSFDGSHEGLYHPLInGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYL-QQLAEH-AE 4803
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  747 ENQHHPSL--ILIGGEAAPLALWQQ-LNAQPALFAHNLYGPTEYTVDTfraeLKQTARPV---------IGNPIGNTQAY 814
Cdd:PRK12316 4804 RDGEPPSLrvYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTV----LLWKARDGdacgaaympIGTPLGNRSGY 4879
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  815 VLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRG 893
Cdd:PRK12316 4880 VLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRG 4959
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  894 YRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEKTSEQ--LSQQYLSQLRQNLPEYMVPSALTVMS 971
Cdd:PRK12316 4960 FRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQaeLRDELKAALRERLPEYMVPAHLVFLA 5039
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  972 EFPRNVSGKVDKKALPKPQIRAHSRMAETPEQQLLCQITA---SVLKLDAIGIDDDFFMTGGDSISAIMLCTQLR-QRGY 1047
Cdd:PRK12316 5040 RMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAiwaEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQlELGL 5119
                        1050      1060
                  ....*....|....*....|....*
gi 490930577 1048 SLRPSDVFQFKTVAAMAPQLTRLDE 1072
Cdd:PRK12316 5120 ELPLRELFQTPTLAAFVELAAAAGS 5144
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
487-987 2.03e-120

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: 388.53  E-value: 2.03e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd17652     1 PDAPAVVFGDE----TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  567 QMMCEDANPLFVLTTQAlaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfqDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd17652    77 AYMLADARPALLLTTPD-----------------------------------------NLAYVIYTSGSTGRPKGVVVTH 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  647 GSLLNLIlshkptiywpvlEAVNERFPDRP-LRAAHTHSFSFDSSwlqvFWMLW-----GQELHIFDENMRRDAFGLVQE 720
Cdd:cd17652   116 RGLANLA------------AAQIAAFDVGPgSRVLQFASPSFDAS----VWELLmallaGATLVLAPAEELLPGEPLADL 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  721 IQQRQIDTLDLPPSFCAQMMTNGLfvenqhhPSL--ILIGGEAAPLALWQQLNAQPALFahNLYGPTEYTVDTFRAELKQ 798
Cdd:cd17652   180 LREHRITHVTLPPAALAALPPDDL-------PDLrtLVVAGEACPAELVDRWAPGRRMI--NAYGPTETTVCATMAGPLP 250
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  799 TARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSA 876
Cdd:cd17652   251 GGGVPpIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRAD 330
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  877 GKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYCVVKDIELDekTSEQLSQqylsQLR 955
Cdd:cd17652   331 GQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDkRLVAYVVPAPGAAP--TAAELRA----HLA 404
                         490       500       510
                  ....*....|....*....|....*....|..
gi 490930577  956 QNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17652   405 ERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1534-2031 6.96e-120

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: 388.82  E-value: 6.96e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEvrLQVCA--LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLP 1611
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAE--LDRLSsrLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1612 IDLQHPTERIKFMLQDAKSKLVigeqkdlaaivhpsiatfafnelfdetkvdLSSykttviTPQHPAYLIYTSGTTGQPK 1691
Cdd:cd05918    79 LDPSHPLQRLQEILQDTGAKVV------------------------------LTS------SPSDAAYVIFTSGSTGKPK 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1692 GVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLAllSLIQKYQVTTLH 1771
Cdd:cd05918   123 GVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLA--GFINRLRVTWAF 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1772 FVPSMLAVFenaateilssaQRQSLPICRVFCS-GEALPTALAKSFTEHfsCELHNLYGPTEAAVDVSYMDATLGLHPEE 1850
Cdd:cd05918   201 LTPSVARLL-----------DPEDVPSLRTLVLgGEALTQSDVDTWADR--VRLINAYGPAECTIAATVSPVVPSTDPRN 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1851 scvaIGYPVwNTQLYILDQ--YLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANP-------FTAGQRMYRTGDI 1921
Cdd:cd05918   268 ----IGRPL-GATCWVVDPdnHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDL 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1922 ARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLI--SGLDVVVHAISSEQNKANVQLVAYLQT------------- 1986
Cdd:cd05918   343 VRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlpGAKEVVVEVVKPKDGSSSPQLVAFVVLdgsssgsgdgdsl 422
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1987 ------TAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05918   423 flepsdEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
1546-2031 2.65e-119

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: 385.67  E-value: 2.65e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVigeqkdlaaivhpsiatfafnelfdetkvdlssykttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd17650    81 EDSGAKLL-------------------------------------LTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSA-TDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSML-AVFENA 1783
Cdd:cd17650   124 AWRREYELDSfPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIrPVMAYV 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1784 ATEILSSAQRQSLPICRVFCSGEALPTALAKsFTEHFscELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQ 1863
Cdd:cd17650   204 YRNGLDLSAMRLLIVGSDGCKAQDFKTLAAR-FGQGM--RIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTA 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1864 LYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:cd17650   281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIR 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1944 GQRIELGEIEQQLRLISGLDVVVHAIsSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHN 2023
Cdd:cd17650   361 GFRIELGEIESQLARHPAIDEAVVAV-REDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPN 439

                  ....*...
gi 490930577 2024 GKLDRKAL 2031
Cdd:cd17650   440 GKVDRRAL 447
PRK12467 PRK12467
peptide synthase; Provisional
54-1064 1.29e-116

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 416.48  E-value: 1.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   54 DIPTFKKAIQIGLNEADTVIASYSSDP--SQPFIELNNQVQFQIEEFDFchLTPKKAQQRLWDWMPSDRQcaKSLKAGET 131
Cdd:PRK12467 2681 DVERFRTAWQAVIDRHEILRSGFLWDGelEEPLQVVYKQARLPFSRLDW--RDRADLEQALDALAAADRQ--QGFDLLSA 2756
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  132 QLFRQVLFTT-HDKVYWYQRYHHIMLDGFSMINLTKRIVELYQqlqeGKDLSvSPFIGVNEVISERQAYENSHQfkidQA 210
Cdd:PRK12467 2757 PLLRLTLVRTgEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYF----GQPPP-AREGRYRDYIAWLQAQDAEAS----EA 2827
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  211 FWKAYCEDLPSPISL--STHHLAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNG 288
Cdd:PRK12467 2828 FWKEQLAALEEPTRLarALYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFG 2907
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  289 ipfmrrlgskAIRSTLPT------------VNVLPVkfkVAEKDSWVSLA---QHVQEQLREIRPHQKYDAEQILR---- 349
Cdd:PRK12467 2908 ----------ATVAGRPAqlrgaeqqlglfINTLPV---IASPRAEQTVSdwlQQVQAQNLALREFEHTPLADIQRwagq 2974
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  350 ----DLNSIDIHErmygpilNY-------KAFDQDLVIdgEKVKTHHISTGPIDdfefSFIVQDHELIIELRADSQRYTQ 418
Cdd:PRK12467 2975 ggeaLFDSILVFE-------NYpisealkQGAPSGLRF--GAVSSREQTNYPLT----LAVGLGDTLELEFSYDRQHFDA 3041
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  419 DELFNHGQRLTLLLEQALIRPEQPCSNFNITTPQELTALTQSGIGPRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErp 498
Cdd:PRK12467 3042 AAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSE-RLVHQLIEAQVARTPEAPALVFGD-- 3118
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  499 nlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFV 578
Cdd:PRK12467 3119 --QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLL 3196
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  579 LTTQALAQQLPQ--NIQQLHLDQEGVQTQIRKQDASDIPAENrkfdfqdVAYVIFTSGSTGRPKGVMNTHGSLLNLIlsh 656
Cdd:PRK12467 3197 LTQAHLLEQLPApaGDTALTLDRLDLNGYSENNPSTRVMGEN-------LAYVIYTSGSTGKPKGVGVRHGALANHL--- 3266
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  657 kptiYWpVLEAVNERFPDRPLRAAhthSFSFDSSWLQVFWMLW-GQELHIFDeNMRRDAFGLVQEIQQRQIDTLDLPPSF 735
Cdd:PRK12467 3267 ----CW-IAEAYELDANDRVLLFM---SFSFDGAQERFLWTLIcGGCLVVRD-NDLWDPEELWQAIHAHRISIACFPPAY 3337
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  736 CAQMMTNGlfvENQHHPSL--ILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVDTFRAELKQTARPV-----IGNP 807
Cdd:PRK12467 3338 LQQFAEDA---GGADCASLdiYVFGGEAVPPAAFEQVKRKlKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEapyapIGRP 3414
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  808 IGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFE-HGQRMYRTGDLVRWNSAGKLEFMGRCD 886
Cdd:PRK12467 3415 VAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRID 3494
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  887 DQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYcVVKDIEldektSEQLSQQYLSQLRQNLPEYMVPSA 966
Cdd:PRK12467 3495 HQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAY-VVPADP-----QGDWRETLRDHLAASLPDYMVPAQ 3568
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  967 LTVMSEFPRNVSGKVDKKALPKPQI---RAHSRMAETPEQQlLCQITASVLKLDAIGIDDDFFMTGGDSISAIMLCTQLR 1043
Cdd:PRK12467 3569 LLVLAAMPLGPNGKVDRKALPDPDAkgsREYVAPRSEVEQQ-LAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIR 3647
                        1050      1060
                  ....*....|....*....|..
gi 490930577 1044 Q-RGYSLRPSDVFQFKTVAAMA 1064
Cdd:PRK12467 3648 QsLGLKLSLRDLMSAPTIAELA 3669
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
504-916 8.48e-115

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: 371.21  E-value: 8.48e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   504 SFAELAVKVNQLTRFLQEN-GARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQ 582
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   583 ALAQQLPQnIQQLHLDQEGVQTQIRkQDASDIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHkptiyw 662
Cdd:TIGR01733   81 ALASRLAG-LVLPVILLDPLELAAL-DDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL------ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   663 pvleavNERFPDRPL-RAAHTHSFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQE-IQQRQIDTLDLPPSFcAQM 739
Cdd:TIGR01733  153 ------ARRYGLDPDdRVLQFASLSFDASVEEIFGALLaGATLVVPPEDEERDDAALLAAlIAEHPVTVLNLTPSL-LAL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   740 MTNGLfVENQHHPSLILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVDTF-----RAELKQTARPVIGNPIGNTQA 813
Cdd:TIGR01733  226 LAAAL-PPALASLRLVILGGEALTPALVDRWRARgPGARLINLYGPTETTVWSTatlvdPDDAPRESPVPIGRPLANTRL 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   814 YVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF--EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKI 891
Cdd:TIGR01733  305 YVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI 384
                          410       420
                   ....*....|....*....|....*
gi 490930577   892 RGYRVEIGEVENALSILTNVESAVV 916
Cdd:TIGR01733  385 RGYRIELGEIEAALLRHPGVREAVV 409
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
1536-2031 4.07e-114

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: 370.10  E-value: 4.07e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1536 QLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQ 1615
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1616 HPTERIKFMLQDAKSKLVIgeqkdlaaivhpsiatfafnelfdetkvdlssyktTVITPQHPAYLIYTSGTTGQPKGVMV 1695
Cdd:cd17653    81 LPSARIQAILRTSGATLLL-----------------------------------TTDSPDDLAYIIFTSGSTGIPKGVMV 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1696 SHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIApidAHRDPLAllSLIQKyqVTTLHFVPS 1775
Cdd:cd17653   126 PHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLA---DPSDPFA--HVART--VDALMSTPS 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 MLAVFEnaateilssaqRQSLP-ICRVFCSGEALPTALAKSFTEhfSCELHNLYGPTEAAVDVSYmdatLGLHPEEScVA 1854
Cdd:cd17653   199 ILSTLS-----------PQDFPnLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTM----TELLPGQP-VT 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1855 IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIG 1934
Cdd:cd17653   261 IGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLG 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1935 RADDQLKIRGQRIELGEIEQQLRLISGLDVVVHAISSEQNkanvqLVAYLqTTAPVDIDQLKKQLAKHLPAYMVPTHYML 2014
Cdd:cd17653   341 REDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNGR-----LVAFV-TPETVDVDGLRSELAKHLPSYAVPDRIIA 414
                         490
                  ....*....|....*..
gi 490930577 2015 VEQFPLSHNGKLDRKAL 2031
Cdd:cd17653   415 LDSFPLTANGKVDRKAL 431
PRK05691 PRK05691
peptide synthase; Validated
41-1288 4.39e-114

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 408.40  E-value: 4.39e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   41 YTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELNNQVQFQIEEFDFCHLTPKKAQQRLWDWmpSDR 120
Cdd:PRK05691 1751 YNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQL--ADS 1828
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  121 QCAKSLKAGETQLFRQVLFTTHD-KVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQEGKD--LSVSPFIGVNEVISERQ 197
Cdd:PRK05691 1829 EAHQPFDLERGPLLRACLVKAAErEHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDREspLEPLPVQYLDYSVWQRQ 1908
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  198 AYENSH-QFKIDqaFWKAycedlpspiSLSTHH----LAAKTTATFVK-HQ---LRF--STGILEQIQALAAQTKLALNd 266
Cdd:PRK05691 1909 WLESGErQRQLD--YWKA---------QLGNEHplleLPADRPRPPVQsHRgelYRFdlSPELAARVRAFNAQRGLTLF- 1976
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  267 MMMSLSLH-YIYKMTDKAELVNGIPFMRRL--GSKAIRSTLPTVNVLPVKFkvaekDSWVSLAQhVQEQLR----EIRPH 339
Cdd:PRK05691 1977 MTMTATLAaLLYRYSGQRDLRIGAPVANRIrpESEGLIGAFLNTQVLRCQL-----DGQMSVSE-LLEQVRqtviEGQSH 2050
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  340 QKYDAEQILRDLNSIdiHERMYGPILNYK------AFDQDLVIDGEKVKthhistgpiddfefsFIVQD-----HELIIE 408
Cdd:PRK05691 2051 QDLPFDHLVEALQPP--RSAAYNPLFQVMcnvqrwEFQQSRQLAGMTVE---------------YLVNDaratkFDLNLE 2113
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  409 LRADSQR------YTQDeLFN---------HGQRLtllLEQALIRPEQPCSNFNITTPQELTALTQSgIGPRVSHPEQYN 473
Cdd:PRK05691 2114 VTDLDGRlgccltYSRD-LFDepriarmaeHWQNL---LEALLGDPQQRLAELPLLAAAEQQQLLDS-LAGEAGEARLDQ 2188
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  474 NVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGAS 553
Cdd:PRK05691 2189 TLHGLFAAQAARTPQAPALTFAG----QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGA 2264
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  554 FLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQ---QLPQNIQQLHLDQEGVQtqIRKQDASDIPAENRKfdfQDVAYVI 630
Cdd:PRK05691 2265 YVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEalgELPAGVARWCLEDDAAA--LAAYSDAPLPFLSLP---QHQAYLI 2339
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  631 FTSGSTGRPKGVMNTHGSllnlILSHkptiywpvLEAVNERFPDRPLRAA-HTHSFSFDSSWLQVFWMLWGQELHIFDEN 709
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGE----IAMH--------CQAVIERFGMRADDCElHFYSINFDAASERLLVPLLCGARVVLRAQ 2407
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  710 MRRDAFGLVQEIQQRQIDTLDLPPSFCAQMmTNGLFVENQHHP-SLILIGGEAAPLALWQQLNA--QPALFaHNLYGPTE 786
Cdd:PRK05691 2408 GQWGAEEICQLIREQQVSILGFTPSYGSQL-AQWLAGQGEQLPvRMCITGGEALTGEHLQRIRQafAPQLF-FNAYGPTE 2485
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  787 YTVDTFRA----ELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEH- 860
Cdd:PRK05691 2486 TVVMPLAClapeQLEEGAASVpIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAd 2565
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  861 GQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDE 940
Cdd:PRK05691 2566 GGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDD 2645
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  941 KTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQIRAHSRMAETPEQQL---LCQITASVLKLD 1017
Cdd:PRK05691 2646 EAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELeqqLAQIWREVLNVE 2725
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1018 AIGIDDDFFMTGGDSISAIMLCTQLRQRGYSLRPSDVFQFKTVAAMAPQLTRldeqqaavskplfsadlEQKVQEKYGKN 1097
Cdd:PRK05691 2726 RVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATH-----------------SEAAQAEQGPL 2788
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1098 STILPLLPLQKgMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEepvfiyslhptqaW 1177
Cdd:PRK05691 2789 QGASGLTPIQH-WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGR-------------W 2854
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1178 PVQFCSVTPDLLEQTIQEA-----------LQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDF 1245
Cdd:PRK05691 2855 QAEYRAVTAQELLWQVTVAdfaecaalfadAQRSLDLQQgP--LLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDL 2932
                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1246 IKAYQQ----TNQQLPVLEHS---YETVIKALSGRDH-ETSKVIWQRDLAD 1288
Cdd:PRK05691 2933 QALYRQlsagAEPALPAKTSAfrdWAARLQAYAGSESlREELGWWQAQLGG 2983
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
1546-2031 2.05e-113

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: 370.06  E-value: 2.05e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIGEQKDLAAIVHPSIATFAFNElFDETKVDLSSyktTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDLD-ALAAPAPPPP---VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPsmlAVFENAAT 1785
Cdd:cd12114   157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVP---ALLEMLLD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1786 EiLSSAQRQSLPICRVFCSGE----ALPTALAKSFTEhfsCELHNLYGPTEAAVDVSYMDATlGLHPEESCVAIGYPVWN 1861
Cdd:cd12114   234 V-LEAAQALLPSLRLVLLSGDwiplDLPARLRALAPD---ARLISLGGATEASIWSIYHPID-EVPPDWRSIPYGRPLAN 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1862 TQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPftAGQRMYRTGDIARWHADGSIQYIGRADDQLK 1941
Cdd:cd12114   309 QRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1942 IRGQRIELGEIEQQLRLISGLD-VVVHAIsseQNKANVQLVAYLQTTA---PVDIDQLKKQLAKHLPAYMVPTHYMLVEQ 2017
Cdd:cd12114   387 VRGYRIELGEIEAALQAHPGVArAVVVVL---GDPGGKRLAAFVVPDNdgtPIAPDALRAFLAQTLPAYMIPSRVIALEA 463
                         490
                  ....*....|....
gi 490930577 2018 FPLSHNGKLDRKAL 2031
Cdd:cd12114   464 LPLTANGKVDRAAL 477
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
1533-2032 5.97e-113

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: 368.30  E-value: 5.97e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI 1612
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1613 DLQHPTERIKFMLQDAKSKLVIGEQKDLAaivhpsiatfafnelfdetkvdlssykttvitpqhpaYLIYTSGTTGQPKG 1692
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLTQPENLA-------------------------------------YVIYTSGSTGKPKG 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1693 VMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHF 1772
Cdd:cd17644   124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1773 VPSMLAVFENAAT-EILSSAQRQSLpicrVFCSGEALPTALAKSFTEHFS--CELHNLYGPTEAAVDVSYMDATLGLHPE 1849
Cdd:cd17644   204 PPAYWHLLVLELLlSTIDLPSSLRL----VIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERN 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 ESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF--TAGQRMYRTGDIARWHAD 1927
Cdd:cd17644   280 ITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnsSESERLYKTGDLARYLPD 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1928 GSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYL--QTTAPVDIDQLKKQLAKHLPA 2005
Cdd:cd17644   360 GNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAV-VIVREDQPGNKRLVAYIvpHYEESPSTVELRQFLKAKLPD 438
                         490       500
                  ....*....|....*....|....*..
gi 490930577 2006 YMVPTHYMLVEQFPLSHNGKLDRKALP 2032
Cdd:cd17644   439 YMIPSAFVVLEELPLTPNGKIDRRALP 465
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
487-986 4.87e-112

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: 365.09  E-value: 4.87e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd17643     1 PEAVAVVDED----RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  567 QMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd17643    77 AFILADSGPSLLLT-----------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSH 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  647 GSLLNLilshkptiywpvLEAVnerfpDRPLRAAHT------HSFSFDSSwlqvFWMLWGQELH-----IFDENMRRDAF 715
Cdd:cd17643   116 ANVLAL------------FAAT-----QRWFGFNEDdvwtlfHSYAFDFS----VWEIWGALLHggrlvVVPYEVARSPE 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  716 GLVQEIQQRQIDTLDLPPSFCAQMMTnGLFVENQHHPSL--ILIGGEAAPLAL---WQQ--LNAQPALFahNLYGPTEYT 788
Cdd:cd17643   175 DFARLLRDEGVTVLNQTPSAFYQLVE-AADRDGRDPLALryVIFGGEALEAAMlrpWAGrfGLDRPQLV--NMYGITETT 251
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  789 VD-TFR----AELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF-EHGQ 862
Cdd:cd17643   252 VHvTFRpldaADLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGS 331
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  863 RMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIA-EPINNSHRLLGYCVVKDieldek 941
Cdd:cd17643   332 RMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVrEDEPGDTRLVAYVVADD------ 405
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 490930577  942 TSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17643   406 GAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
AMP-binding pfam00501
AMP-binding enzyme;
1538-1943 1.47e-111

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 362.40  E-value: 1.47e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1538 LREQARITPEQTALS-DENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:pfam00501    1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1617 PTERIKFMLQDAKSKLVIGEQKDLAAIVHP--------------SIATFAFNELFDETKVDLSSYKTTVITPQ--HPAYL 1680
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEalgklevvklvlvlDRDPVLKEEPLPEEAKPADVPPPPPPPPDpdDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1681 IYTSGTTGQPKGVMVSHQAIVNRILWMQSEYP----LSATDTILQKTPCTFDVSV-WEFFWSYLVGARLVIAPIDAHRDP 1755
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1756 LALLSLIQKYQVTTLHFVPSMLAVFENAATeiLSSAQRQSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAV 1835
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGA--PKRALLSSLRL--VLSGGAPLPPELARRFRELFGGALVNGYGLTETTG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1836 DVSYMDatLGLHPEESCVAIGYPVWNTQLYILDQY-LRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVAnpftagQR 1914
Cdd:pfam00501  317 VVTTPL--PLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DG 388
                          410       420
                   ....*....|....*....|....*....
gi 490930577  1915 MYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:pfam00501  389 WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
1542-2031 1.70e-110

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: 360.41  E-value: 1.70e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGEQKDLAaivhpsiatfafnelfdetkvdlssykttvitpqhpaYLIYTSGTTGQPKGVMVSHQAIV 1701
Cdd:cd05945    81 REILDAAKPALLIADGDDNA-------------------------------------YIIFTSGSTGRPKGVQISHDNLV 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1702 NRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPS---MLA 1778
Cdd:cd05945   124 SFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSfaaMCL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1779 VFENAATEILSSAqRQSLpicrvFCsGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGY 1857
Cdd:cd05945   204 LSPTFTPESLPSL-RHFL-----FC-GEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGY 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1858 PVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPftaGQRMYRTGDIARWHADGSIQYIGRAD 1937
Cdd:cd05945   277 AKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLD 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1938 DQLKIRGQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYLQTTAPVDI---DQLKKQLAKHLPAYMVPTHYML 2014
Cdd:cd05945   354 FQVKLNGYRIELEEIEAALRQVPGVKEAV-VVPKYKGEKVTELIAFVVPKPGAEAgltKAIKAELAERLPPYMIPRRFVY 432
                         490
                  ....*....|....*..
gi 490930577 2015 VEQFPLSHNGKLDRKAL 2031
Cdd:cd05945   433 LDELPLNANGKIDRKAL 449
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
1535-2032 4.55e-109

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: 356.09  E-value: 4.55e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1535 QQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDL 1614
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1615 QHPTERIKFMLQDAKSKLVIGEQKDLAaivhpsiatfafnelfdetkvdlssykttvitpqhpaYLIYTSGTTGQPKGVM 1694
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTNPDDLA-------------------------------------YVIYTSGSTGLPKGVM 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTtLHFVP 1774
Cdd:cd17645   124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLP 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1775 SMLAvfenaatEILSSAQRQSLPIcrVFCSGEALPTALAKSFTehfsceLHNLYGPTEAAVdvsyMDATLGLHPEESCVA 1854
Cdd:cd17645   203 TGAA-------EQFMQLDNQSLRV--LLTGGDKLKKIERKGYK------LVNNYGPTENTV----VATSFEIDKPYANIP 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1855 IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIG 1934
Cdd:cd17645   264 IGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLG 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1935 RADDQLKIRGQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYML 2014
Cdd:cd17645   344 RLDQQVKIRGYRIEPGEIEPFLMNHPLIELAA-VLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVH 422
                         490
                  ....*....|....*...
gi 490930577 2015 VEQFPLSHNGKLDRKALP 2032
Cdd:cd17645   423 LKALPLTANGKVDRKALP 440
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
478-987 4.42e-108

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: 354.05  E-value: 4.42e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  478 IFYEQVKKYPERTAIVSgERpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPL 557
Cdd:cd17644     5 LFEEQVERTPDAVAVVF-ED---QQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  558 DLDYPIDRMQMMCEDANpLFVLTTQalaqqlPQNIqqlhldqegvqtqirkqdasdipaenrkfdfqdvAYVIFTSGSTG 637
Cdd:cd17644    81 DPNYPQERLTYILEDAQ-ISVLLTQ------PENL----------------------------------AYVIYTSGSTG 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  638 RPKGVMNTHGSLLNLIlshkptiyWPVLEAVNERFPDRPLRAAhthSFSFDSSWLQVFwMLW--GQELHIFDENMRRDAF 715
Cdd:cd17644   120 KPKGVMIEHQSLVNLS--------HGLIKEYGITSSDRVLQFA---SIAFDVAAEEIY-VTLlsGATLVLRPEEMRSSLE 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  716 GLVQEIQQRQIDTLDLPPSFCAQMMTNGL--FVENQHHPSLILIGGEAAPLALWQQL--NAQPALFAHNLYGPTEYTVDT 791
Cdd:cd17644   188 DFVQYIQQWQLTVLSLPPAYWHLLVLELLlsTIDLPSSLRLVIVGGEAVQPELVRQWqkNVGNFIQLINVYGPTEATIAA 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  792 FRAELK-----QTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEH--GQRM 864
Cdd:cd17644   268 TVCRLTqlterNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERL 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  865 YRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIA-EPINNSHRLLGYcVVKDIELDEKTS 943
Cdd:cd17644   348 YKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVrEDQPGNKRLVAY-IVPHYEESPSTV 426
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 490930577  944 EQlsQQYLSqlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17644   427 EL--RQFLK---AKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1534-2037 6.07e-108

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: 353.35  E-value: 6.07e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHPTERIKFMLQDAKSKLVIGeqkdlaaivhpsiatfafnelfdetkvdlssykttvitpqhpAYLIYTSGTTGQPKGV 1693
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1694 MVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYL-VGARLVIAPidaHRDPLALLSLIQKYQVTTLHF 1772
Cdd:COG0318   119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLlAGATLVLLP---RFDPERVLELIERERVTVLFG 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1773 VPSM---LAVFENAATEILSSAQrqslpicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPE 1849
Cdd:COG0318   196 VPTMlarLLRHPEFARYDLSSLR-------LVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRP 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 ESCvaiGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVanpftagQRMYRTGDIARWHADGS 1929
Cdd:COG0318   269 GSV---GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGY 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVV----HAISSEQNKANVQLVAylqtTAPVDIDQLKKQLAKHLP 2004
Cdd:COG0318   339 LYIVGRKKDMIISGGENVYPAEVEEVLAAHPGvAEAAVvgvpDEKWGERVVAFVVLRP----GAELDAEELRAFLRERLA 414
                         490       500       510
                  ....*....|....*....|....*....|...
gi 490930577 2005 AYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLT 2037
Cdd:COG0318   415 RYKVPRRVEFVDELPRTASGKIDRRALRERYAA 447
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
477-986 1.98e-107

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: 351.62  E-value: 1.98e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  477 DIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:cd12115     3 DLVEAQAARTPDAIALVCGDE----SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  557 LDLDYPIDRMQMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGST 636
Cdd:cd12115    79 LDPAYPPERLRFILEDAQARLVLT-----------------------------------------DPDDLAYVIYTSGST 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  637 GRPKGVMNTHGSLLNLIlshkptiYWpvleaVNERFPDRPLRA--AHThSFSFDSSWLQVFWML-WGQELHIFDenmrrD 713
Cdd:cd12115   118 GRPKGVAIEHRNAAAFL-------QW-----AAAAFSAEELAGvlAST-SICFDLSVFELFGPLaTGGKVVLAD-----N 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  714 AFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQhhpSLILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTV-DT 791
Cdd:cd12115   180 VLALPDLPAAAEVTLINTVPSAAAELLRHDALPASV---RVVNLAGEPLPRDLVQRLYARlQVERVVNLYGPSEDTTyST 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  792 FRAELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDL 870
Cdd:cd12115   257 VAPVPPGASGEVsIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDL 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  871 VRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIA-EPINNSHRLLGYCVVKDieldekTSEQLSQQ 949
Cdd:cd12115   337 VRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAiGDAAGERRLVAYIVAEP------GAAGLVED 410
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 490930577  950 YLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd12115   411 LRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
487-987 2.55e-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: 351.29  E-value: 2.55e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd17649     1 PDAVALVFGD----QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  567 QMMCEDANPLFVLTtqalaqQLPQNIqqlhldqegvqtqirkqdasdipaenrkfdfqdvAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd17649    77 RYMLEDSGAGLLLT------HHPRQL----------------------------------AYVIYTSGSTGTPKGVAVSH 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  647 GSLLNLIlshkptiywpvlEAVNERFP----DRPLRAAhthSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAFGLVQEI 721
Cdd:cd17649   117 GPLAAHC------------QATAERYGltpgDRELQFA---SFNFDGAHEQLLPpLICGACVVLRPDELWASADELAEMV 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  722 QQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFAhNLYGPTEYTV-----DTFRA 794
Cdd:cd17649   182 RELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLrlYIFGGEALSPELLRRWLKAPVRLF-NAYGPTEATVtplvwKCEAG 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  795 ELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRW 873
Cdd:cd17649   261 AARAGASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARW 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  874 NSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEKTSEQLSQqylsQ 953
Cdd:cd17649   341 RDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRT----A 416
                         490       500       510
                  ....*....|....*....|....*....|....
gi 490930577  954 LRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17649   417 LRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
1545-2032 6.73e-105

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: 345.61  E-value: 6.73e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1545 TPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFM 1624
Cdd:cd17656     1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1625 LQDAKSKLVIGEQKdlaaivHPSIATFAFN----ELFDETKVDLSSYkTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAI 1700
Cdd:cd17656    81 MLDSGVRVVLTQRH------LKSKLSFNKStillEDPSISQEDTSNI-DYINNSDDLLYIIYTSGTTGKPKGVQLEHKNM 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLhFVPSMLAVF 1780
Cdd:cd17656   154 VNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1781 enaateILSSAQ-RQSLPIC--RVFCSGEALptALAKSFTEHF---SCELHNLYGPTEAAVDVSYMdatlgLHPEESCV- 1853
Cdd:cd17656   233 ------IFSEREfINRFPTCvkHIITAGEQL--VITNEFKEMLhehNVHLHNHYGPSETHVVTTYT-----INPEAEIPe 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1854 --AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQ 1931
Cdd:cd17656   300 lpPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIE 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1932 YIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVHAISSEQNKANvQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTH 2011
Cdd:cd17656   380 FLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEK-YLCAYFVMEQELNISQLREYLAKQLPEYMIPSF 458
                         490       500
                  ....*....|....*....|.
gi 490930577 2012 YMLVEQFPLSHNGKLDRKALP 2032
Cdd:cd17656   459 FVPLDQLPLTPNGKVDRKALP 479
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
1546-2032 7.06e-102

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: 335.91  E-value: 7.06e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQ-RAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFM 1624
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLsVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1625 LQDAKSKLVIGEQKDLAaivhpsiatfafnelfdetkvdlssykttvitpqhpaYLIYTSGTTGQPKGVMVSHQAIVNRI 1704
Cdd:cd17648    81 LEDTGARVVITNSTDLA-------------------------------------YAIYTSGTTGKPKGVLVEHGSVVNLR 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1705 LWMQSEYPLSATDT--ILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFEn 1782
Cdd:cd17648   124 TSLSERYFGRDNGDeaVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYD- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1783 aateiLSSaqRQSLPicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVdvsYMDATLGLHPEESCVAIGYPVWNT 1862
Cdd:cd17648   203 -----LAR--LPHLK--RVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTV---TNHKRFFPGDQRFDKSLGRPVRNT 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1863 QLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQ--------RMYRTGDIARWHADGSIQYIG 1934
Cdd:cd17648   271 KCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLG 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1935 RADDQLKIRGQRIELGEIEQQLRLISGLD--VVVHAISSEQNKANVQ--LVA-YLQTTAPVDIDQLKKQLAKHLPAYMVP 2009
Cdd:cd17648   351 RNDFQVKIRGQRIEPGEVEAALASYPGVRecAVVAKEDASQAQSRIQkyLVGyYLPEPGHVPESDLLSFLRAKLPRYMVP 430
                         490       500
                  ....*....|....*....|...
gi 490930577 2010 THYMLVEQFPLSHNGKLDRKALP 2032
Cdd:cd17648   431 ARLVRLEGIPVTINGKLDVRALP 453
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
487-986 7.61e-102

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: 336.55  E-value: 7.61e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd12114     1 PDATAVICGD----GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  567 QMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQEgvqtqirKQDASDIPAEnRKFDFQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd12114    77 EAILADAGARLVLTDGPDAQLDVAVFDVLILDLD-------ALAAPAPPPP-VDVAPDDLAYVIFTSGSTGTPKGVMISH 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  647 GSLLNLIlshkptiywpvlEAVNERF----PDRPLRAAhthSFSFDSSWLQVFWML-WGQELHIFDENMRRDAFGLVQEI 721
Cdd:cd12114   149 RAALNTI------------LDINRRFavgpDDRVLALS---SLSFDLSVYDIFGALsAGATLVLPDEARRRDPAHWAELI 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  722 QQRQIDTLDLPPSFcAQMMTNGLFVENQHHPSL--ILIGGEAAPLAL---WQQLNAQPALFAhnLYGPTE-------YTV 789
Cdd:cd12114   214 ERHGVTLWNSVPAL-LEMLLDVLEAAQALLPSLrlVLLSGDWIPLDLparLRALAPDARLIS--LGGATEasiwsiyHPI 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  790 DTFRAELKqtarpVI--GNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPfeHGQRMYRT 867
Cdd:cd12114   291 DEVPPDWR-----SIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRT 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  868 GDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYcVVKDIELDEKTSEQLS 947
Cdd:cd12114   364 GDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAF-VVPDNDGTPIAPDALR 442
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 490930577  948 QqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd12114   443 A----FLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
487-987 1.95e-94

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: 315.18  E-value: 1.95e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd17656     2 PDAVAVVFEN----QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  567 QMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQEgvqtQIRKQDASDIPAENRKfdfQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd17656    78 IYIMLDSGVRVVLTQRHLKSKLSFNKSTILLEDP----SISQEDTSNIDYINNS---DDLLYIIYTSGTTGKPKGVQLEH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  647 GSLLNLILSHKptiywpvlEAVNERFPDRPLRAAhthSFSFDSSWLQVF-WMLWGQELHIFDENMRRDAFGLVQEIQQRQ 725
Cdd:cd17656   151 KNMVNLLHFER--------EKTNINFSDKVLQFA---TCSFDVCYQEIFsTLLSGGTLYIIREETKRDVEQLFDLVKRHN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  726 IDTLDLPPSFCAQmmtngLFVENQHHPSL------ILIGGEAAPLA-LWQQLNAQPALFAHNLYGPTE---YTVDTFRAE 795
Cdd:cd17656   220 IEVVFLPVAFLKF-----IFSEREFINRFptcvkhIITAGEQLVITnEFKEMLHEHNVHLHNHYGPSEthvVTTYTINPE 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  796 LKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNS 875
Cdd:cd17656   295 AEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLP 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  876 AGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIA-EPINNSHRLLGYCVVkdieLDEKTSEQLSqqylSQL 954
Cdd:cd17656   375 DGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDkADDKGEKYLCAYFVM----EQELNISQLR----EYL 446
                         490       500       510
                  ....*....|....*....|....*....|...
gi 490930577  955 RQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17656   447 AKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
478-987 3.02e-94

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: 313.34  E-value: 3.02e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  478 IFYEQVKKYPERTAIVSgerpNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPL 557
Cdd:cd17645     3 LFEEQVERTPDHVAVVD----RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  558 DLDYPIDRMQMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGSTG 637
Cdd:cd17645    79 DPDYPGERIAYMLADSSAKILLT-----------------------------------------NPDDLAYVIYTSGSTG 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  638 RPKGVMNTHGSLLNLILSHKPtiYWPVLEAvnerfpDRPLRAAhthSFSFDSSWLQVF-WMLWGQELHIFDENMRRDAFG 716
Cdd:cd17645   118 LPKGVMIEHHNLVNLCEWHRP--YFGVTPA------DKSLVYA---SFSFDASAWEIFpHLTAGAALHVVPSERRLDLDA 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  717 LVQEIQQRQIDTLDLPPSFCAQMMTnglfVENqHHPSLILIGGEAAplalwQQLNAQPALFAHNlYGPTEYTVDTFRAEL 796
Cdd:cd17645   187 LNDYFNQEGITISFLPTGAAEQFMQ----LDN-QSLRVLLTGGDKL-----KKIERKGYKLVNN-YGPTENTVVATSFEI 255
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  797 -KQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNS 875
Cdd:cd17645   256 dKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLP 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  876 AGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIA-EPINNSHRLLGYCVVKdielDEKTSEQLSqqylSQL 954
Cdd:cd17645   336 DGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAkEDADGRKYLVAYVTAP----EEIPHEELR----EWL 407
                         490       500       510
                  ....*....|....*....|....*....|...
gi 490930577  955 RQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17645   408 KNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
475-986 8.45e-94

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: 313.71  E-value: 8.45e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  475 VLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASF 554
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWD----GSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  555 LPLDLDYPIDRMQMMCEDANPLFVLTTQAlaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfQDVAYVIFTSG 634
Cdd:cd05918    77 VPLDPSHPLQRLQEILQDTGAKVVLTSSP----------------------------------------SDAAYVIFTSG 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  635 STGRPKGVMNTHGSLLNLILSHKPtiywpvLEAVNERfpDRPLRAAhthSFSFDSSWLQVFWMLwgqelhIF-------- 706
Cdd:cd05918   117 STGKPKGVVIEHRALSTSALAHGR------ALGLTSE--SRVLQFA---SYTFDVSILEIFTTL------AAggclcips 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  707 DENMRRDafgLVQEIQQRQIDTLDLPPSFcAQMMTNGLFvenqhhPSL--ILIGGEAAPLALWQQLNAQPALFahNLYGP 784
Cdd:cd05918   180 EEDRLND---LAGFINRLRVTWAFLTPSV-ARLLDPEDV------PSLrtLVLGGEALTQSDVDTWADRVRLI--NAYGP 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  785 TEYTVDTFRAELKQTARP-VIGNPIGNTqAYVLD--RHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANP---- 857
Cdd:cd05918   248 AECTIAATVSPVVPSTDPrNIGRPLGAT-CWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlk 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  858 ---FEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALS----ILTNVESAVVIAEPINNSHRLLGY 930
Cdd:cd05918   327 qegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRqslpGAKEVVVEVVKPKDGSSSPQLVAF 406
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577  931 CVVKDIELDEKTSEQLSQQYLSQ-----------LRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05918   407 VVLDGSSSGSGDGDSLFLEPSDEfralvaelrskLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
487-986 2.69e-92

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: 307.86  E-value: 2.69e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd17650     1 PDAIAVSDATR----QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  567 QMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd17650    77 QYMLEDSGAKLLLT-----------------------------------------QPEDLAYVIYTSGTTGKPKGVMVEH 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  647 GSLLNLILShkptiyWPVLEAVnERFPDRPLRAAhthSFSFDsswlqVFW------MLWGQELHIFDENMRRDAFGLVQE 720
Cdd:cd17650   116 RNVAHAAHA------WRREYEL-DSFPVRLLQMA---SFSFD-----VFAgdfarsLLNGGTLVICPDEVKLDPAALYDL 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  721 IQQRQIDTLDLPPSFCAQMMTngLFVENQHHPS---LILIGGEAAPLALWQQLNAQpaLFAH----NLYGPTEYTVDTF- 792
Cdd:cd17650   181 ILKSRITLMESTPALIRPVMA--YVYRNGLDLSamrLLIVGSDGCKAQDFKTLAAR--FGQGmriiNSYGVTEATIDSTy 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  793 ----RAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTG 868
Cdd:cd17650   257 yeegRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTG 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  869 DLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYCVVkdielDEKTSEQLS 947
Cdd:cd17650   337 DLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEaRLCAYVVA-----AATLNTAEL 411
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 490930577  948 QQYLSqlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17650   412 RAFLA---KELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
487-987 5.96e-89

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: 298.54  E-value: 5.96e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGA-RKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDR 565
Cdd:cd17648     1 PDRVAVVYGD----KRLTYRELNERANRLAHYLLSVAEiRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDER 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  566 MQMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGSTGRPKGVMNT 645
Cdd:cd17648    77 IQFILEDTGARVVIT-----------------------------------------NSTDLAYAIYTSGTTGKPKGVLVE 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  646 HGSLLNLILShkptiywpvleaVNERFPDRPLRAAHTHSFS---FDSSWLQ-VFWMLWGQELHIFDENMRRDAFGLVQEI 721
Cdd:cd17648   116 HGSVVNLRTS------------LSERYFGRDNGDEAVLFFSnyvFDFFVEQmTLALLNGQKLVVPPDEMRFDPDRFYAYI 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  722 QQRQIDTLDLPPSFCAQmmtnglfVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQT 799
Cdd:cd17648   184 NREKVTYLSGTPSVLQQ-------YDLARLPHLkrVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGD 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  800 AR--PVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQ--------RMYRTGD 869
Cdd:cd17648   257 QRfdKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGD 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  870 LVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH------RLLGYCVVKDIELDEkts 943
Cdd:cd17648   337 LVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAqsriqkYLVGYYLPEPGHVPE--- 413
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 490930577  944 eqlsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17648   414 ----SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
1100-1501 4.86e-88

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: 294.88  E-value: 4.86e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIysLHPTQAWP 1178
Cdd:cd19543     1 IYPLSPMQEGMLFHSLLDPGSGaYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQV--VLKDRKLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1179 VQF---CSVTPDLLEQTIQEAL----QQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ- 1250
Cdd:cd19543    79 WREldlSHLSEAEQEAELEALAeedrERGFDLARA-PLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAa 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1251 QTNQQLPVLE--HSYETVIKALSGRDHETSKVIWQRDLADL--QPLILFNQA-----QQAVQETSYRLSAELGAKLQHKL 1321
Cdd:cd19543   158 LGEGQPPSLPpvRPYRDYIAWLQRQDKEAAEAYWREYLAGFeePTPLPKELPadadgSYEPGEVSFELSAELTARLQELA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1322 RQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVE 1401
Cdd:cd19543   238 RQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1402 HLEHDGLGLSAIQQLIAQG-NLFDSLLVVENYPDNQYLQQKLGDAA--ISKLTNRGYSHYPLALLVIPDHQIELLLE-QR 1477
Cdd:cd19543   318 LREHEYVPLYEIQAWSEGKqALFDHLLVFENYPVDESLEEEQDEDGlrITDVSAEEQTNYPLTVVAIPGEELTIKLSyDA 397
                         410       420
                  ....*....|....*....|....*.
gi 490930577 1478 GVIDQP--EHFLERMIQLIEIALNEP 1501
Cdd:cd19543   398 EVFDEAtiERLLGHLRRVLEQVAANP 423
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
483-986 1.50e-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: 294.15  E-value: 1.50e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  483 VKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYP 562
Cdd:cd05945     1 AAANPDRPAVVEGGRT----LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  563 IDRMQMMCEDANPLFVLTTQAlaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfqDVAYVIFTSGSTGRPKGV 642
Cdd:cd05945    77 AERIREILDAAKPALLIADGD-----------------------------------------DNAYIIFTSGSTGRPKGV 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  643 MNTHGSLLNLIlshkptiywpvlEAVNERFPDRP-LRAAHTHSFSFDSSWLQVF--WMLwGQELHIFDENMRRDAFGLVQ 719
Cdd:cd05945   116 QISHDNLVSFT------------NWMLSDFPLGPgDVFLNQAPFSFDLSVMDLYpaLAS-GATLVPVPRDATADPKQLFR 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  720 EIQQRQIDTLDLPPSFCAQMMTNGLFVEnQHHPSL--ILIGGEAAPLALWQQL-NAQPALFAHNLYGPTEYTVDT----F 792
Cdd:cd05945   183 FLAEHGITVWVSTPSFAAMCLLSPTFTP-ESLPSLrhFLFCGEVLPHKTARALqQRFPDARIYNTYGPTEATVAVtyieV 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  793 RAELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPfehGQRMYRTGDLV 871
Cdd:cd05945   262 TPEVLDGYDRLpIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLV 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  872 RWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYcvvkdIELDEKTSEQLSQQY 950
Cdd:cd05945   339 RLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVtELIAF-----VVPKPGAEAGLTKAI 413
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 490930577  951 LSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05945   414 KAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
477-986 1.51e-87

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: 293.83  E-value: 1.51e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  477 DIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLG----GSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  557 LDLDYPIDRMQMMCEDANPLFVLTTqalaqqlpqniqqlhldqegvqtqirkqDASDipaenrkfdfqDVAYVIFTSGST 636
Cdd:cd17653    77 LDAKLPSARIQAILRTSGATLLLTT----------------------------DSPD-----------DLAYIIFTSGST 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  637 GRPKGVMNTHGSLLNLilshkptiywpvLEAVNERFPDRP-LRAAHTHSFSFDSSWLQVFWML-WGQELHIFDENmrrDA 714
Cdd:cd17653   118 GIPKGVMVPHRGVLNY------------VSQPPARLDVGPgSRVAQVLSIAFDACIGEIFSTLcNGGTLVLADPS---DP 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  715 FGLVQeiqqRQIDTLDLPPSFCAQmmtnglfVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFahNLYGPTEYTVDTF 792
Cdd:cd17653   183 FAHVA----RTVDALMSTPSILST-------LSPQDFPNLktIFLGGEAVPPSLLDRWSPGRRLY--NAYGPTECTISST 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  793 RAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVR 872
Cdd:cd17653   250 MTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGR 329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  873 WNSAGKLEFMGRCDDQIKIRGYRVEIGEVEN-ALSILTNVESAVVIAepINNshRLLGYCVVKDIELDEKTSEqlsqqyl 951
Cdd:cd17653   330 WTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIV--VNG--RLVAFVTPETVDVDGLRSE------- 398
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 490930577  952 sqLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17653   399 --LAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
AMP-binding pfam00501
AMP-binding enzyme;
479-892 5.65e-86

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 288.44  E-value: 5.65e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   479 FYEQVKKYPERTAIVSGERpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLD 558
Cdd:pfam00501    1 LERQAARTPDKTALEVGEG---RRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   559 LDYPIDRMQMMCEDANPLFVLTTQAL--------AQQLPQNIQQLHLDQEGVQT----QIRKQDASDIPAENRKFDFQDV 626
Cdd:pfam00501   78 PRLPAEELAYILEDSGAKVLITDDALkleelleaLGKLEVVKLVLVLDRDPVLKeeplPEEAKPADVPPPPPPPPDPDDL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   627 AYVIFTSGSTGRPKGVMNTHGSLLNLILSHKptIYWPVLEAVNERfpdrpLRAAHTHSFSFDSSWLQVFW--MLWGQELH 704
Cdd:pfam00501  158 AYIIYTSGTTGKPKGVMLTHRNLVANVLSIK--RVRPRGFGLGPD-----DRVLSTLPLFHDFGLSLGLLgpLLAGATVV 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   705 IFDENMRRDAFGLVQEIQQRQIDTLDLPPSFcAQMMTNGLFVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFAHNLY 782
Cdd:pfam00501  231 LPPGFPALDPAALLELIERYKVTVLYGVPTL-LNMLLEAGAPKRALLSSLrlVLSGGAPLPPELARRFRELFGGALVNGY 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   783 GPTEYTVDT---FRAELKQTARPVIGNPIGNTQAYVLD-RHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVAnpf 858
Cdd:pfam00501  310 GLTETTGVVttpLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE--- 386
                          410       420       430
                   ....*....|....*....|....*....|....
gi 490930577   859 ehgQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIR 892
Cdd:pfam00501  387 ---DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
PRK05691 PRK05691
peptide synthase; Validated
478-1075 2.78e-79

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 294.00  E-value: 2.78e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  478 IFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPL 557
Cdd:PRK05691 3725 LFEAQVAAHPQRIAASCLD----QQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPL 3800
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  558 DLDYPIDRMQMMCE-DANPLFVLTTQALAQ------QLPQNIQQLHLDQEGVQtqirkqdASDIPAEN--RKFDFQDVAY 628
Cdd:PRK05691 3801 DPGLPAQRLQRIIElSRTPVLVCSAACREQaralldELGCANRPRLLVWEEVQ-------AGEVASHNpgIYSGPDNLAY 3873
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  629 VIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYWPVLEAVnerfpdrplraAHTHSFSFD-SSWLQVFWMLWGQELHIFD 707
Cdd:PRK05691 3874 VIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVI-----------AQTASQSFDiSVWQFLAAPLFGARVEIVP 3942
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  708 ENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNglfvENQHHPSL--ILIGGEAAPLALWQQ-LNAQPALFAHNLYGP 784
Cdd:PRK05691 3943 NAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAE----DRQALDGLrwMLPTGEAMPPELARQwLQRYPQIGLVNAYGP 4018
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  785 TEYTVDT--FRAELKQTARPV--IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF-E 859
Cdd:PRK05691 4019 AECSDDVafFRVDLASTRGSYlpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgA 4098
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  860 HGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIAEPINNSHrLLGYCVVKDIEL 938
Cdd:PRK05691 4099 PGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVrEAAVAVQEGVNGKH-LVGYLVPHQTVL 4177
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  939 DEktsEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQI-RAHSRMAETPE---QQLLCQITASVL 1014
Cdd:PRK05691 4178 AQ---GALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIgQLQSQAYLAPRnelEQTLATIWADVL 4254
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1015 KLDAIGIDDDFFMTGGDSISAIMLCTQLR---QRGYSLRPsdVFQFKTVAAMAPQL-----TRLDEQQA 1075
Cdd:PRK05691 4255 KVERVGVHDNFFELGGHSLLATQIASRVQkalQRNVPLRA--MFECSTVEELAEYIeglagSAIDEQKV 4321
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
1529-2377 3.47e-78

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 279.28  E-value: 3.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1529 VRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAA 1608
Cdd:COG3319     1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1609 YLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHPSIATFAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGTTG 1688
Cdd:COG3319    81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1689 QPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVT 1768
Cdd:COG3319   161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1769 TLHFVPSMLAVFENAATEILSSAQRQSLPICRVFCSGEALPTALAksftehfscELHNLYGPTEAAVDVSYMDATLGLHP 1848
Cdd:COG3319   241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAA---------AAALAAGGTATTAAVTTTAAAAAPGV 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1849 EESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFT--AGQRMYRTGDIARWHA 1926
Cdd:COG3319   312 AGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGagARGRLRRGGDRGRRLG 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1927 DGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAY 2006
Cdd:COG3319   392 GGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPP 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2007 MVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSAFEHELTRIFQQILNTDqnIGVNEDFFAIGGHSILVMK 2086
Cdd:COG3319   472 LPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGL--VGDDDDFFGGGGGSLLALL 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2087 LAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQERLAEVEQtgmqPILPIRSGSGHPLFCFYPGSGSAWQYTVLNRYLH 2166
Cdd:COG3319   550 LLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSP----LVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALG 625
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2167 SDLPIIGLQSPRPDGLLANSTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVAAKLTEQGEKVDYLGLLDTYP- 2245
Cdd:COG3319   626 PDRPVYGLQAPGLDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLDSYAp 705
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2246 ------------------AEIHQWLDLSVEEMNAEAEQEQLQFFNDILADADSALSEETRRLqEDIFANYRDAVRLLKPY 2307
Cdd:COG3319   706 galarldeaellaallrdLARGVDLPLDAEELRALDPEERLARLLERLREAGLPAGLDAERL-RRLLRVFRANLRALRRY 784
                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 2308 KMPHFDGELHLVVAEKDLLP-YIQPEQQWSPLVK-KLNIVRLsEADHTDILSPQQLETLGPILNRMICQARG 2377
Cdd:COG3319   785 RPRPYDGPVLLFRAEEDPPGrADDPALGWRPLVAgGLEVHDV-PGDHFSMLREPHVAELAAALRAALAAAEA 855
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
18-439 8.98e-77

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: 261.92  E-value: 8.98e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   18 RFELASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELNNQVQFQIEE 97
Cdd:cd19533     1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   98 FDF-CHLTPKKAQQrlwDWMPSDRQCAKSLKAGEtqLFRQVLFTT-HDKVYWYQRYHHIMLDGFSMINLTKRIVELYQQL 175
Cdd:cd19533    81 IDLsGDPDPEGAAQ---QWMQEDLRKPLPLDNDP--LFRHALFTLgDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  176 QEGKDLSVSPFIGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHhlAAKTTATFVKHQLRFSTGILEQIQA 255
Cdd:cd19533   156 LKGRPAPPAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARR--APGRSLAFLRRTAELPPELTRTLLE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  256 LAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLRE 335
Cdd:cd19533   234 AAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRS 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  336 IRPHQKYDAEQILRDLNSIDIHERMYGPILNYKAFDQDLVIDGEKVKTHHISTGPIDDFE-FSFIVQDH-ELIIELRADS 413
Cdd:cd19533   314 LLRHQRYRYEDLRRDLGLTGELHPLFGPTVNYMPFDYGLDFGGVVGLTHNLSSGPTNDLSiFVYDRDDEsGLRIDFDANP 393
                         410       420
                  ....*....|....*....|....*.
gi 490930577  414 QRYTQDELFNHGQRLTLLLEQALIRP 439
Cdd:cd19533   394 ALYSGEDLARHQERLLRLLEEAAADP 419
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
475-986 3.32e-76

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: 261.67  E-value: 3.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  475 VLDIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASF 554
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGR----RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  555 LPLDLDYPIDRMQMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfqdvAYVIFTSG 634
Cdd:COG0318    77 VPLNPRLTAEELAYILEDSGARALVT----------------------------------------------ALILYTSG 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  635 STGRPKGVMNTHGSLLNlilshkptiywpVLEAVNERFPDRP-LRAAHTHSFSFDSSWLQVFWM--LWGQELHIFDenmR 711
Cdd:COG0318   111 TTGRPKGVMLTHRNLLA------------NAAAIAAALGLTPgDVVLVALPLFHVFGLTVGLLAplLAGATLVLLP---R 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  712 RDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFvENQHHPSL--ILIGGEAAPLALWQQLNAQ--PALFahNLYGPTE- 786
Cdd:COG0318   176 FDPERVLELIERERVTVLFGVPTMLARLLRHPEF-ARYDLSSLrlVVSGGAPLPPELLERFEERfgVRIV--EGYGLTEt 252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  787 YTVDTFRAELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFvanpfEHGqrMY 865
Cdd:COG0318   253 SPVVTVNPEDPGERRPGsVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-----RDG--WL 325
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  866 RTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYCVVKD-IELDEkts 943
Cdd:COG0318   326 RTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGeRVVAFVVLRPgAELDA--- 402
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 490930577  944 EQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:COG0318   403 EEL----RAFLRERLARYKVPRRVEFVDELPRTASGKIDRRAL 441
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1542-2031 4.93e-68

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 239.41  E-value: 4.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:PRK04813   12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGeqkdlaaiVHPSIATFAFNELFDETKVDLSSYKTTVITPQHP------AYLIYTSGTTGQPKGVMV 1695
Cdd:PRK04813   92 EMIIEVAKPSLIIA--------TEELPLEILGIPVITLDELKDIFATGNPYDFDHAvkgddnYYIIFTSGTTGKPKGVQI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1696 SHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPS 1775
Cdd:PRK04813  164 SHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPS 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 M--LAVFENAATEilssaqrQSLPICRVF--CsGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEE 1850
Cdd:PRK04813  244 FadMCLLDPSFNE-------EHLPNLTHFlfC-GEELPHKTAKKLLERFpSATIYNTYGPTEATVAVTSIEITDEMLDQY 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1851 SCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFvanpFT-AGQRMYRTGDIARWhADGS 1929
Cdd:PRK04813  316 KRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTfDGQPAYHTGDAGYL-EDGL 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYLQTTAPvDID-------QLKKQLAKH 2002
Cdd:PRK04813  391 LFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAV-VVPYNKDHKVQYLIAYVVPKEE-DFErefeltkAIKKELKER 468
                         490       500
                  ....*....|....*....|....*....
gi 490930577 2003 LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK04813  469 LMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
1676-2027 2.47e-64

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: 222.93  E-value: 2.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1676 HPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPidaHRDP 1755
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1756 LALLSLIQKYQVTTLHFVPSM---LAVFENAATEILSSAQrqslpicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTE 1832
Cdd:cd04433    78 EAALELIEREKVTILLGVPTLlarLLKAPESAGYDLSSLR-------ALVSGGAPLPPELLERFEEAPGIKLVNGYGLTE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1833 AAVDVSYMDATLGlhpEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANpftag 1912
Cdd:cd04433   151 TGGTVATGPPDDD---ARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG----- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1913 qrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVD 1991
Cdd:cd04433   223 --WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGvAEAAVVGVPDPEWGERVVAVVVLRPGADLD 300
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 490930577 1992 IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:cd04433   301 AEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
1534-2031 1.11e-59

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: 213.96  E-value: 1.11e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:cd05936     1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHPTERIKFMLQDAKSKLVIgeqkdlaaivhpsiATFAFNELFdetKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGV 1693
Cdd:cd05936    81 PLYTPRELEHILNDSGAKALI--------------VAVSFTDLL---AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1694 MVSHQAIVNRIL----WMqsEYPLSATDTILQKTPctfdvsvweFFWSY----------LVGARLVIAPidahR-DPLAL 1758
Cdd:cd05936   144 MLTHRNLVANALqikaWL--EDLLEGDDVVLAALP---------LFHVFgltvalllplALGATIVLIP----RfRPIGV 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1759 LSLIQKYQVTTLHFVPSMLAVFENAatEILSSAQRQSLPICrvFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAvdvs 1838
Cdd:cd05936   209 LKEIRKHRVTIFPGVPTMYIALLNA--PEFKKRDFSSLRLC--ISGGAPLPVEVAERFEELTGVPIVEGYGLTETS---- 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1839 ymDATLGLHPEESCVA--IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmy 1916
Cdd:cd05936   281 --PVVAVNPLDGPRKPgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL------- 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1917 RTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL-RLISGLDVVV----HAISSEQNKANVQlvayLQTTAPVD 1991
Cdd:cd05936   352 RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLyEHPAVAEAAVvgvpDPYSGEAVKAFVV----LKEGASLT 427
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 490930577 1992 IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05936   428 EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
473-986 4.66e-58

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 210.52  E-value: 4.66e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  473 NNVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQT--VIAGAipRSIDSVVVMLSVLNS 550
Cdd:PRK04813    2 MDIIETIEEFAQTQPDFPAYDYLG----EKLTYGQLKEDSDALAAFIDSLKLPDKSpiIVFGH--MSPEMLATFLGAVKA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  551 GASFLPLDLDYPIDRMQMMCEDANPLFVLttqalaqqlpqNIQQLHLDQEGVQTqIRKQDASDIPAENRKFDFQ------ 624
Cdd:PRK04813   76 GHAYIPVDVSSPAERIEMIIEVAKPSLII-----------ATEELPLEILGIPV-ITLDELKDIFATGNPYDFDhavkgd 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSLL---NLILSHKPTiywpvleavnerfPDRP--LRAAhthSFSFDsswLQVfwMLW 699
Cdd:PRK04813  144 DNYYIIFTSGTTGKPKGVQISHDNLVsftNWMLEDFAL-------------PEGPqfLNQA---PYSFD---LSV--MDL 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  700 ------GQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFcAQM-MTNGLFVEnQHHPSL--ILIGGEAAPLALWQQL 770
Cdd:PRK04813  203 yptlasGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSF-ADMcLLDPSFNE-EHLPNLthFLFCGEELPHKTAKKL 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  771 -NAQPALFAHNLYGPTEYTVDTFRAE-----LKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLG 844
Cdd:PRK04813  281 lERFPSATIYNTYGPTEATVAVTSIEitdemLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLN 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  845 RADLSAARFVanpFEHGQRMYRTGDLVRWNSaGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIaePINNS 924
Cdd:PRK04813  361 NPEKTAEAFF---TFDGQPAYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV--PYNKD 434
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577  925 HR---LLGYCVVKDIELDEktSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK04813  435 HKvqyLIAYVVPKEEDFER--EFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
1570-2130 1.46e-55

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: 214.54  E-value: 1.46e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKdlAAIVHPSIA 1649
Cdd:TIGR03443  283 LAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEK--AGTLDQLVR 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1650 TFAFNELFDETKV-------------------------DLSSYKTT----VITPQHPAYLIYTSGTTGQPKGVMVSHQAI 1700
Cdd:TIGR03443  361 DYIDKELELRTEIpalalqddgslvggsleggetdvlaPYQALKDTptgvVVGPDSNPTLSFTSGSEGIPKGVLGRHFSL 440
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1701 VNRILWMQSEYPLSATD--TILQ---KTPCTFDVsvwefFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPS 1775
Cdd:TIGR03443  441 AYYFPWMAKRFGLSENDkfTMLSgiaHDPIQRDM-----FTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPA 515
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1776 MLAVFENAATeilssAQRQSLPicRVFCSGEALPT-------ALAKSftehfsCELHNLYGPTEAAVDVSYM-------D 1841
Cdd:TIGR03443  516 MGQLLSAQAT-----TPIPSLH--HAFFVGDILTKrdclrlqTLAEN------VCIVNMYGTTETQRAVSYFeipsrssD 582
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1842 ATLgLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVD--GELYLAGHQLAMGYLHRADLTASRFVAN------------ 1907
Cdd:TIGR03443  583 STF-LKNLKDVMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNwfvdpshwidld 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1908 --------PFTAG--QRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLR-------------------- 1957
Cdd:TIGR03443  662 kennkperEFWLGprDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSqhplvrenvtlvrrdkdeep 741
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1958 -LISGLDVVVHAISSEQNKANV-------QLVAYLQTTAPVdIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRK 2029
Cdd:TIGR03443  742 tLVSYIVPQDKSDELEEFKSEVddeessdPVVKGLIKYRKL-IKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKP 820
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  2030 ALPQP-----HLTPSNTEKQYATSAF---EHELTRIFQQIL-NTDQNIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIP 2100
Cdd:TIGR03443  821 ALPFPdtaqlAAVAKNRSASAADEEFtetEREIRDLWLELLpNRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELP 900
                          650       660       670
                   ....*....|....*....|....*....|
gi 490930577  2101 IGQLMSHVTIQRLAALLltqERLAEVEQTG 2130
Cdd:TIGR03443  901 LGLIFKSPTIKGFAKEV---DRLKKGEELA 927
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1537-2031 1.08e-54

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 202.26  E-value: 1.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTAL-----SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLP 1611
Cdd:COG0365    14 CLDRHAEGRGDKVALiwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1612 I--DLqhPTERIKFMLQDAKSKLVI--------GEQKDLAAIVH------PSIAT----------------FAFNELFDE 1659
Cdd:COG0365    94 VfpGF--GAEALADRIEDAEAKVLItadgglrgGKVIDLKEKVDealeelPSLEHvivvgrtgadvpmegdLDWDELLAA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1660 TKVDLSSYKTTvitPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILW-MQSEYPLSATDTILqktpCTFDVSvWEFFWSY 1738
Cdd:COG0365   172 ASAEFEPEPTD---ADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATtAKYVLDLKPGDVFW----CTADIG-WATGHSY 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1739 LV------GARLVI---APIdaHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLpicRVFCS-GEAL 1808
Cdd:COG0365   244 IVygpllnGATVVLyegRPD--FPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSL---RLLGSaGEPL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1809 PTALAKSFTEHFSCELHNLYGPTEAavdVSYMDATLGLHPeescV---AIGYPVWNTQLYILDQYLRPVPVGVDGELYLA 1885
Cdd:COG0365   319 NPEVWEWWYEAVGVPIVDGWGQTET---GGIFISNLPGLP----VkpgSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1886 GHQLAM--GYLHRADLTASRFvanpFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-L 1962
Cdd:COG0365   392 GPWPGMfrGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAvA 467
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490930577 1963 DVVVhaISSEQNKANVQLVAYLQTTAPVD-----IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:COG0365   468 EAAV--VGVPDEIRGQVVKAFVVLKPGVEpsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
1533-2031 7.27e-54

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 198.47  E-value: 7.27e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1533 TLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI 1612
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1613 DLQHPTERIKFMLQDAKSKLVI-------------GEQKDLAAIVHPSIATFAFNELFDETKVDLSSYKTTVIT-PQHP- 1677
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVtsserldllhpalPGCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGDAdPPHPv 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1678 -----AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAH 1752
Cdd:TIGR03098  161 idsdmAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1753 RDplaLLSLIQKYQVTTLHFVPSMLA-VFENAATEILSSAQRqslpicRVFCSGEALPTALAKSFTEHFS-CELHNLYGP 1830
Cdd:TIGR03098  241 RD---VLKALEKHGITGLAAVPPLWAqLAQLDWPESAAPSLR------YLTNSGGAMPRATLSRLRSFLPnARLFLMYGL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1831 TEaAVDVSYMD-ATLGLHPEescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANP- 1908
Cdd:TIGR03098  312 TE-AFRSTYLPpEEVDRRPD----SIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPp 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1909 FTAGQRMYRT----GDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQ---QLRLISglDVVVHAISSEQNKANVQLV 1981
Cdd:TIGR03098  387 FPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEvayATGLVA--EAVAFGVPDPTLGQAIVLV 464
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 490930577  1982 AYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:TIGR03098  465 VTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
1097-1519 7.98e-54

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: 196.40  E-value: 7.98e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1097 NSTILPLLPLQKGMLFLSQVE-NQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPV-FIYSLHPT 1174
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEpHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVqVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1175 QAWPVQFCSVTPDLLEQTIQEA----LQQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ 1250
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFiqrdLQSPFDLEKG-PLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1251 QT--NQQLPVLE-HSYETVIKALSGR----DHETSKVIWQRDLA-DLQPLILFNQAQQAVQ------ETSYRLSAELGAK 1316
Cdd:pfam00668  160 QLlkGEPLPLPPkTPYKDYAEWLQQYlqseDYQKDAAYWLEQLEgELPVLQLPKDYARPADrsfkgdRLSFTLDEDTEEL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1317 LQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQ 1396
Cdd:pfam00668  240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQ 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1397 QLHVEHLEHDGLGL------SAIQQLIAQGNLFDSLLVVENYPDnQYLQQKLGDAAISKLTNRGYSH----YPLALLVIP 1466
Cdd:pfam00668  318 EDLLSAEPHQGYPFgdlvndLRLPRDLSRHPLFDPMFSFQNYLG-QDSQEEEFQLSELDLSVSSVIEeeakYDLSLTASE 396
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577  1467 DH-QIELLLE-QRGVIDQP--EHFLERMIQLIEIALNEPETSLSHYRLQLAEEHDLI 1519
Cdd:pfam00668  397 RGgGLTIKIDyNTSLFDEEtiERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
1526-2035 1.60e-53

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 197.72  E-value: 1.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1526 QYYvrQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEA 1605
Cdd:PRK06187    2 QDY--PLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1606 GAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQK--DLAAIVHPSIAT---------------FAFNELFDETKVDLSS-Y 1667
Cdd:PRK06187   80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAAILPQLPTvrtvivegdgpaaplAPEVGEYEELLAAASDtF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1668 KTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCtFDVSVWEffWSYL---VGARL 1744
Cdd:PRK06187  160 DFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWG--LPYLalmAGAKQ 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1745 VIapidAHR-DPLALLSLIQKYQVTTLHFVPSMLavfenaaTEILSS--AQRQSLPICRVFCSG-EALPTALAKSFTEHF 1820
Cdd:PRK06187  237 VI----PRRfDPENLLDLIETERVTFFFAVPTIW-------QMLLKAprAYFVDFSSLRLVIYGgAALPPALLREFKEKF 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1821 SCELHNLYGPTEAAVDVSYmdatlgLHPEESCVAI-------GYPVWNTQLYILDQYLRPVPV--GVDGELYLAGHQLAM 1891
Cdd:PRK06187  306 GIDLVQGYGMTETSPVVSV------LPPEDQLPGQwtkrrsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQ 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 GYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISG----LDVVVH 1967
Cdd:PRK06187  380 GYWNRPEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELED---ALYGhpavAEVAVI 449
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1968 AISSEQNKANVqlVAY--LQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPH 2035
Cdd:PRK06187  450 GVPDEKWGERP--VAVvvLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
1538-2028 3.66e-53

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: 193.98  E-value: 3.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1538 LREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHP 1617
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1618 TERIKFMLQDAKSKLVIGEqkdlaaivhpsiatfafnelfdetkvdlssykttvitpqhPAYLIYTSGTTGQPKGVMVSH 1697
Cdd:cd17631    81 PPEVAYILADSGAKVLFDD----------------------------------------LALLMYTSGTTGRPKGAMLTH 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1698 QAIVNRILWMQSEYPLSATDTILQKTPcTFDVSVWEFFW--SYLVGARLVIAPidaHRDPLALLSLIQKYQVTTLHFVPS 1775
Cdd:cd17631   121 RNLLWNAVNALAALDLGPDDVLLVVAP-LFHIGGLGVFTlpTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPT 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 MLAVF---ENAATEILSSAQRqslpicrVFCSGEALPTALAKSFTEhFSCELHNLYGPTEAAVDVSYMDATlglHPEESC 1852
Cdd:cd17631   197 MIQALlqhPRFATTDLSSLRA-------VIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTFLSPE---DHRRKL 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1853 VAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQY 1932
Cdd:cd17631   266 GSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYI 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1933 IGRADDQLKIRGQRIELGEIEQQL-RLISGLDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTH 2011
Cdd:cd17631   339 VDRKKDMIISGGENVYPAEVEDVLyEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKS 418
                         490
                  ....*....|....*..
gi 490930577 2012 YMLVEQFPLSHNGKLDR 2028
Cdd:cd17631   419 VEFVDALPRNATGKILK 435
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
1558-2031 1.50e-52

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: 192.69  E-value: 1.50e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVI--G 1635
Cdd:cd17654    17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLqnK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1636 EQKDLAAIVHPSIATFAfnelfdetkvdlssykttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSA 1715
Cdd:cd17654    97 ELDNAPLSFTPEHRHFN------------------IRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1716 TDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALL-SLIQKYQVTTLHFVPSMLAVF--ENAATEILSSAq 1792
Cdd:cd17654   159 EDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLAdILFKRHRITVLQATPTLFRRFgsQSIKSTVLSAT- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1793 rQSLPICRVfcSGEALPTALAKSFTEHFSCELH--NLYGPTEaavdVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQy 1870
Cdd:cd17654   238 -SSLRVLAL--GGEPFPSLVILSSWRGKGNRTRifNIYGITE----VSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQ- 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1871 lrpVPVGVDGELYLAGhqLAMGYLHRADLTasrfvanpfTAGQRMYRTGDIARwHADGSIQYIGRADDQLKIRGQRIELG 1950
Cdd:cd17654   310 ---NGSEGTGQVFLGG--LNRVCILDDEVT---------VPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLD 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1951 EIEQQLRLISGLDVVVHAISSEQnkanvQLVAYLqTTAPVDiDQLKKQLAKH-LPAYMVPTHYMLVEQFPLSHNGKLDRK 2029
Cdd:cd17654   375 LIQQVIESCLGVESCAVTLSDQQ-----RLIAFI-VGESSS-SRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKS 447

                  ..
gi 490930577 2030 AL 2031
Cdd:cd17654   448 EL 449
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
1100-1500 6.92e-52

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: 189.44  E-value: 6.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLfLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVfiyslhpTQ---- 1175
Cdd:cd19542     1 IYPCTPMQEGML-LSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTF-------LQvvlk 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1176 --AWPVQFCSVTPDLLEQTIQEALQQPIHLDQPygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYqqtN 1253
Cdd:cd19542    73 slDPPIEEVETDEDSLDALTRDLLDDPTLFGQP--PHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY---N 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1254 QQLPVLEHSYETVIKALSGRDHETSKVIWQRDLADLQPLILFNQAQQAVQETSYRLSAELGAKLQHKLRQQGITLNVFMQ 1333
Cdd:cd19542   148 GQLLPPAPPFSDYISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTRRSLAKLEAFCASLGVTLASLFQ 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1334 MIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGLSAI 1413
Cdd:cd19542   228 AAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREI 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1414 QQLIAQ---GNLFDSLLVVENYPDNQyLQQKLGDAAISKLTNRGYSHYPLALLVIPDH-QIELLLEQRG-VIDQPehFLE 1488
Cdd:cd19542   308 QRALGLwpsGTLFNTLVSYQNFEASP-ESELSGSSVFELSAAEDPTEYPVAVEVEPSGdSLKVSLAYSTsVLSEE--QAE 384
                         410
                  ....*....|..
gi 490930577 1489 RMIQLIEIALNE 1500
Cdd:cd19542   385 ELLEQFDDILEA 396
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
1553-2026 7.95e-51

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: 188.58  E-value: 7.95e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1553 DENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKL 1632
Cdd:cd05911     6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1633 VIGEQKDLAAI-----------------VHPSIATFAFNELFDETKVDLSSYKTTVIT-PQHPAYLIYTSGTTGQPKGVM 1694
Cdd:cd05911    86 IFTDPDGLEKVkeaakelgpkdkiivldDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGTTGLPKGVC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVNRIL--WMQSEYPLSATDTILQKTPctfdvsvweFFWSY---------LVGARLVIAPIDahrDPLALLSLIQ 1763
Cdd:cd05911   166 LSHRNLIANLSqvQTFLYGNDGSNDVILGFLP---------LYHIYglfttlaslLNGATVIIMPKF---DSELFLDLIE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQVTTLHFVPSMLAVFenAATEILSSAQRQSLPicRVFCSGEALPTALAKSFTEHFS-CELHNLYGPTEAAVDVSYMda 1842
Cdd:cd05911   234 KYKITFLYLVPPIAAAL--AKSPLLDKYDLSSLR--VILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVN-- 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1843 TLGLHPEESCvaiGYPVWNTQLYILDQYLRP-VPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDI 1921
Cdd:cd05911   308 PDGDDKPGSV---GRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDI 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1922 ARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVV----HAISSEQNKANVQLVAYLQTTApvdiDQLK 1996
Cdd:cd05911   379 GYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVaDAAVigipDEVSGELPRAYVVRKPGEKLTE----KEVK 454
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 490930577 1997 KQLAKHlpaymVPTHYML------VEQFPLSHNGKL 2026
Cdd:cd05911   455 DYVAKK-----VASYKQLrggvvfVDEIPKSASGKI 485
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
1546-2031 8.83e-50

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: 185.98  E-value: 8.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTAL--SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKF 1623
Cdd:cd05926     1 PDAPALvvPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1624 MLQDAKSKLVI----GEQKDLAAIVHPSIAT-------------FAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGT 1686
Cdd:cd05926    81 YLADLGSKLVLtpkgELGPASRAASKLGLAIlelaldvgvliraPSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1687 TGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPcTFDVS--VWEFFWSYLVGARLVIAP-IDAHRdplaLLSLIQ 1763
Cdd:cd05926   161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMP-LFHVHglVASLLSTLAAGGSVVLPPrFSAST----FWPDVR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQVTTLHFVPSMLAVFENAATEILSSAqRQSLPICRvfCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDAT 1843
Cdd:cd05926   236 DYNATWYTAVPTIHQILLNRPEPNPESP-PPKLRFIR--SCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPLP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1844 LGLHPEEScvaIGYPVwNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIAR 1923
Cdd:cd05926   313 PGPRKPGS---VGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGY 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1924 WHADGSIQYIGRADDqLKIR-GQRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAK 2001
Cdd:cd05926   383 LDADGYLFLTGRIKE-LINRgGEKISPLEVDGVLLSHPAvLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRK 461
                         490       500       510
                  ....*....|....*....|....*....|
gi 490930577 2002 HLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05926   462 HLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
211-1105 1.62e-49

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: 194.90  E-value: 1.62e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   211 FWKAYCEDLPspISLSTHHLAAKTTATFVKHQLRFstgileQIQALAAQTKLALNDMMMSLSLH--YIYKMTDKAELV-- 286
Cdd:TIGR03443    1 RWSERLDNPT--LSVLPHDYLRPANNRLVEATYSL------QLPSAEVTAGGGSTPFIILLAAFaaLVYRLTGDEDIVlg 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   287 -----NGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVS---LAQHVQEQLREIRPhqkydaeqilrdlnsidihe 358
Cdd:TIGR03443   73 tssnkSGRPFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPfdeLSEHIQAAKKLERT-------------------- 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   359 rmygPILNYKAFdqdlvIDGEKVKTHHISTGPIDDFEFSFIVQDHELIIELRADSQRYTQDELFNHGQRLTLLLEQALIR 438
Cdd:TIGR03443  133 ----PPLFRLAF-----QDAPDNQQTTYSTGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSN 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   439 PEQPCSNFNITTPQELTALtqsgigprvshPEQYNN---------VLDIFYEQVKKYPERTAIV---SGERPNLQHLSF- 505
Cdd:TIGR03443  204 PDEPIGKVSLITPSQKSLL-----------PDPTKDldwsgfrgaIHDIFADNAEKHPDRTCVVetpSFLDPSSKTRSFt 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   506 -AELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANP--LFVLTTQ 582
Cdd:TIGR03443  273 yKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPraLIVIEKA 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   583 ALAQQLPQN-----------IQQLHLDQEG-VQTQIRKQDASDIPAENRKFDFQDVAYVI---------FTSGSTGRPKG 641
Cdd:TIGR03443  353 GTLDQLVRDyidkelelrteIPALALQDDGsLVGGSLEGGETDVLAPYQALKDTPTGVVVgpdsnptlsFTSGSEGIPKG 432
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   642 VMNTHGSLlnlilshkpTIYWPvleavnerfpdrplraahthsfsfdsswlqvfWMlwGQELHIfDENmrrDAFGLVQEI 721
Cdd:TIGR03443  433 VLGRHFSL---------AYYFP--------------------------------WM--AKRFGL-SEN---DKFTMLSGI 465
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   722 Q----QRQIDTldlPPSFCAQMmtnglfvenqHHPSLILIGGEAApLALW----------------QQLNAQ-----PAL 776
Cdd:TIGR03443  466 AhdpiQRDMFT---PLFLGAQL----------LVPTADDIGTPGR-LAEWmakygatvthltpamgQLLSAQattpiPSL 531
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   777 -------------------------FAHNLYGPTE-------YTV------DTFRAELKQtarpVI--GNPIGNTQAYVL 816
Cdd:TIGR03443  532 hhaffvgdiltkrdclrlqtlaenvCIVNMYGTTEtqravsyFEIpsrssdSTFLKNLKD----VMpaGKGMKNVQLLVV 607
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   817 DRH--LQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF------------------EHGQ----RMYRTGDLVR 872
Cdd:TIGR03443  608 NRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkennkperEFWLgprdRLYRTGDLGR 687
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   873 WNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALS----ILTNV--------ESAVVIAE--PINNSHRLLGYCVVKDiel 938
Cdd:TIGR03443  688 YLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSqhplVRENVtlvrrdkdEEPTLVSYivPQDKSDELEEFKSEVD--- 764
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   939 DEKTSEQ----------LSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP---QIRA----HSRMAE-- 999
Cdd:TIGR03443  765 DEESSDPvvkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPdtaQLAAvaknRSASAAde 844
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1000 --TPEQQLLCQITASVL--KLDAIGIDDDFFMTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMAPQLTRL-DEQ 1073
Cdd:TIGR03443  845 efTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKlNVELPLGLIFKSPTIKGFAKEVDRLkKGE 924
                         1050      1060      1070
                   ....*....|....*....|....*....|...
gi 490930577  1074 QAAVSKPLFSADLEQKVQEKYGKNS-TILPLLP 1105
Cdd:TIGR03443  925 ELADEGDSEIEEEETVLELDYAKDAkTLVDSLP 957
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1567-2031 2.03e-48

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: 180.71  E-value: 2.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1567 VCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAA----YLPIDLQHPTERIKFMLQDAKSKLVIGEQK---- 1638
Cdd:cd05922     3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGaadr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1639 -DLAAIVHPSIATFAFNELFDETKVDLSSYkttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATD 1717
Cdd:cd05922    83 lRDALPASPDPGTVLDADGIRAARASAPAH---EVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 TILQKTPCTFDVSVWEFFWSYLVGARLVIAPidAHRDPLALLSLIQKYQVTTLHFVPSMLavfenaatEILSSAQRQ--S 1795
Cdd:cd05922   160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTN--DGVLDDAFWEDLREHGATGLAGVPSTY--------AMLTRLGFDpaK 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1796 LPICRVFC-SGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEEScvaIGYPVWNTQLYILDQYLRP 1873
Cdd:cd05922   230 LPSLRYLTqAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPERILEKPGS---IGLAIPGGEFEILDDDGTP 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1874 VPVGVDGELYLAGHQLAMGYLHRadltaSRFVANPFTAGQRMYrTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:cd05922   307 TPPGEPGEIVHRGPNVMKGYWND-----PPYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIE 380
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1954 QQLRLIsGLDVVVHAISSEqNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05922   381 AAARSI-GLIIEAAAVGLP-DPLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
625-982 3.00e-48

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: 176.71  E-value: 3.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiywpVLEAVNERFPDRPLraaHTHSFSFDSSWLQVFWML-WGQEL 703
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAA--------LAASGGLTEGDVFL---STLPLFHIGGLFGLLGALlAGGTV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  704 HIFDenmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFvENQHHPSL--ILIGGEAAPLALWQQLNAQPALFAHNL 781
Cdd:cd04433    70 VLLP---KFDPEAALELIEREKVTILLGVPTLLARLLKAPES-AGYDLSSLraLVSGGAPLPPELLERFEEAPGIKLVNG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  782 YGPTE--YTVDTFRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANpfe 859
Cdd:cd04433   146 YGLTEtgGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG--- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  860 hgqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGY----CVVKD 935
Cdd:cd04433   223 ----WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVP----DPEWGErvvaVVVLR 294
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 490930577  936 iELDEKTSEQLSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVD 982
Cdd:cd04433   295 -PGADLDAEELRA----HVRERLAPYKVPRRVVFVDALPRTASGKID 336
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
1548-2034 9.14e-47

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: 177.71  E-value: 9.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1548 QTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQD 1627
Cdd:cd17647    11 PSLNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1628 AKSKLVIGEQKdLAAIVHP-SIATFAFnelfdetkvdlssykttvitpqhpayliyTSGTTGQPKGVMVSHQAIVNRILW 1706
Cdd:cd17647    91 AKPRGLIVIRA-AGVVVGPdSNPTLSF-----------------------------TSGSEGIPKGVLGRHFSLAYYFPW 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1707 MQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATE 1786
Cdd:cd17647   141 MAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATT 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1787 ilssaqrQSLPICRVFCSGEALPT---ALAKSFTEhfSCELHNLYGPTEAAVDVSYMDATLG------LHPEESCVAIGY 1857
Cdd:cd17647   221 -------PFPKLHHAFFVGDILTKrdcLRLQTLAE--NVRIVNMYGTTETQRAVSYFEVPSRssdptfLKNLKDVMPAGR 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1858 PVWNTQLYILDQYLRPVPVGVD--GELYLAGHQLAMGYLHRADLTASRFVAN--------------------PFTAG--Q 1913
Cdd:cd17647   292 GMLNVQLLVVNRNDRTQICGIGevGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnepwrQFWLGprD 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1914 RMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQlrlISGLDVVVHAISSEQNKANVQ--LVAYL------- 1984
Cdd:cd17647   372 RLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTH---ISQHPLVRENITLVRRDKDEEptLVSYIvprfdkp 448
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1985 ------QTTAPVD----------------IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQP 2034
Cdd:cd17647   449 ddesfaQEDVPKEvstdpivkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
1100-1476 1.14e-44

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: 167.86  E-value: 1.14e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLFLSqVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQAWpv 1179
Cdd:cd19545     1 IYPCTPLQEGLMALT-ARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISW-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 qfcsVTPDLLEQTIQEALQQPIHLDQPygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQQLPVl 1259
Cdd:cd19545    78 ----TESTSLDEYLEEDRAAPMGLGGP--LVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPP- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1260 ehSYETVIKALSGRDHETSKVIWQRDLADLQPLIlFNQAQqavqetSYRLSAELGAKLQHKLR-----QQGITLNVFMQM 1334
Cdd:cd19545   151 --PFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAV-FPPLP------SSRYQPRPDATLEHSISlpssaSSGVTLATVLRA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1335 IWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGLSAIQ 1414
Cdd:cd19545   222 AWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIR 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1415 QLI---AQGNLFDSLLVVEnyPDNQYLQQKLGDAAISKLTNR--GYSHYPLALL-----------------VIPDHQIEL 1472
Cdd:cd19545   302 RLGpdaRAACNFQTLLVVQ--PALPSSTSESLELGIEEESEDleDFSSYGLTLEcqlsgsglrvrarydssVISEEQVER 379

                  ....
gi 490930577 1473 LLEQ 1476
Cdd:cd19545   380 LLDQ 383
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
1558-2031 4.32e-43

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: 164.43  E-value: 4.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 KDlaaivhpsiatfafnelfdetkvdlssykttvitpqhPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATD 1717
Cdd:cd05972    81 ED-------------------------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 TILqktpCTFDVSVWEFFWSYLVGARLVIAPIDAHR----DPLALLSLIQKYQVTTLHFVPsmlAVFENAATEILSSAQR 1793
Cdd:cd05972   124 IHW----NIADPGWAKGAWSSFFGPWLLGATVFVYEgprfDAERILELLERYGVTSFCGPP---TAYRMLIKQDLSSYKF 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1794 QSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSyMDATLGLHPEescvAIGYPVWNTQLYILDQYLRP 1873
Cdd:cd05972   197 SHLRL--VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVG-NFPDMPVKPG----SMGRPTPGYDVAIIDDDGRE 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1874 VPVGVDGEL--YLAGHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGE 1951
Cdd:cd05972   270 LPPGEEGDIaiKLPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFE 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1952 IEQQLR-----LISGLDVVVHAISSEQNKANVQLVAYLQTTaPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKL 2026
Cdd:cd05972   343 VESALLehpavAEAAVVGSPDPVRGEVVKAFVVLTSGYEPS-EELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421

                  ....*
gi 490930577 2027 DRKAL 2031
Cdd:cd05972   422 RRVEL 426
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1557-2032 4.95e-43

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: 164.00  E-value: 4.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIge 1636
Cdd:cd05934     3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 qkdlaaivhpsiatfafnelfdetkVDlssykttvitpqhPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSAT 1716
Cdd:cd05934    81 -------------------------VD-------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGED 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1717 DTILQKTPcTF--DVSVWEFFWSYLVGARLVIAPidahR-DPLALLSLIQKYQVTTLHFVPSMLAVFenAATEIlsSAQR 1793
Cdd:cd05934   123 DVYLTVLP-LFhiNAQAVSVLAALSVGATLVLLP----RfSASRFWSDVRRYGATVTNYLGAMLSYL--LAQPP--SPDD 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1794 QSLPIcRVFCSGEALPtALAKSFTEHFSCELHNLYGPTEAAVdvsymdATLGLHPEESCV-AIGYPVWNTQLYILDQYLR 1872
Cdd:cd05934   194 RAHRL-RAAYGAPNPP-ELHEEFEERFGVRLLEGYGMTETIV------GVIGPRDEPRRPgSIGRPAPGYEVRIVDDDGQ 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1873 PVPVGVDGELYL---AGHQLAMGYLHRADLTASRFvANpftagqRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIEL 1949
Cdd:cd05934   266 ELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RN------GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISS 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1950 GEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:cd05934   339 AEVERAILRHPAvREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAK 418

                  ....
gi 490930577 2029 KALP 2032
Cdd:cd05934   419 AQLR 422
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
1558-2026 7.41e-43

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: 164.09  E-value: 7.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSK-LVIGE 1636
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKvFVVPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 ---QKDLAAIvhpsiatfafnelfdetkvdlssykttvitPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPL 1713
Cdd:cd05903    82 rfrQFDPAAM------------------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1714 SATDTILQKTPCT-FDVSVWEFFWSYLVGARLVIAPIdahRDPLALLSLIQKYQVTTL----HFVPSMLAVFENAATEil 1788
Cdd:cd05903   132 GPGDVFLVASPMAhQTGFVYGFTLPLLLGAPVVLQDI---WDPDKALALMREHGVTFMmgatPFLTDLLNAVEEAGEP-- 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1789 ssaqrqsLPICRVF-CSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLglhPEESCVAIGYPVWNTQLYIL 1867
Cdd:cd05903   207 -------LSRLRTFvCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAP---EDRRLYTDGRPLPGVEIKVV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1868 DQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASrfvanpfTAGQRMYRTGDIARWHADGSIQYIGRADDqLKIR-GQR 1946
Cdd:cd05903   277 DDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-------AAPEGWFRTGDLARLDEDGYLRITGRSKD-IIIRgGEN 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1947 IELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQL-----KKQLAKHlpayMVPTHYMLVEQFPL 2020
Cdd:cd05903   349 IPVLEVEDLLLGHPGvIEAAVVALPDERLGERACAVVVTKSGALLTFDELvayldRQGVAKQ----YWPERLVHVDDLPR 424

                  ....*.
gi 490930577 2021 SHNGKL 2026
Cdd:cd05903   425 TPSGKV 430
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
1548-2031 1.00e-42

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: 163.40  E-value: 1.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1548 QTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID-LQHPTErIKFMLQ 1626
Cdd:cd05919     1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINpLLHPDD-YAYIAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1627 DAKSKLVIGEQKDLAaivhpsiatfafnelfdetkvdlssykttvitpqhpaYLIYTSGTTGQPKGVMVSHQAIVNRILW 1706
Cdd:cd05919    80 DCEARLVVTSADDIA-------------------------------------YLLYSSGTTGPPKGVMHAHRDPLLFADA 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1707 MQSEY-PLSATDTILQKTPCTFDV----SVWeFFWSylVGARLVIAPidAHRDPLALLSLIQKYQVTTLHFVPSMLAVFE 1781
Cdd:cd05919   123 MAREAlGLTPGDRVFSSAKMFFGYglgnSLW-FPLA--VGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLL 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1782 NAATeiLSSAQRQSLPICrvFCSGEALPTALAKSFTEHFSCELHNLYGPTEaaVDVSYMDATLGLHPEESCvaiGYPVWN 1861
Cdd:cd05919   198 DSCA--GSPDALRSLRLC--VSAGEALPRGLGERWMEHFGGPILDGIGATE--VGHIFLSNRPGAWRLGST---GRPVPG 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1862 TQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLK 1941
Cdd:cd05919   269 YEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLK 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1942 IRGQRIELGEIEQqlrLISGLDVVVHA--ISSEQNKANVQLVAYLQTTAPVDIDQ-----LKKQLAKHLPAYMVPTHYML 2014
Cdd:cd05919   342 VGGQWVSPVEVES---LIIQHPAVAEAavVAVPESTGLSRLTAFVVLKSPAAPQEslardIHRHLLERLSAHKVPRRIAF 418
                         490
                  ....*....|....*..
gi 490930577 2015 VEQFPLSHNGKLDRKAL 2031
Cdd:cd05919   419 VDELPRTATGKLQRFKL 435
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
1533-2031 1.47e-42

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: 164.60  E-value: 1.47e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSD--ENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYL 1610
Cdd:cd05923     2 TVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1611 PIDLQHPTERIKFMLQDAKSKLVIgeqKDLAAIVHPSIATFAFNELFDETKVDLS-------SYKTTVITPQHPAYLIYT 1683
Cdd:cd05923    82 LINPRLKAAELAELIERGEMTAAV---IAVDAQVMDAIFQSGVRVLALSDLVGLGepesagpLIEDPPREPEQPAFVFYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1684 SGTTGQPKGVMVSHQAIVNRILWM--QSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAhrDPLALLSL 1761
Cdd:cd05923   159 SGTTGLPKGAVIPQRAAESRVLFMstQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADALKL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1762 IQKYQVTTLHFVPSMLAVFenAATEILSSAQRQSLPicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMD 1841
Cdd:cd05923   237 IEQERVTSLFATPTHLDAL--AAAAEFAGLKLSSLR--HVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1842 ATLGlhpeescvAIGYPVWNTQLYILDQYLRPV---PVGVDGELY--LAGHQLAMGYLHRADLTASRFVanpftagQRMY 1916
Cdd:cd05923   313 ARTG--------TEMRPGFFSEVRIVRIGGSPDealANGEEGELIvaAAADAAFTGYLNQPEATAKKLQ-------DGWY 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1917 RTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD-VVVHAISSEQNKANVQLVAYLQtTAPVDIDQL 1995
Cdd:cd05923   378 RTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTeVVVIGVADERWGQSVTACVVPR-EGTLSADEL 456
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 490930577 1996 KK-QLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05923   457 DQfCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
1537-2031 1.84e-42

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: 164.46  E-value: 1.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:cd05959     9 VDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQ-----------KDLAAIVH--------PSIATFAFNELFDETKVDLSSYKTtviTPQHP 1677
Cdd:cd05959    89 TPDDYAYYLEDSRARVVVVSGelapvlaaaltKSEHTLVVlivsggagPEAGALLLAELVAAEAEQLKPAAT---HADDP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 AYLIYTSGTTGQPKGVMVSHQAIVnrilWMQSEYplsaTDTILQKTPCTFDVSVWEFFWSY----------LVGARLVIA 1747
Cdd:cd05959   166 AFWLYSSGSTGRPKGVVHLHADIY----WTAELY----ARNVLGIREDDVCFSAAKLFFAYglgnsltfplSVGATTVLM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1748 PidAHRDPLALLSLIQKYQVTTLHFVP----SMLAVfENAATEILSsaqrqSLPICrvFCSGEALPTALAKSFTEHFSCE 1823
Cdd:cd05959   238 P--ERPTPAAVFKRIRRYRPTVFFGVPtlyaAMLAA-PNLPSRDLS-----SLRLC--VSAGEALPAEVGERWKARFGLD 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1824 LHNLYGPTEAavdvsymdatlgLH------PEESCV-AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHR 1896
Cdd:cd05959   308 ILDGIGSTEM------------LHiflsnrPGRVRYgTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNN 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1897 ADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlRLISGLDVVVHA-ISSEQNK 1975
Cdd:cd05959   376 RDKTRDTFQGE-------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVES--ALVQHPAVLEAAvVGVEDED 446
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1976 ANVQLVAYL-----QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05959   447 GLTKPKAFVvlrpgYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1559-2031 1.32e-40

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: 157.21  E-value: 1.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1559 SFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIgeqk 1638
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1639 dlaaivhpsiatfafnelfdetkVDLSSykttvitpqHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDT 1718
Cdd:cd05971    84 -----------------------TDGSD---------DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDG 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1719 ILQKTPCT-------FDVsvweFFWSYLVGArlviaPIDAHR----DPLALLSLIQKYQVTTLHFVPSMLAVFEnAATEI 1787
Cdd:cd05971   132 DLYWTPADwawigglLDV----LLPSLYFGV-----PVLAHRmtkfDPKAALDLMSRYGVTTAFLPPTALKMMR-QQGEQ 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1788 LSSAQRQSLPIcrvFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEescvAIGYPVWNTQLYIL 1867
Cdd:cd05971   202 LKHAQVKLRAI---ATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPG----SMGKPIPGHRVAIV 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1868 DQYLRPVPVGVDGELYLAGHQLAM--GYLHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQ 1945
Cdd:cd05971   275 DDNGTPLPPGEVGEIAVELPDPVAflGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGY 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1946 RIELGEIEQQL-RLISGLDVVV----HAISSEQNKANVQLVAylqttAPVDIDQLKKQLAKH----LPAYMVPTHYMLVE 2016
Cdd:cd05971   348 RIGPAEIEECLlKHPAVLMAAVvgipDPIRGEIVKAFVVLNP-----GETPSDALAREIQELvktrLAAHEYPREIEFVN 422
                         490
                  ....*....|....*
gi 490930577 2017 QFPLSHNGKLDRKAL 2031
Cdd:cd05971   423 ELPRTATGKIRRREL 437
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
1547-2031 3.74e-40

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: 155.91  E-value: 3.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1547 EQTALSDENHQLSFSEVRLQVCALAQQLQRAG-VQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIgeqkDLAAIvhpsiatfafnelfdetkvdlssykttvitpqhpaylIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd05941    81 TDSEPSLVL----DPALI-------------------------------------LYTSGTTGRPKGVVLTHANLAANVR 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTP------------CTFdvsvweffwsyLVGARLVIAPIDahrDPLALLSLIQKYQVTTLHFV 1773
Cdd:cd05941   120 ALVDAWRWTEDDVLLHVLPlhhvhglvnallCPL-----------FAGASVEFLPKF---DPKEVAISRLMPSITVFMGV 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1774 PSM----LAVFENAATEIlSSAQRQSLPICRVFCSGEA-LPTALAKSFTEHFSCELHNLYGPTEAAvdvsyMDATLGLHP 1848
Cdd:cd05941   186 PTIytrlLQYYEAHFTDP-QFARAAAAERLRLMVSGSAaLPVPTLEEWEAITGHTLLERYGMTEIG-----MALSNPLDG 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1849 EESCVAIGYPVWNTQLYILDQ-YLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHAD 1927
Cdd:cd05941   260 ERRPGTVGMPLPGVQARIVDEeTGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDED 333
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1928 GSIQYIGR-ADDQLKIRGQRIELGEIEQQLRLISGLD--VVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLP 2004
Cdd:cd05941   334 GYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSecAVIGVPDPDWGERVVAVVVLRAGAAALSLEELKEWAKQRLA 413
                         490       500
                  ....*....|....*....|....*..
gi 490930577 2005 AYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05941   414 PYKRPRRLILVDELPRNAMGKVNKKEL 440
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
1528-2031 4.23e-40

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: 156.72  E-value: 4.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1528 YVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGA 1607
Cdd:cd05920    11 YWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 ayLPIdLQHPTER---IKFMLQDAKSKlvigeqkdlAAIVHPSIATFAFNELFDETKVDlssykttviTPQhPAYLIYTS 1684
Cdd:cd05920    91 --VPV-LALPSHRrseLSAFCAHAEAV---------AYIVPDRHAGFDHRALARELAES---------IPE-VALFLLSG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1685 GTTGQPKGVMVSHQaivnrilwmQSEYPLSATDTILQKTPCT-----------FDVSVWEFFWSYLVGARLVIAPiDAhr 1753
Cdd:cd05920   149 GTTGTPKLIPRTHN---------DYAYNVRASAEVCGLDQDTvylavlpaahnFPLACPGVLGTLLAGGRVVLAP-DP-- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1754 DPLALLSLIQKYQVTTLHFVPSMLAVFENAATEilSSAQRQSLPICRVfcSGEALPTALAKSFTEHFSCELHNLYGPTEA 1833
Cdd:cd05920   217 SPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQV--GGARLSPALARRVPPVLGCTLQQVFGMAEG 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1834 AVDVSYMDatlglHPEESCVAI-GYPVW-NTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFta 1911
Cdd:cd05920   293 LLNYTRLD-----DPDEVIIHTqGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-- 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1912 gqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTaPV 1990
Cdd:cd05920   366 ----YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVhDAAVVAMPDELLGERSCAFVVLRDP-PP 440
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 490930577 1991 DIDQLKKQL-AKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05920   441 SAAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
1100-1501 4.30e-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: 155.30  E-value: 4.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLFLSqvENQS-------NYNAFTRLSLNGDidpvRLQQALITVLKRHPQLGGHFDseLAEEPVFIYSLH 1172
Cdd:cd19536     1 MYPLSSLQEGMLFHS--LLNPggsvylhNYTYTVGRRLNLD----LLLEALQVLIDRHDILRTSFI--EDGLGQPVQVVH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1173 PTQAWPVQFCSVTP-DLLEQTIQEALQQPIHLDQPYG---LIRATLIQHAP-EQSELLIMVHHLLTDGWSTPLFLQDFIK 1247
Cdd:cd19536    73 RQAQVPVTELDLTPlEEQLDPLRAYKEETKIRRFDLGrapLVRAALVRKDErERFLLVISDHHSILDGWSLYLLVKEILA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1248 AYQQTNQQLPVLE---HSYETVIK-ALSGRDHETSKVIWQRDL--ADLQPLILFNQAQQA--VQETSYRLSAELGAKLQH 1319
Cdd:cd19536   153 VYNQLLEYKPLSLppaQPYRDFVAhERASIQQAASERYWREYLagATLATLPALSEAVGGgpEQDSELLVSVPLPVRSRS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1320 KLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNmQQTLWEQLPQLQQLH 1399
Cdd:cd19536   233 LAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLS-EETVEDLLKRAQEQE 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1400 VEHLEHDGLGLSAIQQLIAQGNLFDSLLVVENYPDNQYLQQKLGDAAIS--KLTNRGYSHYPLALLVIPdHQIELLLE-- 1475
Cdd:cd19536   312 LESLSHEQVPLADIQRCSEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRrgLLFSEFKSNYDVNLSVLP-KQDRLELKla 390
                         410       420
                  ....*....|....*....|....*....
gi 490930577 1476 -QRGVID--QPEHFLERMIQLIEIALNEP 1501
Cdd:cd19536   391 yNSQVLDeeQAQRLAAYYKSAIAELATAP 419
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
41-458 1.11e-39

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: 154.80  E-value: 1.11e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577    41 YTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELN-NQVQFQIEEFDFCHLTPKKAQQRLWDWMPSD 119
Cdd:pfam00668   27 YNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVIlEERPFELEIIDISDLSESEEEEAIEAFIQRD 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   120 RQcaKSLKAGETQLFRQVLFT-THDKVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQEGKDLSVSPFIGVNEVISERQA 198
Cdd:pfam00668  107 LQ--SPFDLEKGPLFRAGLFRiAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGEPLPLPPKTPYKDYAEWLQQ 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   199 YENSHQFKIDQAFWKAYCEDLPSPISLSTHHlAAKTTATFVKHQLRFST--GILEQIQALAAQTKLALNDMMMSLSLHYI 276
Cdd:pfam00668  185 YLQSEDYQKDAAYWLEQLEGELPVLQLPKDY-ARPADRSFKGDRLSFTLdeDTEELLRKLAKAHGTTLNDVLLAAYGLLL 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   277 YKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNS--I 354
Cdd:pfam00668  264 SRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLRLprD 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   355 DIHERMYGPILNYKAFDQDLVIDGE--------KVKTHHISTGPiddFEFSFIVQDHE--LIIELRADSQRYTQDELFNH 424
Cdd:pfam00668  344 LSRHPLFDPMFSFQNYLGQDSQEEEfqlseldlSVSSVIEEEAK---YDLSLTASERGggLTIKIDYNTSLFDEETIERF 420
                          410       420       430
                   ....*....|....*....|....*....|....
gi 490930577   425 GQRLTLLLEQALIRPEQPCSNFNITTPQELTALT 458
Cdd:pfam00668  421 AEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
469-986 1.84e-39

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 156.81  E-value: 1.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  469 PEQYN---NVLDifyEQVKKYPERTAIVS-GERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVM 544
Cdd:COG0365     5 GGRLNiayNCLD---RHAEGRGDKVALIWeGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  545 L---------SVLNSGasFLPLDLdypIDRMqmmcEDANPLFVLTT----------------QALAQQLPQNIQQLHLDQ 599
Cdd:COG0365    82 LacarigavhSPVFPG--FGAEAL---ADRI----EDAEAKVLITAdgglrggkvidlkekvDEALEELPSLEHVIVVGR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  600 EGVQT---------QIRKQDASDIPAENRKFDfqDVAYVIFTSGSTGRPKGVMNTHGSLLnlilshkptiywpvleavne 670
Cdd:COG0365   153 TGADVpmegdldwdELLAAASAEFEPEPTDAD--DPLFILYTSGTTGKPKGVVHTHGGYL-------------------- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  671 rfpdrpLRAAHTHSFSFDsswLQ---VFW-------------MLWGQELH-----IFDEN-MRRDAFGLVQEIQQRQIDT 728
Cdd:COG0365   211 ------VHAATTAKYVLD---LKpgdVFWctadigwatghsyIVYGPLLNgatvvLYEGRpDFPDPGRLWELIEKYGVTV 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  729 LDLPPSFCAQMMTNGLFVENQHHPS---LILIGGEAAPLALWQQLNAQPALFAHNLYGPTEytvdtfraelkqTARPVIG 805
Cdd:COG0365   282 FFTAPTAIRALMKAGDEPLKKYDLSslrLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTE------------TGGIFIS 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  806 NPIGNT-------------QAYVLDRHLQRCPTGVIGELYISGF--GIANGYLGRADlsaaRFVANPFEHGQRMYRTGDL 870
Cdd:COG0365   350 NLPGLPvkpgsmgkpvpgyDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPE----RYRETYFGRFPGWYRTGDG 425
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  871 VRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVV-IAEPINNsHRLLGYCVVKD-IELDEKTSEQLS 947
Cdd:COG0365   426 ARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVaEAAVVgVPDEIRG-QVVKAFVVLKPgVEPSDELAKELQ 504
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 490930577  948 QqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:COG0365   505 A----HVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
1533-2031 1.89e-39

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 155.83  E-value: 1.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI 1612
Cdd:PRK07656    6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1613 DLQHPTERIKFMLQDAKSKLVIGEQ----------KDLAAIVHpsIATFAFNELFDETKVDLS----------SYKTTVI 1672
Cdd:PRK07656   86 NTRYTADEAAYILARGDAKALFVLGlflgvdysatTRLPALEH--VVICETEEDDPHTEKMKTftdflaagdpAERAPEV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1673 TPQHPAYLIYTSGTTGQPKGVMVSH-QAIVNRILWmqSEY-PLSATDTILQKTPctfdvsvweFF--------W--SYLV 1740
Cdd:PRK07656  164 DPDDVADILFTSGTTGRPKGAMLTHrQLLSNAADW--AEYlGLTEGDRYLAANP---------FFhvfgykagVnaPLMR 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1741 GARLVIAPidaHRDPLALLSLIQKYQVTTLHFVPSM---LAVFENAATEILSSaqrqslpiCRVFCSGEA-LPTALAKSF 1816
Cdd:PRK07656  233 GATILPLP---VFDPDEVFRLIETERITVLPGPPTMynsLLQHPDRSAEDLSS--------LRLAVTGAAsMPVALLERF 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1817 TEHFSCE-LHNLYGPTEAA-VdvsymdATL-GLHPEESCVA--IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAM 1891
Cdd:PRK07656  302 ESELGVDiVLTGYGLSEASgV------TTFnRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMK 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 GYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVV---- 1966
Cdd:PRK07656  376 GYYDDPEATAAAIDADGW------LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVaEAAVigvp 449
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1967 HAISSEQNKANVqlvaYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK07656  450 DERLGEVGKAYV----VLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1537-2031 1.16e-38

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: 153.56  E-value: 1.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALS----DENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI 1612
Cdd:cd12119     1 LLEHAARLHGDREIVSrtheGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1613 DLQHPTERIKFMLQDAKSKLVI--GEQKDLAAIVHPSIATF-AFNELFDETKVDLSSYKT-----TVITPQHPAY----- 1679
Cdd:cd12119    81 NPRLFPEQIAYIINHAEDRVVFvdRDFLPLLEAIAPRLPTVeHVVVMTDDAAMPEPAGVGvlayeELLAAESPEYdwpdf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 -------LIYTSGTTGQPKGVMVSHQAIV--NRILWMQSEYPLSATDTILqktPCT--FDVSVWEF-FWSYLVGARLVIa 1747
Cdd:cd12119   161 dentaaaICYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLGLSESDVVL---PVVpmFHVNAWGLpYAAAMVGAKLVL- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1748 PiDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAateiLSSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHnL 1827
Cdd:cd12119   237 P-GPYLDPASLAELIEREGVTFAAGVPTVWQGLLDH----LEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIH-A 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1828 YGPTEAA--VDVSYMDATLGLHPEESCVAI----GYPVWNTQLYILDQYLRPVPvgVD----GELYLAGHQLAMGYLHRA 1897
Cdd:cd12119   311 WGMTETSplGTVARPPSEHSNLSEDEQLALrakqGRPVPGVELRIVDDDGRELP--WDgkavGELQVRGPWVTKSYYKND 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1898 DlTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQNKA 1976
Cdd:cd12119   389 E-ESEALTEDGW------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAvAEAAVIGVPHPKWGE 461
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1977 NVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd12119   462 RPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
1557-2031 1.32e-38

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: 151.09  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVI-- 1634
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVvg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1635 GEQKDLAAIVhpsiatfafnelfdetkvdlssykttvitpqhpayliYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLS 1714
Cdd:cd05935    81 SELDDLALIP-------------------------------------YTSGTTGLPKGCMHTHFSAAANALQSAVWTGLT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1715 ATDTILQKTPcTFDVSvwEFFWSYL----VGARLVIApidAHRDPLALLSLIQKYQVTTLHFVPSMLAVfenaateILSS 1790
Cdd:cd05935   124 PSDVILACLP-LFHVT--GFVGSLNtavyVGGTYVLM---ARWDRETALELIEKYKVTFWTNIPTMLVD-------LLAT 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1791 A--QRQSLPICRVFCSGEA-LPTALAKSFTEHFSCELHNLYGPTEAavdVSYMDATLGLHPEESCvaIGYPVWNTQLYIL 1867
Cdd:cd05935   191 PefKTRDLSSLKVLTGGGApMPPAVAEKLLKLTGLRFVEGYGLTET---MSQTHTNPPLRPKLQC--LGIP*FGVDARVI 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1868 D-QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVanpFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQR 1946
Cdd:cd05935   266 DiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1947 IELGEIEQQL---RLIsgLDVVVHAI----SSEQNKANVQL-VAYLQTTAPVDIDQLKKQlakHLPAYMVPTHYMLVEQF 2018
Cdd:cd05935   343 VWPAEVEAKLykhPAI--*EVCVISVpderVGEEVKAFIVLrPEYRGKVTEEDIIEWARE---QMAAYKYPREVEFVDEL 417
                         490
                  ....*....|...
gi 490930577 2019 PLSHNGKLDRKAL 2031
Cdd:cd05935   418 PRSASGKILWRLL 430
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
503-986 3.06e-38

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: 150.70  E-value: 3.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQ 582
Cdd:cd17654    17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  583 ALAQqlpqniQQLHLDQEGVQTQIRKQDASdipaenrkfdfqdvAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIyw 662
Cdd:cd17654    97 ELDN------APLSFTPEHRHFNIRTDECL--------------AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLF-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  663 pVLEAVNERFPDRPLraahthsfSFDSSWLQVFWMLWGQELHIFDENMRRDAFGLVQEI--QQRQIDTLDLPPSFCAQMM 740
Cdd:cd17654   155 -NITSEDILFLTSPL--------TFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADIlfKRHRITVLQATPTLFRRFG 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  741 TNGLFVEN-QHHPSL--ILIGGEAAP----LALWQQLNAQPALFahNLYGPTEYTVDTFRAELKQTARPV-IGNPIGNTQ 812
Cdd:cd17654   226 SQSIKSTVlSATSSLrvLALGGEPFPslviLSSWRGKGNRTRIF--NIYGITEVSCWALAYKVPEEDSPVqLGSPLLGTV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  813 AYVLDrhlqRCPTGVIGELY---ISGFGIANGYLGRADlsaarfvanpfehGQrMYRTGDLVRwNSAGKLEFMGRCDDQI 889
Cdd:cd17654   304 IEVRD----QNGSEGTGQVFlggLNRVCILDDEVTVPK-------------GT-MRATGDFVT-VKDGELFFLGRKDSQI 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  890 KIRGYRVEIGEVENALSILTNVESAVVIAEpinNSHRLLGYCV---VKDIELDEKTSEQLSqqylsqlRQNLPEYMVpsa 966
Cdd:cd17654   365 KRRGKRINLDLIQQVIESCLGVESCAVTLS---DQQRLIAFIVgesSSSRIHKELQLTLLS-------SHAIPDTFV--- 431
                         490       500
                  ....*....|....*....|
gi 490930577  967 ltVMSEFPRNVSGKVDKKAL 986
Cdd:cd17654   432 --QIDKLPLTSHGKVDKSEL 449
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
485-983 7.85e-38

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: 148.91  E-value: 7.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  485 KYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDldypid 564
Cdd:cd17631     7 RHPDRTALVFGGRS----LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  565 rmqmmcedanplFVLTTQALAQQLpqniqqlhldqegvqtqirkQDASDipaenrKFDFQDVAYVIFTSGSTGRPKGVMN 644
Cdd:cd17631    77 ------------FRLTPPEVAYIL--------------------ADSGA------KVLFDDLALLMYTSGTTGRPKGAML 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  645 THGSLLNLILSHkpTIYWPVLEAvnerfpDRPLRAAH-THSFSFDSSWLQVFWMlwGQELHIfdenMRR-DAFGLVQEIQ 722
Cdd:cd17631   119 THRNLLWNAVNA--LAALDLGPD------DVLLVVAPlFHIGGLGVFTLPTLLR--GGTVVI----LRKfDPETVLDLIE 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  723 QRQIDTLDLPPSFCAQMMTNGLFvENQHHPSL--ILIGGEAAPLALWQQLNAQPALFaHNLYGPTE--YTVDTFRAELKQ 798
Cdd:cd17631   185 RHRVTSFFLVPTMIQALLQHPRF-ATTDLSSLraVIYGGAPMPERLLRALQARGVKF-VQGYGMTEtsPGVTFLSPEDHR 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  799 TARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAArfvanPFEHGqrMYRTGDLVRWNSAGK 878
Cdd:cd17631   263 RKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAA-----AFRDG--WFHTGDLGRLDEDGY 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  879 LEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLG-----YCVVKD-IELDEktseqlsQQYLS 952
Cdd:cd17631   336 LYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVP----DEKWGeavvaVVVPRPgAELDE-------DELIA 404
                         490       500       510
                  ....*....|....*....|....*....|.
gi 490930577  953 QLRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:cd17631   405 HCRERLARYKIPKSVEFVDALPRNATGKILK 435
PRK07788 PRK07788
acyl-CoA synthetase; Validated
1529-2032 8.20e-38

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 151.62  E-value: 8.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1529 VRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVaLPR-SVKLSIAILAVIEAGA 1607
Cdd:PRK07788   46 RRYGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAV-LARnHRGFVLALYAAGKVGA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 --AYLPIDLQHPT-------ERIKFMLQDAK-SKLVIGEQKDL----AAIVHPSIATFAFNElfDETKVDLSSYKTTVIT 1673
Cdd:PRK07788  125 riILLNTGFSGPQlaevaarEGVKALVYDDEfTDLLSALPPDLgrlrAWGGNPDDDEPSGST--DETLDDLIAGSSTAPL 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1674 P---QHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPC--TFDVSVWEFfwSYLVGARLVIap 1748
Cdd:PRK07788  203 PkppKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTL--AMALGSTVVL-- 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 idaHR--DPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLPIcrVFCSGEALPTALAKSFTEHFSCELHN 1826
Cdd:PRK07788  279 ---RRrfDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKI--IFVSGSALSPELATRALEAFGPVLYN 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1827 LYGPTEAAVdvsymdATLGlHPEESCVA---IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYlhradlTASR 1903
Cdd:PRK07788  354 LYGSTEVAF------ATIA-TPEDLAEApgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1904 fvaNPFTAGQRMyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISGL-DVV-VHAISSEQNKANVQLV 1981
Cdd:PRK07788  421 ---DKQIIDGLL-SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVED---LLAGHpDVVeAAVIGVDDEEFGQRLR 493
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1982 AYLQTT--APVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALP 2032
Cdd:PRK07788  494 AFVVKApgAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1538-2035 1.61e-37

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 149.34  E-value: 1.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1538 LREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHP 1617
Cdd:PRK03640    8 LKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1618 TERIKFMLQDAKSKLVIGEQkDLAAIVHPSIaTFAFNELFDETKVDlssykttvITPQHPAYL------IYTSGTTGQPK 1691
Cdd:PRK03640   88 REELLWQLDDAEVKCLITDD-DFEAKLIPGI-SVKFAELMNGPKEE--------AEIQEEFDLdevatiMYTSGTTGKPK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1692 GVMVSHQ----AIVNRILWMQseypLSATDTILQKTPcTFDVSVWE-FFWSYLVGARLVIAPidaHRDPLALLSLIQKYQ 1766
Cdd:PRK03640  158 GVIQTYGnhwwSAVGSALNLG----LTEDDCWLAAVP-IFHISGLSiLMRSVIYGMRVVLVE---KFDAEKINKLLQTGG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1767 VTTLHFVPSMLavfenaaTEILSSAQRQSLPI---CRVFCSGEALPTALAKsftehfsCELHNL-----YGPTEAAVDVs 1838
Cdd:PRK03640  230 VTIISVVSTML-------QRLLERLGEGTYPSsfrCMLLGGGPAPKPLLEQ-------CKEKGIpvyqsYGMTETASQI- 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1839 ymdATLGlhPEESCVAI---GYPVWNTQLYILDQyLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrm 1915
Cdd:PRK03640  295 ---VTLS--PEDALTKLgsaGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF------ 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1916 yRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVHAISSEQNKANVQlVAYLQTTAPVDIDQL 1995
Cdd:PRK03640  363 -KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVP-VAFVVKSGEVTEEEL 440
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 490930577 1996 KKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPH 2035
Cdd:PRK03640  441 RHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
21-434 1.94e-37

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: 147.56  E-value: 1.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   21 LASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASY---SSDPSQPFIELnnQVQFQIEE 97
Cdd:cd19066     4 LSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFceeAGRYEQVVLDK--TVRFRIEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   98 FDFCHLTPKKAqqRLWDWMPSDRQCAKSLKAGEtqLFRQVLFTTHD-KVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQ 176
Cdd:cd19066    82 IDLRNLADPEA--RLLELIDQIQQTIYDLERGP--LVRVALFRLADeRDVLVVAIHHIIVDGGSFQILFEDISSVYDAAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  177 EGKDLSVSPFIGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHHL-AAKTTATFVKHQLRFSTGILEQIQA 255
Cdd:cd19066   158 RQKPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRpSQVASYEVLTLEFFLRSEETKRLRE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  256 LAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLRE 335
Cdd:cd19066   238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSRE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  336 IRPHQKYDAEQILRDLNSIDIHER--MYGPILNYKAFDQ-DLVIDGEKVKT--HHISTGPIDDFEFSFIVQDH-ELIIEL 409
Cdd:cd19066   318 AIEHQRVPFIELVRHLGVVPEAPKhpLFEPVFTFKNNQQqLGKTGGFIFTTpvYTSSEGTVFDLDLEASEDPDgDLLLRL 397
                         410       420
                  ....*....|....*....|....*
gi 490930577  410 RADSQRYTQDELFNHGQRLTLLLEQ 434
Cdd:cd19066   398 EYSRGVYDERTIDRFAERYMTALRQ 422
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
1559-2031 2.40e-36

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: 144.51  E-value: 2.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1559 SFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG--- 1635
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTdsl 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1636 -EQKDLAAIVHPSIatfafnELFDETKVDLSSYkttvITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLS 1714
Cdd:TIGR01923   81 lEEKDFQADSLDRI------EAAGRYETSLSAS----FNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFT 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1715 ATDTILQKTPcTFDVSVWEFFW-SYLVGARLVIAPIDAhrdplALLSLIQKYQVTTLHFVPSMLavfenaaTEILSSAQR 1793
Cdd:TIGR01923  151 EDDNWLLSLP-LYHISGLSILFrWLIEGATLRIVDKFN-----QLLEMIANERVTHISLVPTQL-------NRLLDEGGH 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1794 QSLpICRVFCSGEALPTALAKSFTEHfSCELHNLYGPTEAAVDVSYMDaTLGLHPEEScvaIGYPVWNTQLYILdqylRP 1873
Cdd:TIGR01923  218 NEN-LRKILLGGSAIPAPLIEEAQQY-GLPIYLSYGMTETCSQVTTAT-PEMLHARPD---VGRPLAGREIKIK----VD 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1874 VPVGVdGELYLAGHQLAMGYLHRADLtasrfvaNPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:TIGR01923  288 NKEGH-GEIMVKGANLMKGYLYQGEL-------TPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIE 359
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577  1954 QQLRLISGLDVVVhAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:TIGR01923  360 TVLYQHPGIQEAV-VVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1528-2031 2.77e-36

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: 146.44  E-value: 2.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1528 YVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGA 1607
Cdd:COG1021    21 YWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 ayLPIdLQHPTER---IKFMLQDAKSKLVIGEQK-------DLAAIV---HPSIAT----------FAFNELFDEtKVDL 1664
Cdd:COG1021   101 --IPV-FALPAHRraeISHFAEQSEAVAYIIPDRhrgfdyrALARELqaeVPSLRHvlvvgdagefTSLDALLAA-PADL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1665 SSYkttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIV------NRILWMQSE------------YPLSAtdtilqktPCT 1726
Cdd:COG1021   177 SEP---RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLysvrasAEICGLDADtvylaalpaahnFPLSS--------PGV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1727 FDVsvwefFWsylVGARLVIAPiDAhrDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEilSSAQRQSLpicRVFCSGE 1806
Cdd:COG1021   246 LGV-----LY---AGGTVVLAP-DP--SPDTAFPLIERERVTVTALVPPLALLWLDAAER--SRYDLSSL---RVLQVGG 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1807 A-LPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDatlglHPEEScvaigypVWNTQ---------LYILDQYLRPVPV 1876
Cdd:COG1021   310 AkLSPELARRVRPALGCTLQQVFGMAEGLVNYTRLD-----DPEEV-------ILTTQgrpispddeVRIVDEDGNPVPP 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1877 GVDGELYLAGHQLAMGYlHRAD-LTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLkIR-GQRIELGEIEQ 1954
Cdd:COG1021   378 GEVGELLTRGPYTIRGY-YRAPeHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVEN 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1955 QLrlisgldvVVH-AIsseqnkANVQLV------------AYLQTT-APVDIDQLKKQL-AKHLPAYMVPTHYMLVEQFP 2019
Cdd:COG1021   450 LL--------LAHpAV------HDAAVVampdeylgerscAFVVPRgEPLTLAELRRFLrERGLAAFKLPDRLEFVDALP 515
                         570
                  ....*....|..
gi 490930577 2020 LSHNGKLDRKAL 2031
Cdd:COG1021   516 LTAVGKIDKKAL 527
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
1558-2031 8.33e-36

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: 143.41  E-value: 8.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVigeq 1637
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVL---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 kdlaaIVHPsiatfafnELFDETkvdlssykttviTPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATD 1717
Cdd:cd05969    77 -----ITTE--------ELYERT------------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 tilqKTPCTFDV-----SVWEFFWSYLVGARLVIapIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQ 1792
Cdd:cd05969   132 ----IYWCTADPgwvtgTVYGIWAPWLNGVTNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYD 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1793 RQSLpicRVFCS-GEAL-PTALAKSfTEHFSCELHNLYGPTEAAVDV--SY--MDATLGlhpeescvAIGYPVWNTQLYI 1866
Cdd:cd05969   206 LSSL---RFIHSvGEPLnPEAIRWG-MEVFGVPIHDTWWQTETGSIMiaNYpcMPIKPG--------SMGKPLPGVKAAV 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1867 LDQYLRPVPVGVDGELYLAGHQLAM--GYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:cd05969   274 VDENGNELPPGTKGILALKPGWPSMfrGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSG 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1945 QRIELGEIEQQL---RLISGLDVV--VHAISSEQNKANVQLVAYLQTTapvdiDQLKKQLAKH----LPAYMVPTHYMLV 2015
Cdd:cd05969   347 HRVGPFEVESALmehPAVAEAGVIgkPDPLRGEIIKAFISLKEGFEPS-----DELKEEIINFvrqkLGAHVAPREIEFV 421
                         490
                  ....*....|....*.
gi 490930577 2016 EQFPLSHNGKLDRKAL 2031
Cdd:cd05969   422 DNLPKTRSGKIMRRVL 437
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
1101-1494 1.38e-35

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: 142.16  E-value: 1.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQ-VENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFdSELAEEPVFIYSLHPTQAWPV 1179
Cdd:cd19066     2 IPLSPMQRGMWFLKKlATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF-CEEAGRYEQVVLDKTVRFRIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTPDLLEQTIQEALQQPIH--LDQPYG-LIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQQ- 1255
Cdd:cd19066    81 IIDLRNLADPEARLLELIDQIQQtiYDLERGpLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1256 --LPVLEHSYETVIKALSGR----DHETSKVIWQRDLADLQPLILFNQAQQAVQETSYR-------LSAELGAKLQHKLR 1322
Cdd:cd19066   161 ptLPPPVGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEvltleffLRSEETKRLREVAR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1323 QQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEH 1402
Cdd:cd19066   241 ESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1403 LEH-DGLGLSAIQQLIAQGNLFDSLL--VVENYPDNQYLQQKLGDAAISKL--TNRGYSHYPLALLVIPDHQIELLLE-- 1475
Cdd:cd19066   319 IEHqRVPFIELVRHLGVVPEAPKHPLfePVFTFKNNQQQLGKTGGFIFTTPvyTSSEGTVFDLDLEASEDPDGDLLLRle 398
                         410       420
                  ....*....|....*....|..
gi 490930577 1476 -QRGVIDQP--EHFLERMIQLI 1494
Cdd:cd19066   399 ySRGVYDERtiDRFAERYMTAL 420
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
1530-2031 1.02e-34

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 142.11  E-value: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVI 1603
Cdd:PRK13295   22 HDRTINDDLDACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACS 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1604 EAGAAY---LPIDLQHpteRIKFMLQDAKSKLVIGEQK----DLAAIV---HPSIATF------------AFNELFDETK 1661
Cdd:PRK13295  102 RIGAVLnplMPIFRER---ELSFMLKHAESKVLVVPKTfrgfDHAAMArrlRPELPALrhvvvvggdgadSFEALLITPA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1662 VDLSSYKTTVITPQHP-----AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSvweFFW 1736
Cdd:PRK13295  179 WEQEPDAPAILARLRPgpddvTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTG---FMY 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1737 SYLV----GARLVIAPIdahRDPLALLSLIQKYQVTtlhfvpsmlavFENAATEILS------SAQRQSLPICRVF-CSG 1805
Cdd:PRK13295  256 GLMMpvmlGATAVLQDI---WDPARAAELIRTEGVT-----------FTMASTPFLTdltravKESGRPVSSLRTFlCAG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1806 EALPTALAKSFTEHFSCELHNLYGPTE-AAVDVSYMDATlglhPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYL 1884
Cdd:PRK13295  322 APIPGALVERARAALGAKIVSAWGMTEnGAVTLTKLDDP----DERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQV 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1885 AGHQLAMGYLHRADLTAsrfvanpfTAGQRMYRTGDIARWHADGSIQYIGRADDQLkIRG-QRIELGEIEQQL-RLISGL 1962
Cdd:PRK13295  398 RGCSNFGGYLKRPQLNG--------TDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGgENIPVVEIEALLyRHPAIA 468
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1963 DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQL-AKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK13295  469 QVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
486-989 1.36e-34

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: 141.12  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  486 YPERTAIV---SGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYP 562
Cdd:cd17647     1 FPERTCVVetpSLNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  563 IDRMQMMCEDANPlfvlttQALaqqlpqniqqlhldqegvqTQIRKQDASDIPAENRKFDFqdvayvifTSGSTGRPKGV 642
Cdd:cd17647    81 PARQNIYLGVAKP------RGL-------------------IVIRAAGVVVGPDSNPTLSF--------TSGSEGIPKGV 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  643 MNTHGSLlnlilshkpTIYWPVLeavnerfpdrplraahthSFSFDSSWLQVFWMLWGqelhIFDENMRRDAFG---LVQ 719
Cdd:cd17647   128 LGRHFSL---------AYYFPWM------------------AKRFNLSENDKFTMLSG----IAHDPIQRDMFTplfLGA 176
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  720 EIQQRQIDTLDLPPSFCAQMMTNGLFVeNQHHPSL--ILIGGEAAPL------------------ALWQQLnaQPALFAH 779
Cdd:cd17647   177 QLLVPTQDDIGTPGRLAEWMAKYGATV-THLTPAMgqLLTAQATTPFpklhhaffvgdiltkrdcLRLQTL--AENVRIV 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  780 NLYGPTEytvdTFRA----ELKQTA---------RPVI--GNPIGNTQAYVLDRH--LQRCPTGVIGELYISGFGIANGY 842
Cdd:cd17647   254 NMYGTTE----TQRAvsyfEVPSRSsdptflknlKDVMpaGRGMLNVQLLVVNRNdrTQICGIGEVGEIYVRAGGLAEGY 329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  843 LGRADLSAARFVAN--------------------PFEHG--QRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGE 900
Cdd:cd17647   330 RGLPELNKEKFVNNwfvepdhwnyldkdnnepwrQFWLGprDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGE 409
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  901 VENALSILTNV-ESAVVIAEPINNSHRLLGYCVVKDIELDEKTSEQ---------------------LSQQYLSQLRQNL 958
Cdd:cd17647   410 IDTHISQHPLVrENITLVRRDKDEEPTLVSYIVPRFDKPDDESFAQedvpkevstdpivkgligyrkLIKDIREFLKKRL 489
                         570       580       590
                  ....*....|....*....|....*....|.
gi 490930577  959 PEYMVPSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:cd17647   490 ASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
1556-2011 2.40e-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: 139.27  E-value: 2.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1556 HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG 1635
Cdd:cd05907     4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1636 EqkdlaaivhpsiatfafnelfdetkvdlssykttviTPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSA 1715
Cdd:cd05907    84 E------------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1716 TDTILQKTPCT--FDVSVWEFFWSYLvGARLVIAPIDAhrdplALLSLIQKYQVTTLHFVPSML-AVFENAATEILSSAQ 1792
Cdd:cd05907   128 GDRHLSFLPLAhvFERRAGLYVPLLA-GARIYFASSAE-----TLLDDLSEVRPTVFLAVPRVWeKVYAAIKVKAVPGLK 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1793 RQ-----SLPICRVFCSGEA-LPTALAKSFtEHFSCELHNLYGPTE--AAVDVSymdatlglHPEESCVA-IGYPVWNTQ 1863
Cdd:cd05907   202 RKlfdlaVGGRLRFAASGGApLPAELLHFF-RALGIPVYEGYGLTEtsAVVTLN--------PPGDNRIGtVGKPLPGVE 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1864 LYIldqylrpvpvGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:cd05907   273 VRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDLIITS 336
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1944 -GQRIELGEIEQQLR---LISglDVVVHAissEQNKANVQLVAylqttapVDIDQLKKQLAKHLPAYMVPTH 2011
Cdd:cd05907   337 gGKNISPEPIENALKaspLIS--QAVVIG---DGRPFLVALIV-------PDPEALEAWAEEHGIAYTDVAE 396
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1523-1967 5.98e-34

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 140.62  E-value: 5.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1523 NQTQYYVRQSTLQQLLREQARITPEQTALSD-ENHQ---LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIA 1598
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkEDGIwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1599 ILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHPSIAT-------FAFNELFDETKVDLSSYKTTV 1671
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDElpslrhiVVLDPRGLRDDPRLLSLDELL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1672 ------------------ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILqktpctfdvS--- 1730
Cdd:COG1022   162 algrevadpaelearraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL---------Sflp 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1731 ---VWEFFWSYLV---GARLVIAPidahrDPLALLSLIQKYQVTTLHFVPsmlAVFENAATEILSSAQRQS--------- 1795
Cdd:COG1022   233 lahVFERTVSYYAlaaGATVAFAE-----SPDTLAEDLREVKPTFMLAVP---RVWEKVYAGIQAKAEEAGglkrklfrw 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1796 -------------------------LPI----------------CRVFCSG-EALPTALAKsFtehFSC---ELHNLYGP 1830
Cdd:COG1022   305 alavgrryararlagkspslllrlkHALadklvfsklrealggrLRFAVSGgAALGPELAR-F---FRAlgiPVLEGYGL 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1831 TEAAVDVSymdatlgLHPEESCVA--IGYPVWNTQLYIldqylrpvpvGVDGELYLAGHQLAMGYLHRADLTASRFVANP 1908
Cdd:COG1022   381 TETSPVIT-------VNRPGDNRIgtVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADG 443
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1909 FtagqrmYRTGDIARWHADGSIQYIGRADDQLKIR-GQRIELGEIEQQLR---LISglDVVVH 1967
Cdd:COG1022   444 W------LHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKaspLIE--QAVVV 498
PRK08316 PRK08316
acyl-CoA synthetase; Validated
1529-2026 9.20e-34

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 138.91  E-value: 9.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1529 VRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAA 1608
Cdd:PRK08316    8 ARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1609 YLPIDLQHPTERIKFMLQDAKSKLVIGEQkDLAAIVHPSIATFAFNELFDETKVDLSSYKTTVITPQH------------ 1676
Cdd:PRK08316   88 HVPVNFMLTGEELAYILDHSGARAFLVDP-ALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADwaeagsvaepdv 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 ------PAYLIYTSGTTGQPKGVMVSHQAIVnrilwmqSEY-------PLSATDTILQKTP---CT-FDVsvweFFWSYL 1739
Cdd:PRK08316  167 eladddLAQILYTSGTESLPKGAMLTHRALI-------AEYvscivagDMSADDIPLHALPlyhCAqLDV----FLGPYL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1740 -VGARLVI--APidahrDPLALLSLIQKYQVTTLhFVP-----SML--AVFEnaaTEILSSaqrqslpICRVFCSGEALP 1809
Cdd:PRK08316  236 yVGATNVIldAP-----DPELILRTIEAERITSF-FAPptvwiSLLrhPDFD---TRDLSS-------LRKGYYGASIMP 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1810 TALAKSFTEHF-SCELHNLYGPTEAAvdvSYmdATLgLHPEE------SCvaiGYPVWNTQLYILDQYLRPVPVGVDGEL 1882
Cdd:PRK08316  300 VEVLKELRERLpGLRFYNCYGQTEIA---PL--ATV-LGPEEhlrrpgSA---GRPVLNVETRVVDDDGNDVAPGEVGEI 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1883 YLAGHQLAMGYLHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL 1962
Cdd:PRK08316  371 VHRSPQLMLGYWDDPEKTAEAFRGGWF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAV 443
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1963 -DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKL 2026
Cdd:PRK08316  444 aEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
2144-2368 1.34e-33

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 130.20  E-value: 1.34e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  2144 PLFCFYPGSGSAWQYTVLNRYLHSDLPIIGLQSPRPDGLLANSTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYA 2223
Cdd:pfam00975    2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  2224 VAAKLTEQGEKVDYLGLLDTY-PAEIHQWLdlsveeMNAEAEQEQLQFFNDILADADSALSEEtrRLQEDIFANYRDAVR 2302
Cdd:pfam00975   82 VARRLERQGEAVRSLFLSDASaPHTVRYEA------SRAPDDDEVVAEFTDEGGTPEELLEDE--ELLSMLLPALRADYR 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  2303 LLKPYKMPHFDG-ELHLVVAEKDLLPYIQPEQQW-SPLVKKLNIVRLSEADHTDILS--PQQLETLGPIL 2368
Cdd:pfam00975  154 ALESYSCPPLDAqSATLFYGSDDPLHDADDLAEWvRDHTPGEFDVHVFDGDHFYLIEhlEAVLEIIEAKL 223
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
475-986 1.58e-33

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: 136.92  E-value: 1.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  475 VLDIFYEQVKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASF 554
Cdd:cd05936     1 LADLLEEAARRFPDKTALIFMGRK----LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  555 LPLDLDYPIDRMQMMCEDANPLFVLTTQALaqqlpqniqqlhldqegvQTQIRKQDASDIPAENRKfdfQDVAYVIFTSG 634
Cdd:cd05936    77 VPLNPLYTPRELEHILNDSGAKALIVAVSF------------------TDLLAAGAPLGERVALTP---EDVAVLQYTSG 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  635 STGRPKGVMNTHGSLL-NL--ILSHKPTIYWP---VLEAVnerfpdrPLraahTHSFSFDSSwLQVFWMLwGQELHIFDe 708
Cdd:cd05936   136 TTGVPKGAMLTHRNLVaNAlqIKAWLEDLLEGddvVLAAL-------PL----FHVFGLTVA-LLLPLAL-GATIVLIP- 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  709 nmRRDAFGLVQEIQQRQidtldlPPSFCAqmmTNGLFVENQHHP--------SLILIGGEAAPLALwQQLNAQPALFAHN 780
Cdd:cd05936   202 --RFRPIGVLKEIRKHR------VTIFPG---VPTMYIALLNAPefkkrdfsSLRLCISGGAPLPV-EVAERFEELTGVP 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  781 L---YGPTE----YTVDTFRAELKQTArpvIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARF 853
Cdd:cd05936   270 IvegYGLTEtspvVAVNPLDGPRKPGS---IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  854 VANPFehgqrmyRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLG---- 929
Cdd:cd05936   347 VDGWL-------RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVP----DPYSGeavk 415
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577  930 -YCVVKDielDEKTSEQlsqQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05936   416 aFVVLKE---GASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
1103-1329 9.13e-33

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 128.62  E-value: 9.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1103 LLPLQKGMLFLSQveNQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElAEEPVFIysLHPTQAWPVQFC 1182
Cdd:COG4908     1 LSPAQKRFLFLEP--GSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEE-DGEPVQR--IDPDADLPLEVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1183 SVT-------PDLLEQTIQEALQQPIHLDQPYgLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ---- 1251
Cdd:COG4908    76 DLSalpeperEAELEELVAEEASRPFDLARGP-LLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAAlleg 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1252 TNQQLPVLEHSYETVI----KALSGRDHETSKVIWQRDLADLQPLILF-------NQAQQAVQETSYRLSAELGAKLQHK 1320
Cdd:COG4908   155 EPPPLPELPIQYADYAawqrAWLQSEALEKQLEYWRQQLAGAPPVLELptdrprpAVQTFRGATLSFTLPAELTEALKAL 234

                  ....*....
gi 490930577 1321 LRQQGITLN 1329
Cdd:COG4908   235 AKAHGATVN 243
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
1100-1466 1.58e-32

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: 133.21  E-value: 1.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLF--LSQVENQSNYNAfTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFD-SELAEEPVFIYS-LHPTQ 1175
Cdd:cd19547     1 VYPLAPMQEGMLFrgLFWPDSDAYFNQ-NVLELVGGTDEDVLREAWRRVADRYEILRTGFTwRDRAEPLQYVRDdLAPPW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1176 A---WPVQFCSVTPDLLEQTIQEALQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ 1251
Cdd:cd19547    80 AlldWSGEDPDRRAELLERLLADDRAAGLSLADcP--LYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1252 TNQ-QLPVLE-----HSYETVIKALSGRDHETSKvIWQRDLADLQPLI----------LFNQAQQAVQETSYRLSAELGa 1315
Cdd:cd19547   158 LAHgREPQLSpcrpyRDYVRWIRARTAQSEESER-FWREYLRDLTPSPfstapadregEFDTVVHEFPEQLTRLVNEAA- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1316 klqhklRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQL 1395
Cdd:cd19547   236 ------RGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETI 309
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 1396 QQLHVEHLEHDGLGLSAIQ-----QLIAQGNLFDSLLVVENYPDNQYLQQKLGDAAISkLTNRGYSHYPLALLVIP 1466
Cdd:cd19547   310 HRDLATTAAHGHVPLAQIKswasgERLSGGRVFDNLVAFENYPEDNLPGDDLSIQIID-LHAQEKTEYPIGLIVLP 384
PRK06145 PRK06145
acyl-CoA synthetase; Validated
1542-2031 1.85e-32

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 134.24  E-value: 1.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGEQK--DLAAIVHPSIATFAFNelfdETKVDLSSYKTTVITPQHPA------YLIYTSGTTGQPKGV 1693
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEfdAIVALETPKIVIDAAA----QADSRRLAQGGLEIPPQAAVaptdlvRLMYTSGTTDRPKGV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1694 MVSHqaivNRILWMQSEYP----LSATDTILQKTPC----TFDVSVWEFFWsylVGARLVIapidaHR--DPLALLSLIQ 1763
Cdd:PRK06145  168 MHSY----GNLHWKSIDHVialgLTASERLLVVGPLyhvgAFDLPGIAVLW---VGGTLRI-----HRefDPEAVLAAIE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQVTTLHFVPSMLavfenaaTEILSSAQRQSLPICR---VFCSGEALPTALAKSFTEHFS-CELHNLYGPTEAAVDVSY 1839
Cdd:PRK06145  236 RHRLTCAWMAPVML-------SRVLTVPDRDRFDLDSlawCIGGGEKTPESRIRDFTRVFTrARYIDAYGLTETCSGDTL 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1840 MDATLGLhpeESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmyRTG 1919
Cdd:PRK06145  309 MEAGREI---EKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSG 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1920 DIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQ 1998
Cdd:PRK06145  379 DVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVaEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRH 458
                         490       500       510
                  ....*....|....*....|....*....|...
gi 490930577 1999 LAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06145  459 CRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
503-986 1.94e-32

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: 132.85  E-value: 1.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLdldypidrmqmmcedanplfvlTTQ 582
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPL----------------------TTL 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  583 ALAQQLPQNIQqlHLDQEGVQTqirkqdasdipaenrkfDFQDVAYVIFTSGSTGRPKGVMNTHGSLLnlilSHKPTIYW 662
Cdd:cd05972    59 LGPKDIEYRLE--AAGAKAIVT-----------------DAEDPALIYFTSGTTGLPKGVLHTHSYPL----GHIPTAAY 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  663 PVleavnerfpdrPLRAAHTHSFSFDSSWLQVFWM----LWGQELHIFDENMRR-DAFGLVQEIQQRQIDTLDLPPSFCA 737
Cdd:cd05972   116 WL-----------GLRPDDIHWNIADPGWAKGAWSsffgPWLLGATVFVYEGPRfDAERILELLERYGVTSFCGPPTAYR 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  738 QMMTNGLFVENQHHPSLILIGGEaaPL-----ALWQqlnAQPALFAHNLYGPTE--YTVDTFR-AELKQTArpvIGNPIG 809
Cdd:cd05972   185 MLIKQDLSSYKFSHLRLVVSAGE--PLnpeviEWWR---AATGLPIRDGYGQTEtgLTVGNFPdMPVKPGS---MGRPTP 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  810 NTQAYVLDRHLQRCPTGVIGELYI--SGFGIANGYLGRADLSAARFVANpfehgqrMYRTGDLVRWNSAGKLEFMGRCDD 887
Cdd:cd05972   257 GYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADD 329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  888 QIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLG-----YCVVKDielDEKTSEQLSQQYLSQLRQNLPEYM 962
Cdd:cd05972   330 IIKSSGYRIGPFEVESALLEHPAVAEAAVVGSP----DPVRGevvkaFVVLTS---GYEPSEELAEELQGHVKKVLAPYK 402
                         490       500
                  ....*....|....*....|....
gi 490930577  963 VPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05972   403 YPREIEFVEELPKTISGKIRRVEL 426
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
1558-2031 3.00e-32

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: 133.61  E-value: 3.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRaGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:cd05909     8 LTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 K--DLAAIVHPSIATFAFNELF-DETKVDLSSYKTTVI--------------------TPQHPAYLIYTSGTTGQPKGVM 1694
Cdd:cd05909    87 QfiEKLKLHHLFDVEYDARIVYlEDLRAKISKADKCKAflagkfppkwllrifgvapvQPDDPAVILFTSGSEGLPKGVV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVNRILWMQSEYPLSATDTILQKTPC----TFDVSVWEFFwsyLVGARLVIAPidahrDPL---ALLSLIQKYQV 1767
Cdd:cd05909   167 LSHKNLLANVEQITAIFDPNPEDVVFGALPFfhsfGLTGCLWLPL---LSGIKVVFHP-----NPLdykKIPELIYDKKA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1768 TTLHFVPSMLAVFENAATEilssaqrQSLPICR-VFCSGEALPTALAKSFTEHFSCELHNLYGPTEA----AVDVSYMDA 1842
Cdd:cd05909   239 TILLGTPTFLRGYARAAHP-------EDFSSLRlVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECspviSVNTPQSPN 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1843 tlglhpEESCVaiGYPVWNTQLYILD-QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTAsrfvanpFTAGQRMYRTGDI 1921
Cdd:cd05909   312 ------KEGTV--GRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDI 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1922 ARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVHAISSEQNKANVQLVAYLQTTAPvDIDQLKKQLAK 2001
Cdd:cd05909   377 GKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPDGRKGEKIVLLTTTTDT-DPSSLNDILKN 455
                         490       500       510
                  ....*....|....*....|....*....|.
gi 490930577 2002 H-LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05909   456 AgISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK13382 PRK13382
bile acid CoA ligase;
1542-2034 3.67e-31

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 131.03  E-value: 3.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:PRK13382   53 AQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPAL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGEQ-------KDLAAIVHP--SIA-TFAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPK 1691
Cdd:PRK13382  133 AEVVTREGVDTVIYDEefsatvdRALADCPQAtrIVAwTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILLTSGTTGTPK 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1692 GVMVSH-------QAIVNRIlwmqseyPLSATDTILQKTPCtfdVSVWEFfwSYLVGARLVIAPIDAHR--DPLALLSLI 1762
Cdd:PRK13382  213 GARRSGpggigtlKAILDRT-------PWRAEEPTVIVAPM---FHAWGF--SQLVLAASLACTIVTRRrfDPEATLDLI 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1763 QKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDA 1842
Cdd:PRK13382  281 DRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRF--AAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPA 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1843 TLGLHPEEScvaiGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADltasrfvaNPFTAGqrMYRTGDIA 1922
Cdd:PRK13382  359 DLRAAPDTA----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGST--------KDFHDG--FMASGDVG 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1923 RWHADGSIQYIGRADDQLKIRGQRIELGEIEqqlRLISGLDVVVHA--ISSEQNKANVQLVAYLQTT--APVDIDQLKKQ 1998
Cdd:PRK13382  425 YLDENGRLFVVGRDDEMIVSGGENVYPIEVE---KTLATHPDVAEAavIGVDDEQYGQRLAAFVVLKpgASATPETLKQH 501
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 490930577 1999 LAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQP 2034
Cdd:PRK13382  502 VRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
1677-2031 5.91e-31

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: 125.91  E-value: 5.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 PAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPcTFDVSVWEFFW-SYLVGARLVIAPidahRDP 1755
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVrSLLAGAELVLLE----RNQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1756 LALLSLiQKYQVTTLHFVPSMLavfENAATEILSSAQRQSLPicRVFCSGEALPTALAKSFTEHfSCELHNLYGPTEAAV 1835
Cdd:cd17630    77 ALAEDL-APPGVTHVSLVPTQL---QRLLDSGQGPAALKSLR--AVLLGGAPIPPELLERAADR-GIPLYTTYGMTETAS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1836 DVSymDATLGLHPEESCvaiGYPVWNTQLYILDqylrpvpvgvDGELYLAGHQLAMGYLhradltasRFVANPFTAGQRM 1915
Cdd:cd17630   150 QVA--TKRPDGFGRGGV---GVLLPGRELRIVE----------DGEIWVGGASLAMGYL--------RGQLVPEFNEDGW 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1916 YRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEqnKANVQLVAYLQTTAPVDIDQ 1994
Cdd:cd17630   207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAvRDAFVVGVPDE--ELGQRPVAVIVGRGPADPAE 284
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 490930577 1995 LKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd17630   285 LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
491-981 2.77e-30

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: 127.71  E-value: 2.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  491 AIVSGErpNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMC 570
Cdd:cd05911     1 AQIDAD--TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  571 EDANPLFVLTTQAL------AQQLPQNIQQLHLDQEGVQTQIRKQDASDIPAENRKFDF--------QDVAYVIFTSGST 636
Cdd:cd05911    79 KISKPKVIFTDPDGlekvkeAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLppplkdgkDDTAAILYSSGTT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  637 GRPKGVMNTHgslLNLILSHKPTIYwpvLEAVNERFPDR-----PLraahTHSFSFdssWLQVFWMLWGQELHIfdenMR 711
Cdd:cd05911   159 GLPKGVCLSH---RNLIANLSQVQT---FLYGNDGSNDVilgflPL----YHIYGL---FTTLASLLNGATVII----MP 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  712 R---DAFglVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQhHPSLILIGGEAAPLA--LWQQLNAQ-PALFAHNLYGPT 785
Cdd:cd05911   222 KfdsELF--LDLIEKYKITFLYLVPPIAAALAKSPLLDKYD-LSSLRVILSGGAPLSkeLQELLAKRfPNATIKQGYGMT 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  786 EYTVDTFRAELKQTARPVIGNPIGNTQAYVLDRHL-QRCPTGVIGELYISGFGIANGYLGRADLSAARFvanpFEHGqrM 864
Cdd:cd05911   299 ETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETF----DEDG--W 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  865 YRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKdiELDEKTSE 944
Cdd:cd05911   373 LHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVR--KPGEKLTE 450
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 490930577  945 QLSQQYLSqlrQNLPEYmvpSALT----VMSEFPRNVSGKV 981
Cdd:cd05911   451 KEVKDYVA---KKVASY---KQLRggvvFVDEIPKSASGKI 485
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
1531-2029 3.14e-30

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 128.58  E-value: 3.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1531 QSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAA-- 1608
Cdd:PRK05605   31 DTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvv 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1609 -----YLPIDLQHPTER---------------------------------IKFM--LQDAKSKLVIGEQKDL-AAIVHPS 1647
Cdd:PRK05605  111 ehnplYTAHELEHPFEDhgarvaivwdkvaptverlrrttpletivsvnmIAAMplLQRLALRLPIPALRKArAALTGPA 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1648 IATFAFNELFDET---KVDLSSYKTtvITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL----WMQSeyplsatdtiL 1720
Cdd:PRK05605  191 PGTVPWETLVDAAiggDGSDVSHPR--PTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkaWVPG----------L 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1721 QKTPCTFdVSVWEFFWSY----------LVGARLVIAPidAHRDPLaLLSLIQKYQVTtlhFVPSMLAVFENaateILSS 1790
Cdd:PRK05605  259 GDGPERV-LAALPMFHAYgltlcltlavSIGGELVLLP--APDIDL-ILDAMKKHPPT---WLPGVPPLYEK----IAEA 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1791 AQRQSLPICRV---FCSGEALPTALAKSFTEHFSCELHNLYGPTEAAvdvsymDATLG--LHPEESCVAIGYPVWNTQLY 1865
Cdd:PRK05605  328 AEERGVDLSGVrnaFSGAMALPVSTVELWEKLTGGLLVEGYGLTETS------PIIVGnpMSDDRRPGYVGVPFPDTEVR 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1866 ILDQ--YLRPVPVGVDGELYLAGHQLAMGYLHRADLTasrfvANPFTAGqrMYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:PRK05605  402 IVDPedPDETMPDGEEGELLVRGPQVFKGYWNRPEET-----AKSFLDG--WFRTGDVVVMEEDGFIRIVDRIKELIITG 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1944 GQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSH 2022
Cdd:PRK05605  475 GFNVYPAEVEEVLREHPGVeDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQ 554

                  ....*..
gi 490930577 2023 NGKLDRK 2029
Cdd:PRK05605  555 LGKVRRR 561
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
1543-2026 3.28e-30

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: 128.85  E-value: 3.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1543 RITPEQTAL---SDENHQ---LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:cd17634    64 RENGDRTAIiyeGDDTSQsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVI--------GEQKDLAAIV----HPSIATFAFNELFDETKVDL------------------SS 1666
Cdd:cd17634   144 APEAVAGRIIDSSSRLLItadggvraGRSVPLKKNVddalNPNVTSVEHVIVLKRTGSDIdwqegrdlwwrdliakasPE 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1667 YKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILW-MQSEYPLSATDTILqktpCTFDVSvWEFFWSYLV----- 1740
Cdd:cd17634   224 HQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATtMKYVFDYGPGDIYW----CTADVG-WVTGHSYLLygpla 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1741 -GARLVI---APIdaHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLPIcrVFCSGEALPTALAKSF 1816
Cdd:cd17634   299 cGATTLLyegVPN--WPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRI--LGSVGEPINPEAYEWY 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1817 TEHFS---CELHNLYGPTEAA-VDVSYMDATLGLHPEESCVaigyPVWNTQLYILDQYLRPVPVGVDGELYLAGH--QLA 1890
Cdd:cd17634   375 WKKIGkekCPVVDTWWQTETGgFMITPLPGAIELKAGSATR----PVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQT 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1891 MGYLHRADltasRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL----RLISGLDV-V 1965
Cdd:cd17634   451 RTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLvahpKVAEAAVVgI 526
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1966 VHAISSEQNKANVQLVAYLqTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKL 2026
Cdd:cd17634   527 PHAIKGQAPYAYVVLNHGV-EPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
1104-1382 4.01e-30

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: 125.93  E-value: 4.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1104 LPL---QKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElAEEPV-FIyslHPTQAWP 1178
Cdd:cd19531     2 LPLsfaQQRLWFLDQLEPGSAaYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEV-DGEPVqVI---LPPLPLP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1179 VQFCSVTPDL-------LEQTIQEALQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAY- 1249
Cdd:cd19531    78 LPVVDLSGLPeaereaeAQRLAREEARRPFDLARgP--LLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYa 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1250 ---QQTNQQLPVLEHSYetvikalsgRDHetskVIWQRD-----------------LADLQPLI--LFNQAQQAVQetSY 1307
Cdd:cd19531   156 aflAGRPSPLPPLPIQY---------ADY----AVWQREwlqgevlerqlaywreqLAGAPPVLelPTDRPRPAVQ--SF 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1308 R-------LSAELGAKLQhKL-RQQGITLnvFMQMI--WAMTLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIP 1377
Cdd:cd19531   221 RgarvrftLPAELTAALR-ALaRREGATL--FMTLLaaFQVLLHRYSGQDDIVVGTPVAGRNRA--ELEGLIGFFVNTLV 295

                  ....*
gi 490930577 1378 VRVKL 1382
Cdd:cd19531   296 LRTDL 300
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
512-986 4.14e-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: 126.40  E-value: 4.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  512 VNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGAS----FLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQ 587
Cdd:cd05922     3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  588 LPQNIQQLHLDQEGVQTQIRKQDASDIPA-ENRKfdfQDVAYVIFTSGSTGRPKGVMNTHGSLLNlilshkptiywpVLE 666
Cdd:cd05922    83 LRDALPASPDPGTVLDADGIRAARASAPAhEVSH---EDLALLLYTSGSTGSPKLVRLSHQNLLA------------NAR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  667 AVNERFPDRPL-RAAHTHSFSFDSSWLQVF-WMLWGQELHIFDENMRRDAFglVQEIQQRQIDTLDLPPSFCAQMMTNGL 744
Cdd:cd05922   148 SIAEYLGITADdRALTVLPLSYDYGLSVLNtHLLRGATLVLTNDGVLDDAF--WEDLREHGATGLAGVPSTYAMLTRLGF 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  745 fvENQHHPSLILI--GGEAAPLALWQQLN-AQPALFAHNLYGPTEYT--VDTFRAELKQTARPVIGNPIGNTQAYVLDRH 819
Cdd:cd05922   226 --DPAKLPSLRYLtqAGGRLPQETIARLReLLPGAQVYVMYGQTEATrrMTYLPPERILEKPGSIGLAIPGGEFEILDDD 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  820 LQRCPTGVIGELYISGfgiANGYLGRADlsAARFVANPFEHGQRMYrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIG 899
Cdd:cd05922   304 GTPTPPGEPGEIVHRG---PNVMKGYWN--DPPYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPT 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  900 EVENALSILTNVESAVVIAEPINNSHRLLgYCVVKDIELDEKTSeqlsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSG 979
Cdd:cd05922   378 EIEAAARSIGLIIEAAAVGLPDPLGEKLA-LFVTAPDKIDPKDV-------LRSLAERLPPYKVPATVRVVDELPLTASG 449

                  ....*..
gi 490930577  980 KVDKKAL 986
Cdd:cd05922   450 KVDYAAL 456
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
1530-2031 5.33e-30

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 130.81  E-value: 5.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTALSDE-NHQLSFSEVRLQVCALAQQLQRaGVQAGDIVAVALPRSVKLSIAILAVIEAGAA 1608
Cdd:PRK08633  613 ALPPLAEAWIDTAKRNWSRLAVADStGGELSYGKALTGALALARLLKR-ELKDEENVGILLPPSVAGALANLALLLAGKV 691
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1609 ylPIDLQHPTER--IKFMLQDAKSKLVIG--------EQKDLAAIVHPSIATFAFNELFDE-TKVD-------------- 1663
Cdd:PRK08633  692 --PVNLNYTASEaaLKSAIEQAQIKTVITsrkfleklKNKGFDLELPENVKVIYLEDLKAKiSKVDkltallaarllpar 769
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1664 -LSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPctfdvsvweFFWSY---- 1738
Cdd:PRK08633  770 lLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLP---------FFHSFgltv 840
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1739 ------LVGARLViapidAHRDPL---ALLSLIQKYQVTTLHFVPSMLAVFenAATEILSSAQRQSLPIcrVFCSGEALP 1809
Cdd:PRK08633  841 tlwlplLEGIKVV-----YHPDPTdalGIAKLVAKHRATILLGTPTFLRLY--LRNKKLHPLMFASLRL--VVAGAEKLK 911
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1810 TALAKSFTEHFSCELHNLYGPTE----AAVDV-SYMDATLGLHPEESCVAIGYPVWNTQLYILD-QYLRPVPVGVDGELY 1883
Cdd:PRK08633  912 PEVADAFEEKFGIRILEGYGATEtspvASVNLpDVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLIL 991
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1884 LAGHQLAMGYLHRADLTASRFVAnpfTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-- 1961
Cdd:PRK08633  992 IGGPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGge 1068
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1962 -LDVVVHAISSEqnKANVQLVAyLQTTAPVDIDQLKKQLAK-HLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK08633 1069 eVVFAVTAVPDE--KKGEKLVV-LHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
1542-1999 7.60e-30

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: 127.35  E-value: 7.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGvQAGDIVAVALPRSVKLSIAILAVIEAGA----AYLP 1611
Cdd:cd05931     3 AAARPDRPAYtflddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAiavpLPPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1612 iDLQHPTERIKFMLQDAKSKLVIGEQKDLAAiVHPSIATFAFNELFDETKVDL------SSYKTTVITPQHPAYLIYTSG 1685
Cdd:cd05931    82 -TPGRHAERLAAILADAGPRVVLTTAAALAA-VRAFAASRPAAGTPRLLVVDLlpdtsaADWPPPSPDPDDIAYLQYTSG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1686 TTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEF-FWSYLVGARLV-IAPIDAHRDPLALLSLIQ 1763
Cdd:cd05931   160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGPSVlMSPAAFLRRPLRWLRLIS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQVTTlHFVPSMlAvFENAATEIlSSAQRQSLPICRV---FCSGEAL-PTALAKsFTEHFSCelHNL--------YGPT 1831
Cdd:cd05931   240 RYRATI-SAAPNF-A-YDLCVRRV-RDEDLEGLDLSSWrvaLNGAEPVrPATLRR-FAEAFAP--FGFrpeafrpsYGLA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1832 EAAVDVS-----------YMDATLGLHPEESC----------VAIGYPVWNTQLYILD-QYLRPVPVGVDGELYLAGHQL 1889
Cdd:cd05931   313 EATLFVSggppgtgpvvlRVDRDALAGRAVAVaaddpaarelVSCGRPLPDQEVRIVDpETGRELPDGEVGEIWVRGPSV 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1890 AMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHaDGSIqYI-GRADDQLKIRGQRIELGEIEQQLRLISGL----DV 1964
Cdd:cd05931   393 ASGYWGRPEATAETFGALAATDEGGWLRTGDLGFLH-DGEL-YItGRLKDLIIVRGRNHYPQDIEATAEEAHPAlrpgCV 470
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 490930577 1965 VVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQL 1999
Cdd:cd05931   471 AAFSVPDDGEERLVVVAEVERGADPADLAAIAAAI 505
PRK09088 PRK09088
acyl-CoA synthetase; Validated
1541-2031 8.24e-30

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 126.07  E-value: 8.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1541 QARITPEQTALSD--ENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPT 1618
Cdd:PRK09088    4 HARLQPQRLAAVDlaLGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1619 ERIKFMLQDAKSKLVIGEQKdLAAIVHPSIATFAFNELFDETKVDLSSYkttvITPQHPAYLIYTSGTTGQPKGVMVSHQ 1698
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDA-VAAGRTDVEDLAAFIASADALEPADTPS----IPPERVSLILFTSGTSGQPKGVMLSER 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1699 AIVNRILWMQSEYPLSATDTILQKTPctfdvsvweFFwsYLVGARLVIAPIDAHR---------DPLALLSLIQKYQVTT 1769
Cdd:PRK09088  159 NLQQTAHNFGVLGRVDAHSSFLCDAP---------MF--HIIGLITSVRPVLAVGgsilvsngfEPKRTLGRLGDPALGI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1770 LHF--VPSMLAVFENAATEILSSAQRqslpICRVFCSGEALPTALAKSFTEHfSCELHNLYGPTEA------AVDVSYMD 1841
Cdd:PRK09088  228 THYfcVPQMAQAFRAQPGFDAAALRH----LTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAgtvfgmSVDCDVIR 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1842 ATLGlhpeescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFvanpftAGQRMYRTGDI 1921
Cdd:PRK09088  303 AKAG--------AAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDI 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1922 ARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLA 2000
Cdd:PRK09088  369 ARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIrECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLS 448
                         490       500       510
                  ....*....|....*....|....*....|.
gi 490930577 2001 KHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK09088  449 TRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
1542-2033 1.08e-29

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: 126.46  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTAL-----SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:cd05970    27 AKEYPDKLALvwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKD-----------------LAAIVHPSIAT--FAFNELFDETKVDLSSYKTTVITPQHP 1677
Cdd:cd05970   107 TAKDIVYRIESADIKMIVAIAEDnipeeiekaapecpskpKLVWVGDPVPEgwIDFRKLIKNASPDFERPTANSYPCGED 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 AYLIY-TSGTTGQPKgvMVSHQ------AIVNRILWMQSE---YPLSATDTILQKtpctfdvSVW-EFFWSYLVGARLVI 1746
Cdd:cd05970   187 ILLVYfSSGTTGMPK--MVEHDftyplgHIVTAKYWQNVReggLHLTVADTGWGK-------AVWgKIYGQWIAGAAVFV 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1747 APIDAHrDPLALLSLIQKYQVTTLHFVPSmlaVFENAATEILSSAQRQSLPICRVfcSGEALPTALAKSFTEHFSCELHN 1826
Cdd:cd05970   258 YDYDKF-DPKALLEKLSKYGVTTFCAPPT---IYRFLIREDLSRYDLSSLRYCTT--AGEALNPEVFNTFKEKTGIKLME 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1827 LYGPTEAAVDV---SYMDATLGlhpeescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYL---AGHQLAM--GYLHRAD 1898
Cdd:cd05970   332 GFGQTETTLTIatfPWMEPKPG--------SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVGLfgGYYKDAE 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1899 LTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIelGEIEQQLRLISGLDVVVHAISSEQN---- 1974
Cdd:cd05970   404 KTAEVWHDG-------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRI--GPFEVESALIQHPAVLECAVTGVPDpirg 474
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 1975 ---KANVQLVAYLQTTapvdiDQLKKQLAKHLPAYMVPTHY----MLVEQFPLSHNGKLDRKALPQ 2033
Cdd:cd05970   475 qvvKATIVLAKGYEPS-----EELKKELQDHVKKVTAPYKYprivEFVDELPKTISGKIRRVEIRE 535
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
488-986 6.72e-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: 122.40  E-value: 6.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  488 ERTAIVSGERpnlqHLSFAELAVKVNQL-TRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd05941     1 DRIAIVDDGD----SITYADLVARAARLaNRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  567 QMMCEDANPLFVLttqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfqDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd05941    77 EYVITDSEPSLVL---------------------------------------------DPALILYTSGTTGRPKGVVLTH 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  647 GSLLNLILShkptiywpVLEAVNERFPDR-----PLRaaHTHSFsfdssWLQVFWMLW-GQELHI---FD---ENMRRD- 713
Cdd:cd05941   112 ANLAANVRA--------LVDAWRWTEDDVllhvlPLH--HVHGL-----VNALLCPLFaGASVEFlpkFDpkeVAISRLm 176
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  714 ----AFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLfvenqHHPSLILIGGEAAP---LALWQQLNAQPALfahNLYGPTE 786
Cdd:cd05941   177 psitVFMGVPTIYTRLLQYYEAHFTDPQFARAAAA-----ERLRLMVSGSAALPvptLEEWEAITGHTLL---ERYGMTE 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  787 yTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRC-PTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrm 864
Cdd:cd05941   249 -IGMALSNPLDGERRPgTVGMPLPGVQARIVDEETGEPlPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------ 321
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  865 YRTGDLVRWNSAGKLEFMGR-CDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIELdEKTS 943
Cdd:cd05941   322 FKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVP----DPDWGERVVAVVVL-RAGA 396
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 490930577  944 EQLS-QQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05941   397 AALSlEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
492-986 7.07e-29

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: 123.58  E-value: 7.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  492 IVSGERPNLqhlSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCE 571
Cdd:cd05926     7 VVPGSTPAL---TYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  572 DANPLFVLT-------TQALAQQLPQNIQQLHLDqegVQTQIRKQDASDIPAENRKFDFQ---------DVAYVIFTSGS 635
Cdd:cd05926    84 DLGSKLVLTpkgelgpASRAASKLGLAILELALD---VGVLIRAPSAESLSNLLADKKNAksegvplpdDLALILHTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  636 TGRPKGVMNTHGSLL----NLILSHKPTiywpvleavnerFPDR-----PLraAHTHSF------------------SFD 688
Cdd:cd05926   161 TGRPKGVPLTHRNLAasatNITNTYKLT------------PDDRtlvvmPL--FHVHGLvasllstlaaggsvvlppRFS 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  689 SSwlqVFWmlwgqelhifdenmrrdafglvQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGEAAPLALwQ 768
Cdd:cd05926   227 AS---TFW----------------------PDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPP-A 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  769 QLNAQPALFAHNL---YGPTEYTVDTFRAELKQTARPV--IGNPIGnTQAYVLDRHLQRCPTGVIGELYISGFGIANGYL 843
Cdd:cd05926   281 VLEALEATFGAPVleaYGMTEAAHQMTSNPLPPGPRKPgsVGKPVG-VEVRILDEDGEILPPGVVGEICLRGPNVTRGYL 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  844 GRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinn 923
Cdd:cd05926   360 NNPEANAEAAFKDGW------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVP--- 430
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577  924 sHRLLGYCVVKDIELDEK---TSEQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05926   431 -DEKYGEEVAAAVVLREGasvTEEEL----RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
PRK06178 PRK06178
acyl-CoA synthetase; Validated
1526-2031 1.96e-28

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 123.23  E-value: 1.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1526 QYYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEA 1605
Cdd:PRK06178   27 EYPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1606 GAAYLPIDLQHPTERIKFMLQDAKSKLVIG------------EQKDLAAIVH-------PSIATFAFNELFDETKV---- 1662
Cdd:PRK06178  107 GAVHVPVSPLFREHELSYELNDAGAEVLLAldqlapvveqvrAETSLRHVIVtsladvlPAEPTLPLPDSLRAPRLaaag 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1663 --DL--SSYKTTVITPQHPAYLI------YTSGTTGQPKGVMVSHQaivNRILWMQSEYPLSATDTilqkTPCTFdVSVW 1732
Cdd:PRK06178  187 aiDLlpALRACTAPVPLPPPALDalaalnYTGGTTGMPKGCEHTQR---DMVYTAAAAYAVAVVGG----EDSVF-LSFL 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1733 EFFW----------SYLVGARLVIApidAHRDPLALLSLIQKYQVTtlhfvpSMLAVFENAAtEIL---SSAQR--QSLP 1797
Cdd:PRK06178  259 PEFWiagenfgllfPLFSGATLVLL---ARWDAVAFMAAVERYRVT------RTVMLVDNAV-ELMdhpRFAEYdlSSLR 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1798 ICRVFCSGEALPTALAKSFTEHFSCELHNL-YGPTEA----AVDVSYMDATLGLHPEEscVAIGYPVWNTQLYILD-QYL 1871
Cdd:PRK06178  329 QVRVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTEThtcdTFTAGFQDDDFDLLSQP--VFVGLPVPGTEFKICDfETG 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1872 RPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGE 1951
Cdd:PRK06178  407 ELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSE 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1952 IEQQLRL---ISGLDVVVHAissEQNKANVQlVAYLQTT--APVDIDQLKKQLAKHLPAYMVPTHYmLVEQFPLSHNGKL 2026
Cdd:PRK06178  480 VEALLGQhpaVLGSAVVGRP---DPDKGQVP-VAFVQLKpgADLTAAALQAWCRENMAVYKVPEIR-IVDALPMTATGKV 554

                  ....*
gi 490930577 2027 DRKAL 2031
Cdd:PRK06178  555 RKQDL 559
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
1531-2026 2.15e-28

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 122.76  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1531 QSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRA-GVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:PRK08314    9 ETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKFMLQDAKSKLVIGEQkDLAAIVHPSIATFAF---------NELFDETKVDLSSYKTT---------- 1670
Cdd:PRK08314   89 VPVNPMNREEELAHYVTDSGARVAIVGS-ELAPKVAPAVGNLRLrhvivaqysDYLPAEPEIAVPAWLRAepplqalapg 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1671 ------------------VITPQHPAYLIYTSGTTGQPKGVMVSHQ----AIVNRILWMQSeyplSATDTILQKTPcTFD 1728
Cdd:PRK08314  168 gvvawkealaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRtvmaNAVGSVLWSNS----TPESVVLAVLP-LFH 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1729 VS--VWEFFWSYLVGARLVIAPI-DahRDplALLSLIQKYQVTTLHFVPSMLAVFenaateiLSSAQRQSLPICRVFC-- 1803
Cdd:PRK08314  243 VTgmVHSMNAPIYAGATVVLMPRwD--RE--AAARLIERYRVTHWTNIPTMVVDF-------LASPGLAERDLSSLRYig 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1804 -SGEALPTALAKSFTEHFSCELHNLYGPTE--AAVDVSYMDatlglHPEESCVAIgyPVWNTQLYILD-QYLRPVPVGVD 1879
Cdd:PRK08314  312 gGGAAMPEAVAERLKELTGLDYVEGYGLTEtmAQTHSNPPD-----RPKLQCLGI--PTFGVDARVIDpETLEELPPGEV 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1880 GELYLAGHQLAMGYLHRADLTASRFVAnpfTAGQRMYRTGDIARWHADGsiqYIGRAdDQLK----IRGQRIELGEIE-- 1953
Cdd:PRK08314  385 GEIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEG---YFFIT-DRLKrminASGFKVWPAEVEnl 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1954 -------QQLRLISGLDvvvhAISSEQNKANVQLVA-YLQTTAPVDIDQLKKQlakHLPAYMVPTHYMLVEQFPLSHNGK 2025
Cdd:PRK08314  458 lykhpaiQEACVIATPD----PRRGETVKAVVVLRPeARGKTTEEEIIAWARE---HMAAYKYPRIVEFVDSLPKSGSGK 530

                  .
gi 490930577 2026 L 2026
Cdd:PRK08314  531 I 531
PRK06188 PRK06188
acyl-CoA synthetase; Validated
1535-2031 3.16e-28

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 122.02  E-value: 3.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1535 QQLLREQARiTPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIdl 1614
Cdd:PRK06188   16 HLLVSALKR-YPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1615 qHPT---ERIKFMLQDAKSK-LVIGEQK------DLAAIVhPSI-ATFAFNELfdETKVDLSSYKTTV--------ITPQ 1675
Cdd:PRK06188   93 -HPLgslDDHAYVLEDAGIStLIVDPAPfveralALLARV-PSLkHVLTLGPV--PDGVDLLAAAAKFgpaplvaaALPP 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1676 HPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTfDVSVWEFFWSYLVGARLVIAPidaHRDP 1755
Cdd:PRK06188  169 DIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLS-HAGGAFFLPTLLRGGTVIVLA---KFDP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1756 LALLSLIQKYQVTTLHFVPSMLAVF---ENAATEILSSAQrqslpicRVFCSGEAL-PTALAKSFtEHFSCELHNLYGPT 1831
Cdd:PRK06188  245 AEVLRAIEEQRITATFLVPTMIYALldhPDLRTRDLSSLE-------TVYYGASPMsPVRLAEAI-ERFGPIFAQYYGQT 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1832 EAAVDVSYM--DATLGLHPE--ESCvaiGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFvan 1907
Cdd:PRK06188  317 EAPMVITYLrkRDHDPDDPKrlTSC---GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF--- 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1908 pftAGQRMyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEqqlrlisglDVVV--HAISS--------EQNKAN 1977
Cdd:PRK06188  391 ---RDGWL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVE---------DVLAehPAVAQvavigvpdEKWGEA 457
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 490930577 1978 VQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06188  458 VTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
1537-2025 7.67e-28

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: 120.10  E-value: 7.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:cd12118     9 FLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKdlaaivhpsiatFAFNELFDETKVDLssyktTVITPQ---HPAYLIYTSGTTGQPKGV 1693
Cdd:cd12118    89 DAEEIAFILRHSEAKVLFVDRE------------FEYEDLLAEGDPDF-----EWIPPAdewDPIALNYTSGTTGRPKGV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1694 MVSH-----QAIVNRILWMQSEYPlsatdTILQKTPcTFDVSVWEFFWS-YLVGARLVIAPidaHRDPLALLSLIQKYQV 1767
Cdd:cd12118   152 VYHHrgaylNALANILEWEMKQHP-----VYLWTLP-MFHCNGWCFPWTvAAVGGTNVCLR---KVDAKAIYDLIEKHKV 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1768 TtlHF--VPSMLAVFENAAteilsSAQRQSLP-ICRVFCSGEALPTALAKSFTEHFSCELHnLYGPTEA---AVDVSYMD 1841
Cdd:cd12118   223 T--HFcgAPTVLNMLANAP-----PSDARPLPhRVHVMTAGAPPPAAVLAKMEELGFDVTH-VYGLTETygpATVCAWKP 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1842 ATLGLHPEESCV-----AIGYPVwNTQLYILD-QYLRPVPV-GVD-GELYLAGHQLAMGYLHRADLTASRFvanpftAGQ 1913
Cdd:cd12118   295 EWDELPTEERARlkarqGVRYVG-LEEVDVLDpETMKPVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEAF------RGG 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1914 rMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQ----NKANVQLVAYLQTTA 1988
Cdd:cd12118   368 -WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAvLEAAVVARPDEKwgevPCAFVELKEGAKVTE 446
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 490930577 1989 pvdiDQLKKQLAKHLPAYMVPTHYMLVEqFPLSHNGK 2025
Cdd:cd12118   447 ----EEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
PRK06164 PRK06164
acyl-CoA synthetase; Validated
1530-2033 1.27e-27

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 120.23  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:PRK06164    8 RADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKFMLQDAKSKLVIGEQK----DLAAI---VHPSI-----ATFAFNELFDETKVDLSsYKTTVITPQH- 1676
Cdd:PRK06164   88 IAVNTRYRSHEVAHILGRGRARWLVVWPGfkgiDFAAIlaaVPPDAlpplrAIAVVDDAADATPAPAP-GARVQLFALPd 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 ----------------PAYLIYTSGTTGQPKGVM------VSHQAIVNRIlwmqseYPLSATDTILQKTP-CTFdvsvwe 1733
Cdd:PRK06164  167 pappaaageraadpdaGALLFTTSGTTSGPKLVLhrqatlLRHARAIARA------YGYDPGAVLLAALPfCGV------ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1734 FFWSYLV-----GARLVIAPI-DAHRDplalLSLIQKYQVTtlHFVPSmlavfENAATEILSSA-QRQSLPICRVF---- 1802
Cdd:PRK06164  235 FGFSTLLgalagGAPLVCEPVfDAART----ARALRRHRVT--HTFGN-----DEMLRRILDTAgERADFPSARLFgfas 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1803 ---CSGEALPTALAKSFTehfsceLHNLYGPTEAAVDVSYMDATLglhPE-ESCVAIGYPVW-NTQLYILD-QYLRPVPV 1876
Cdd:PRK06164  304 fapALGELAALARARGVP------LTGLYGSSEVQALVALQPATD---PVsVRIEGGGRPASpEARVRARDpQDGALLPD 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1877 GVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL 1956
Cdd:PRK06164  375 GESGEIEIRAPSLMRGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHAL 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1957 RLISGL-DVVVHAISSEQNKANVQLVAyLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFP--LSHNG-KLDRKALP 2032
Cdd:PRK06164  449 EALPGVaAAQVVGATRDGKTVPVAFVI-PTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPvtESANGaKIQKHRLR 527

                  .
gi 490930577 2033 Q 2033
Cdd:PRK06164  528 E 528
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
1549-2035 2.69e-27

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 119.03  E-value: 2.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1549 TALSDENHqLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDA 1628
Cdd:PRK12406    4 TIISGDRR-RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1629 KSKLVIGeQKDLAAIVHPSI--------------------------ATFAFNELFDETKVDLSSYkTTVITPQhPAYLIY 1682
Cdd:PRK12406   83 GARVLIA-HADLLHGLASALpagvtvlsvptppeiaaayrispallTPPAGAIDWEGWLAQQEPY-DGPPVPQ-PQSMIY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1683 TSGTTGQPKGV---------MVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFfwsylvGARLVIAPidaHR 1753
Cdd:PRK12406  160 TSGTTGHPKGVrraaptpeqAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRL------GGVLVLQP---RF 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1754 DPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLpicRVFCSGEA-LPTALAKSFTEHFSCELHNLYGPTE 1832
Cdd:PRK12406  231 DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSL---RHVIHAAApCPADVKRAMIEWWGPVIYEYYGSTE 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1833 AAVdVSYMDATLGL-HPEescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLA----------GHQLAMGYLHRADLTA 1901
Cdd:PRK12406  308 SGA-VTFATSEDALsHPG----TVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRiagnpdftyhNKPEKRAEIDRGGFIT 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1902 SrfvanpftagqrmyrtGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQL 1980
Cdd:PRK12406  383 S----------------GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVhDCAVFGIPDAEFGEALMA 446
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1981 VAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPH 2035
Cdd:PRK12406  447 VVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPY 501
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1534-2033 3.78e-27

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 118.94  E-value: 3.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARitPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:PRK10946   27 LTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNAL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHP-TERIKFMLQDAKSKLVIGEQKDLAA---------IVHPSIATFAFneLFDETKVDLSSY-----KTTVITPQHP- 1677
Cdd:PRK10946  105 FSHQrSELNAYASQIEPALLIADRQHALFSdddflntlvAEHSSLRVVLL--LNDDGEHSLDDAinhpaEDFTATPSPAd 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 --AYLIYTSGTTGQPKGVMVSHQaivnrilwmQSEYPLSATDTILQKTPCT-----------FDVSVWEFFWSYLVGARL 1744
Cdd:PRK10946  183 evAFFQLSGGSTGTPKLIPRTHN---------DYYYSVRRSVEICGFTPQTrylcalpaahnYPMSSPGALGVFLAGGTV 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1745 VIAPidahrDPLALL--SLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLPICRVfcSGEALPTALAKSFTEHFSC 1822
Cdd:PRK10946  254 VLAP-----DPSATLcfPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQV--GGARLSETLARRIPAELGC 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1823 ELHNLYGPTEAAVDVSYMDATlglhPEESCVAIGYPVW-NTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTA 1901
Cdd:PRK10946  327 QLQQVFGMAEGLVNYTRLDDS----DERIFTTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNA 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1902 SRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLisgLDVVVHA--ISSEQNKANVQ 1979
Cdd:PRK10946  403 SAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLR---HPAVIHAalVSMEDELMGEK 473
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1980 LVAYLQTTAPVDIDQLKKQLAKHLPA-YMVPTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK10946  474 SCAFLVVKEPLKAVQLRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQLRQ 528
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
1546-1956 4.39e-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: 118.11  E-value: 4.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSD--ENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID-LQHPTERIK 1622
Cdd:cd05904    19 PSRPALIDaaTGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANpLSTPAEIAK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1623 FMlQDAKSKLVIG--------EQKDLAAIVHPSIATFAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVM 1694
Cdd:cd05904    99 QV-KDSGAKLAFTtaelaeklASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVM 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQ------AIVNRILWMQSEYPlsatDTILQKTPctfdvsvweFFWSY----------LVGARLVIAPidaHRDPLAL 1758
Cdd:cd05904   178 LTHRnliamvAQFVAGEGSNSDSE----DVFLCVLP---------MFHIYglssfalgllRLGATVVVMP---RFDLEEL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1759 LSLIQKYQVTTLHFVPSMLAVFENAAteILSSAQRQSLPicRVFCSGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDV 1837
Cdd:cd05904   242 LAAIERYKVTHLPVVPPIVLALVKSP--IVDKYDLSSLR--QIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1838 SYMDAtlglhPEESCV---AIGYPVWNTQLYILD-QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVanpftaGQ 1913
Cdd:cd05904   318 AMCFA-----PEKDRAkygSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID------KE 386
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 490930577 1914 RMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL 1956
Cdd:cd05904   387 GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALL 429
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
1513-2031 7.86e-27

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 117.94  E-value: 7.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1513 AEEHDLI-QKTNQTQYYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPR 1591
Cdd:PRK06155    1 GEPLGAGlAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1592 SVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHPSIATFAFNELF-----DETKVDLSs 1666
Cdd:PRK06155   81 RIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWlldapASVSVPAG- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1667 YKTT------------VITPQHPAYLIYTSGTTGQPKGVMVSHQaivnRILW----MQSEYPLSATDTILQKTPCTFDVS 1730
Cdd:PRK06155  160 WSTAplppldapapaaAVQPGDTAAILYTSGTTGPSKGVCCPHA----QFYWwgrnSAEDLEIGADDVLYTTLPLFHTNA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1731 VWEFFWSYLVGARLVIAP-IDAHRDPLALlsliQKYQVTTLHFVPSMLAVFENAATEILSSAQRqslpiCRVFCSGeALP 1809
Cdd:PRK06155  236 LNAFFQALLAGATYVLEPrFSASGFWPAV----RRHGATVTYLLGAMVSILLSQPARESDRAHR-----VRVALGP-GVP 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1810 TALAKSFTEHFSCELHNLYGPTEAAVDVSymdatlGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAG--- 1886
Cdd:PRK06155  306 AALHAAFRERFGVDLLDGYGSTETNFVIA------VTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdep 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1887 HQLAMGYLHRADLTASrfvanpftAGQRM-YRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDV 1964
Cdd:PRK06155  380 FAFATGYFGMPEKTVE--------AWRNLwFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAvAAA 451
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 1965 VVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06155  452 AVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
503-983 1.56e-26

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: 115.56  E-value: 1.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLdldYPIDRmqmmceDANPLFVLTTq 582
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFR------EHELAFILRR- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  583 ALAQQLPqniqqlhldqegvqtqirkqdasdIPAENRKFDFQ----DVAYVIFTSGSTGRPKGVMNTHGSLLNLILshkp 658
Cdd:cd05903    72 AKAKVFV------------------------VPERFRQFDPAampdAVALLLFTSGTTGEPKGVMHSHNTLSASIR---- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  659 tiywPVLEAVNERFPDRPLRAAH-THSFSFDSSWLQVfwMLWGQELHIFDenmRRDAFGLVQEIQQRQIDTLDLPPSFCA 737
Cdd:cd05903   124 ----QYAERLGLGPGDVFLVASPmAHQTGFVYGFTLP--LLLGAPVVLQD---IWDPDKALALMREHGVTFMMGATPFLT 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  738 QMMTNGLFVeNQHHPSL--ILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARPVI--GNPIGNTQA 813
Cdd:cd05903   195 DLLNAVEEA-GEPLSRLrtFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYtdGRPLPGVEI 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  814 YVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAArfvanpfEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIR- 892
Cdd:cd05903   274 KVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-------AAPEGWFRTGDLARLDEDGYLRITGRSKDII-IRg 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  893 GYRVEIGEVENALSILTNVESAVVIAEPINN-SHRLLGYCVVKD---IELDEKTseqlsqQYLSqlRQNLPEYMVPSALT 968
Cdd:cd05903   346 GENIPVLEVEDLLLGHPGVIEAAVVALPDERlGERACAVVVTKSgalLTFDELV------AYLD--RQGVAKQYWPERLV 417
                         490
                  ....*....|....*
gi 490930577  969 VMSEFPRNVSGKVDK 983
Cdd:cd05903   418 HVDDLPRTPSGKVQK 432
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
471-986 1.70e-26

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 116.44  E-value: 1.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  471 QYNNVLDIFYEQVKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNS 550
Cdd:PRK06187    4 YPLTIGRILRHGARKHPDKEAVYFDGRR----TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  551 GASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQNIQQLHL--------DQEGVQTQIRKQDASD-IPAENRKF 621
Cdd:PRK06187   80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTvrtvivegDGPAAPLAPEVGEYEElLAAASDTF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  622 DFQDV----AYVIF-TSGSTGRPKGVMNTHGSLLNLILShkpTIYWPVLEAvNERF-PDRPLraAHTHSfsfdSSWLQVF 695
Cdd:PRK06187  160 DFPDIdendAAAMLyTSGTTGHPKGVVLSHRNLFLHSLA---VCAWLKLSR-DDVYlVIVPM--FHVHA----WGLPYLA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  696 WMLwGQELHIfdenMRR-DAFGLVQEIQQRQIDTldlppSFCA----QMMTNGLFVENQHHPSL--ILIGGEAAPLALwq 768
Cdd:PRK06187  230 LMA-GAKQVI----PRRfDPENLLDLIETERVTF-----FFAVptiwQMLLKAPRAYFVDFSSLrlVIYGGAALPPAL-- 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  769 qLNAQPALFAHNL---YGPTE----YTVDTFRAELK-QTARPV-IGNPIGNTQAYVLDRHLQRCP--TGVIGELYISGFG 837
Cdd:PRK06187  298 -LREFKEKFGIDLvqgYGMTEtspvVSVLPPEDQLPgQWTKRRsAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPW 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  838 IANGYLGRADLSAARFVanpfeHGqrMYRTGDLvrwnsaGKLEFMG------RCDDQIKIRG---YRVeigEVENALSIL 908
Cdd:PRK06187  377 LMQGYWNRPEATAETID-----GG--WLHTGDV------GYIDEDGylyitdRIKDVIISGGeniYPR---ELEDALYGH 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  909 TNVESAVVIAEPINNS-HRLLGYCVVKD-IELDEKtseqlsqQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK06187  441 PAVAEVAVIGVPDEKWgERPVAVVVLKPgATLDAK-------ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
481-986 3.30e-26

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 115.39  E-value: 3.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  481 EQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLD 560
Cdd:PRK07656   13 RAARRFGDKEAYVFGD----QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  561 YPIDRMQMMCE--DANPLFVLTT-QALAQQLPQNIQQLHL-----DQEGVQTQIRKQDASDI--PAENRKF----DFQDV 626
Cdd:PRK07656   89 YTADEAAYILArgDAKALFVLGLfLGVDYSATTRLPALEHvviceTEEDDPHTEKMKTFTDFlaAGDPAERapevDPDDV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  627 AYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiyWPVLEAVNERfpDRPLrAAHT--HSFSFDSSWLQ----------- 693
Cdd:PRK07656  169 ADILFTSGTTGRPKGAMLTHRQLLSNAAD------WAEYLGLTEG--DRYL-AANPffHVFGYKAGVNAplmrgatilpl 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  694 -VFwmlwgqelhifdenmrrDAFGLVQEIQQRQIDTLDLPPSfcaqmMTNGLF------VENQHHPSLILIGGEAAPLAL 766
Cdd:PRK07656  240 pVF-----------------DPDEVFRLIETERITVLPGPPT-----MYNSLLqhpdrsAEDLSSLRLAVTGAASMPVAL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  767 WQ----QLNAQPALFAhnlYGPTEYT-VDTF-RAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIA 839
Cdd:PRK07656  298 LErfesELGVDIVLTG---YGLSEASgVTTFnRLDDDRKTVAgTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVM 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  840 NGYLGRADLSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAE 919
Cdd:PRK07656  375 KGYYDDPEATAAAIDADGWLH------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGV 448
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577  920 PinnsHRLLG-----YCVVKD-IELDEktseqlsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK07656  449 P----DERLGevgkaYVVLKPgAELTE-------EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
PRK07638 PRK07638
acyl-CoA synthetase; Validated
1542-2033 4.27e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 114.88  E-value: 4.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLqRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:PRK07638   11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGEQKDLAAIVHPSIATFafneLFDETKVDLSSYKTT---VITPQH-PAYLIYTSGTTGQPKGVMVSH 1697
Cdd:PRK07638   90 KERLAISNADMIVTERYKLNDLPDEEGRVI----EIDEWKRMIEKYLPTyapIENVQNaPFYMGFTSGSTGKPKAFLRAQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1698 QAivnrilWMQS------EYPLSATDTILqkTPCTFDVSVWEF--FWSYLVGARLVIAPidaHRDPLALLSLIQKYQVTT 1769
Cdd:PRK07638  166 QS------WLHSfdcnvhDFHMKREDSVL--IAGTLVHSLFLYgaISTLYVGQTVHLMR---KFIPNQVLDKLETENISV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1770 LHFVPSMlavfenaaTEILSSAQRQSLPICRVFCSGEALPTALAKSFTEHF-SCELHNLYGPTEAAVdVSYmdatlgLHP 1848
Cdd:PRK07638  235 MYTVPTM--------LESLYKENRVIENKMKIISSGAKWEAEAKEKIKNIFpYAKLYEFYGASELSF-VTA------LVD 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1849 EESCV---AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTagqrmyrTGDIARWH 1925
Cdd:PRK07638  300 EESERrpnSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMT-------VRDVGYED 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1926 ADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYLQTTApvDIDQLKKQLAKHLPA 2005
Cdd:PRK07638  373 EEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIV-VIGVPDSYWGEKPVAIIKGSA--TKQQLKSFCLQRLSS 449
                         490       500
                  ....*....|....*....|....*...
gi 490930577 2006 YMVPTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK07638  450 FKIPKEWHFVDEIPYTNSGKIARMEAKS 477
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1526-2033 4.70e-26

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 115.62  E-value: 4.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1526 QYYVRQSTLQQLLREQARITPEQTALSDeNHQLSFSEVRLQVCA--LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVI 1603
Cdd:PRK06087   17 QGYWGDASLADYWQQTARAMPDKIAVVD-NHGASYTYSALDHAAsrLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1604 EAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG----EQKDLAAIVHP---SIATFAFNELFDETKVDLSSYKTTVI---- 1672
Cdd:PRK06087   96 KVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfKQTRPVDLILPlqnQLPQLQQIVGVDKLAPATSSLSLSQIiady 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1673 TP-QHP--------AYLIYTSGTTGQPKGVMVSHqaivNRILWMQSEYP----LSATDTILQKTPCTFDVSvweFFWS-- 1737
Cdd:PRK06087  176 EPlTTAitthgdelAAVLFTSGTEGLPKGVMLTH----NNILASERAYCarlnLTWQDVFMMPAPLGHATG---FLHGvt 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1738 --YLVGARLVIapiDAHRDPLALLSLIQKYQVTTLH----FVPSMLAVFENAATEilssaqrqsLPICRVF-CSGEALPT 1810
Cdd:PRK06087  249 apFLIGARSVL---LDIFTPDACLALLEQQRCTCMLgatpFIYDLLNLLEKQPAD---------LSALRFFlCGGTTIPK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1811 ALAKSFTEHfSCELHNLYGPTEAAVDVsymdatlgLHPEESCVAI-----GYPVWNTQLYILDQYLRPVPVGVDGELYLA 1885
Cdd:PRK06087  317 KVARECQQR-GIKLLSVYGSTESSPHA--------VVNLDDPLSRfmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASR 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1886 GHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDqLKIR-GQRIELGEIEQQLRLISGL-D 1963
Cdd:PRK06087  388 GPNVFMGYLDEPELTARALDEEGW------YYSGDLCRMDEAGYIKITGRKKD-IIVRgGENISSREVEDILLQHPKIhD 460
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490930577 1964 VVVHAISSEqnKANVQLVAYLQTTAPVDIDQLKKQLA----KHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK06087  461 ACVVAMPDE--RLGERSCAYVVLKAPHHSLTLEEVVAffsrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
504-986 9.49e-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: 112.91  E-value: 9.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  504 SFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLdldypidrmqmmcedaNPLFvlTTQA 583
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL----------------FALF--GPEA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  584 LAQQLPQNiqqlhldqegvQTQIRKQDASDipaenrkfdfqDVAYVIFTSGSTGRPKGVMNTHgsllNLILSHKPTIYWP 663
Cdd:cd05971    70 LEYRLSNS-----------GASALVTDGSD-----------DPALIIYTSGTTGPPKGALHAH----RVLLGHLPGVQFP 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  664 vleavNERFPdRPLRAAHTHSfsfDSSW----LQVF--WMLWGqeLHIFDENMRR-DAFGLVQEIQQRQIDTLDLPPSFC 736
Cdd:cd05971   124 -----FNLFP-RDGDLYWTPA---DWAWigglLDVLlpSLYFG--VPVLAHRMTKfDPKAALDLMSRYGVTTAFLPPTAL 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  737 AQMMTNGlfvENQHHPSL----ILIGGEA--APLALW--QQLNAQpalfAHNLYGPTEYTVDTFRAELKQTARP-VIGNP 807
Cdd:cd05971   193 KMMRQQG---EQLKHAQVklraIATGGESlgEELLGWarEQFGVE----VNEFYGQTECNLVIGNCSALFPIKPgSMGKP 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  808 IGNTQAYVLDRHLQRCPTGVIGELYISgFGIANGYLG--RADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRC 885
Cdd:cd05971   266 IPGHRVAIVDDNGTPLPPGEVGEIAVE-LPDPVAFLGywNNPSATEKKMAGDW------LLTGDLGRKDSDGYFWYVGRD 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  886 DDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVkdIELDEKTSEQLSQQYLSQLRQNLPEYMVPS 965
Cdd:cd05971   339 DDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVV--LNPGETPSDALAREIQELVKTRLAAHEYPR 416
                         490       500
                  ....*....|....*....|.
gi 490930577  966 ALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05971   417 EIEFVNELPRTATGKIRRREL 437
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
1102-1435 1.46e-25

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: 112.09  E-value: 1.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1102 PLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQL--------GGHFDSELA---EEPVFIY 1169
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPaYNIPGAWRLTGPLDVEALREALRDVVARHEALrtllvrddGGVPRQEILppgPAPLEVR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1170 SLHPTQAWPVQfcsvtpdLLEQTIQEALQQPIHLDQPYgLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDfIKAY 1249
Cdd:cd19539    83 DLSDPDSDRER-------RLEELLRERESRGFDLDEEP-PIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARD-LAAL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1250 QQTNQQ-----LPVLEHSYETVikALSGRDHETSKVI------WQRDLADLQPLILFNQAQQAVQ------ETSYRLSAE 1312
Cdd:cd19539   154 YAARRKgpaapLPELRQQYKEY--AAWQREALAAPRAaelldfWRRRLRGAEPTALPTDRPRPAGfpypgaDLRFELDAE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1313 LGAKLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQL 1392
Cdd:cd19539   232 LVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLI 309
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 490930577 1393 PQLQQLHVEHLEHDGLGLSAIQQLIAQGN------LFDSLLVVENYPDN 1435
Cdd:cd19539   310 ARVRKALVDAQRHQELPFQQLVAELPVDRdagrhpLVQIVFQVTNAPAG 358
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
1517-2031 1.76e-25

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: 114.51  E-value: 1.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1517 DLIQKTNQTQYYV--RQSTLQQLLREQARITPEQTALSDENHQ-----LSFSEVRLQVCALAQQLQRAGVQAGDIVAVAL 1589
Cdd:cd05968    44 DLSGGKPWAAWFVggRMNIVEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1590 PRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVI--------GEQKDLAAIVHPSIATFAFNE------ 1655
Cdd:cd05968   124 PMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALItadgftrrGREVNLKEEADKACAQCPTVEkvvvvr 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1656 ----LFDETKVDLSSYKTTVITP---------QHPAYLIYTSGTTGQPKGVMVSHQAI-VNRILWMQSEYPLSATDTILQ 1721
Cdd:cd05968   204 hlgnDFTPAKGRDLSYDEEKETAgdgaertesEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTW 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1722 KTPCTFDVSVWEFFWSYLVGARLVI---APidAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLpi 1798
Cdd:cd05968   284 FTDLGWMMGPWLIFGGLILGATMVLydgAP--DHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSL-- 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1799 cRVFCS-GEALPTALAKSFTEHF---SCELHNLYGPTEAAvdvsymDATLGLHPEESCVAIGY--PVWNTQLYILDQYLR 1872
Cdd:cd05968   360 -RVLGStGEPWNPEPWNWLFETVgkgRNPIINYSGGTEIS------GGILGNVLIKPIKPSSFngPVPGMKADVLDESGK 432
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1873 PVPVGVdGELYLAGHQLAM--GYLHRADltasRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELG 1950
Cdd:cd05968   433 PARPEV-GELVLLAPWPGMtrGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPA 507
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1951 EIEQQL----RLISGLDV-VVHAISSEqnkANVQLVAYLQTTAPVDI--DQLKKQLAKHLPAYMVPTHYMLVEQFPLSHN 2023
Cdd:cd05968   508 EIESVLnahpAVLESAAIgVPHPVKGE---AIVCFVVLKPGVTPTEAlaEELMERVADELGKPLSPERILFVKDLPKTRN 584

                  ....*...
gi 490930577 2024 GKLDRKAL 2031
Cdd:cd05968   585 AKVMRRVI 592
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
562-987 2.00e-25

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: 111.61  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  562 PIDRMQMMCeDANPLFVLTTQAL----AQQLPQNIqqlHLDQEGVQTQIRKQDAsdipaenrKFDFQDVAYVIFTSGSTG 637
Cdd:cd05934    27 PGDRVALML-DNCPEFLFAWFALaklgAVLVPINT---ALRGDELAYIIDHSGA--------QLVVVDPASILYTSGTTG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  638 RPKGVMNTHGSLLNlilshkptiyWPVLEAvnERFPDRPLRAAHT-----HSFSFDSSWLQVFWMlwGQELHIFDENMRR 712
Cdd:cd05934    95 PPKGVVITHANLTF----------AGYYSA--RRFGLGEDDVYLTvlplfHINAQAVSVLAALSV--GATLVLLPRFSAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  713 DAFGLVQEIQQRQIDTLDLPPSF-CAQMMTnglfVENQHHPsLILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVDT 791
Cdd:cd05934   161 RFWSDVRRYGATVTNYLGAMLSYlLAQPPS----PDDRAHR-LRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  792 FRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYI---SGFGIANGYLGRADLSAARFvanpfEHGqrMYRTG 868
Cdd:cd05934   236 IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-----RNG--WFHTG 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  869 DLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIELDEktSEQLSQ 948
Cdd:cd05934   309 DLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVP----DEVGEDEVKAVVVLRP--GETLDP 382
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 490930577  949 QYLSQ-LRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd05934   383 EELFAfCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
482-986 3.51e-25

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 111.98  E-value: 3.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  482 QVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDY 561
Cdd:PRK03640   11 RAFLTPDRTAIEFEE----KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  562 PIDRMQMMCEDANPLFVLTTQALAQQLPQNIQQLHldqegvqTQIRKQDASDIPAENrKFDFQDVAYVIFTSGSTGRPKG 641
Cdd:PRK03640   87 SREELLWQLDDAEVKCLITDDDFEAKLIPGISVKF-------AELMNGPKEEAEIQE-EFDLDEVATIMYTSGTTGKPKG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  642 VMNT---H-----GSLLNLILSHKPTiyWpvLEAVnerfpdrPLraAHTHSFS--FDSswlqvfwMLWGQELHIFDenmR 711
Cdd:PRK03640  159 VIQTygnHwwsavGSALNLGLTEDDC--W--LAAV-------PI--FHISGLSilMRS-------VIYGMRVVLVE---K 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  712 RDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNglFVENQHHPSL--ILIGGEAAPLALWQQlnAQpalfAHNL-----YGP 784
Cdd:PRK03640  216 FDAEKINKLLQTGGVTIISVVSTMLQRLLER--LGEGTYPSSFrcMLLGGGPAPKPLLEQ--CK----EKGIpvyqsYGM 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  785 TEYT--VDTFRAELKQTARPVIGNPIGNTQAYVLDrHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgq 862
Cdd:PRK03640  288 TETAsqIVTLSPEDALTKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF---- 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  863 rmyRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEkt 942
Cdd:PRK03640  363 ---KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTE-- 437
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 490930577  943 sEQLSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK03640  438 -EELRH----FCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
1546-2032 7.17e-25

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 111.63  E-value: 7.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTE------ 1619
Cdd:PRK13383   49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDalaaal 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1620 ---RIKFMLQDAKSKLVIGEQKDLAAIVHPSIATfafnelfdetkVDLSSYKTTVITPQHPAYLiyTSGTTGQPKGVMVS 1696
Cdd:PRK13383  129 rahHISTVVADNEFAERIAGADDAVAVIDPATAG-----------AEESGGRPAVAAPGRIVLL--TSGTTGKPKGVPRA 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1697 HQAIVNRILWMQ--SEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIapiDAHRDPLALLSLIQKYQVTTLHFVP 1774
Cdd:PRK13383  196 PQLRSAVGVWVTilDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLT---HRHFDAEAALAQASLHRADAFTAVP 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1775 SMLAVFENAATEILSsaqRQSLPICRV-FCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEescv 1853
Cdd:PRK13383  273 VVLARILELPPRVRA---RNPLPQLRVvMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRDAPE---- 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1854 AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYlhrADLTASRFVANpftagqrMYRTGDIARWHADGSIQYI 1933
Cdd:PRK13383  346 TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVVDG-------MTSTGDMGYLDNAGRLFIV 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1934 GRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHY 2012
Cdd:PRK13383  416 GREDDMIISGGENVYPRAVENALAAHPAVaDNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDI 495
                         490       500
                  ....*....|....*....|
gi 490930577 2013 MLVEQFPLSHNGKLDRKALP 2032
Cdd:PRK13383  496 NIVSSIPRNPTGKVLRKELP 515
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
601-986 8.99e-25

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: 109.86  E-value: 8.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  601 GVQTQIRKQDASDIPAENRK----FDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiyWPVlEAVNERFPDRP 676
Cdd:cd05919    64 VINPLLHPDDYAYIARDCEArlvvTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADA------MAR-EALGLTPGDRV 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  677 LRAAHTHsFSFDSSWLQVFWMLWGQELHIFDEnmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFveNQHHPSLIL 756
Cdd:cd05919   137 FSSAKMF-FGYGLGNSLWFPLAVGASAVLNPG--WPTAERVLATLARFRPTVLYGVPTFYANLLDSCAG--SPDALRSLR 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  757 I---GGEAAPLALWQQLNAQPALFAHNLYGPTEyTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELY 832
Cdd:cd05919   212 LcvsAGEALPRGLGERWMEHFGGPILDGIGATE-VGHIFLSNRPGAWRLgSTGRPVPGYEIRLVDEEGHTIPPGEEGDLL 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  833 ISGFGIANGYLGRADLSAARFVANpfehgqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVE 912
Cdd:cd05919   291 VRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVA 363
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577  913 SAVVIAEPinNSHRLL---GYCVVKDiELDekTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05919   364 EAAVVAVP--ESTGLSrltAFVVLKS-PAA--PQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
1558-2033 1.46e-24

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: 108.97  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLvigeq 1637
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 kdlaaivhPSIATfafnelfdetkvdlssykttvitpqhpayLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATD 1717
Cdd:cd05912    77 --------DDIAT-----------------------------IMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDD 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 TILQKTPcTFDVSvwefFWSYLVgaRLVI--APIDAHR--DPLALLSLIQKYQVTTLHFVPSMLavfeNAATEILSSAQR 1793
Cdd:cd05912   120 NWLCALP-LFHIS----GLSILM--RSVIygMTVYLVDkfDAEQVLHLINSGKVTIISVVPTML----QRLLEILGEGYP 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1794 QSLPiCRVFCSGEALPTALAKsftehfsCELHNL-----YGPTEAAVDVsymdatLGLHPEESCVAI---GYPVWNTQLY 1865
Cdd:cd05912   189 NNLR-CILLGGGPAPKPLLEQ-------CKEKGIpvyqsYGMTETCSQI------VTLSPEDALNKIgsaGKPLFPVELK 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1866 ILDQYLRPvpvGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQ 1945
Cdd:cd05912   255 IEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGE 324
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1946 RIELGEIEQQLRLISGL-DVVVHAISSEqnKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNG 2024
Cdd:cd05912   325 NIYPAEIEEVLLSHPAIkEAGVVGIPDD--KWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASG 402

                  ....*....
gi 490930577 2025 KLDRKALPQ 2033
Cdd:cd05912   403 KLLRHELKQ 411
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
1101-1380 1.48e-24

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: 109.28  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQS-NYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElAEEPV-FIysLHPTQAWP 1178
Cdd:cd19538     2 IPLSFAQRRLWFLHQLEGPSaTYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEE-DGVPYqLI--LEEDEATP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1179 V-QFCSVTPDLLEQTIQEALQQPIHLDQPYGlIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ--TNQQ 1255
Cdd:cd19538    79 KlEIKEVDEEELESEINEAVRYPFDLSEEPP-FRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRArcKGEA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1256 -----LPVLEHSYETVIKALSGRDHETSKVI------WQRDLA---DLQPLILFNQAQQAVQETSYRLSAELGAKLQHKL 1321
Cdd:cd19538   158 pelapLPVQYADYALWQQELLGDESDPDSLIarqlayWKKQLAglpDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQL 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1322 ----RQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSApiNGLEQQIGLFLNTIPVRV 1380
Cdd:cd19538   238 lqlaKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRND--DSLEDLVGFFVNTLVLRT 298
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
465-986 1.90e-24

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: 110.28  E-value: 1.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  465 RVSHPEQYNNVLDIFYEQVKKYPERTAIV----SGERpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDS 540
Cdd:cd05970     9 SINVPENFNFAYDVVDAMAKEYPDKLALVwcddAGEE---RIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  541 VVVMLSVLNSGASFLPL-------DLDYPIDRMQM---MCEDANPLFVLTTQALAQ--QLPQNIQQLHLDQEGvQTQIRK 608
Cdd:cd05970    86 WYSLLALHKLGAIAIPAthqltakDIVYRIESADIkmiVAIAEDNIPEEIEKAAPEcpSKPKLVWVGDPVPEG-WIDFRK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  609 --QDASDI---PAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKptiYWPvleavNERFPDRPLRAAhth 683
Cdd:cd05970   165 liKNASPDferPTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAK---YWQ-----NVREGGLHLTVA--- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  684 sfsfDSSWLQVFW-MLWGQEL---HIFDENMRR-DAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIG 758
Cdd:cd05970   234 ----DTGWGKAVWgKIYGQWIagaAVFVYDYDKfDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  759 GEAAPLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYIS---- 834
Cdd:cd05970   310 GEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskg 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  835 -GFGIANGYLGRADLSAarfvaNPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-E 912
Cdd:cd05970   390 kPVGLFGGYYKDAEKTA-----EVWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVlE 462
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577  913 SAVV-IAEPINnshrllGYCVVKDIEL--DEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05970   463 CAVTgVPDPIR------GQVVKATIVLakGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
PRK07529 PRK07529
AMP-binding domain protein; Validated
1532-2031 2.14e-24

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 111.20  E-value: 2.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARITPEQTALS--------DENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVI 1603
Cdd:PRK07529   25 ASTYELLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1604 EAGAAYlPID-LQHPtERIKFMLQDAKSKLVI------------------GEQKDLAAIV-------------------- 1644
Cdd:PRK07529  105 AAGIAN-PINpLLEP-EQIAELLRAAGAKVLVtlgpfpgtdiwqkvaevlAALPELRTVVevdlarylpgpkrlavplir 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1645 -HPSIATFAFNELFDETKVDLSSYkTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKT 1723
Cdd:PRK07529  183 rKAHARILDFDAELARQPGDRLFS-GRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGL 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1724 PcTFDVsvwefFWSYLV-------GARLVIAPIDAHRDPLA---LLSLIQKYQVTTLHFVPSMLAVFenaateilssAQR 1793
Cdd:PRK07529  262 P-LFHV-----NALLVTglaplarGAHVVLATPQGYRGPGVianFWKIVERYRINFLSGVPTVYAAL----------LQV 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1794 -------QSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTEA--AVDVSYMDATLGLHpeescvAIGYPVWNTQL 1864
Cdd:PRK07529  326 pvdghdiSSLRY--ALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEAtcVSSVNPPDGERRIG------SVGLRLPYQRV 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YIL-----DQYLRPVPVGVDGELYLAGHQLAMGYLhRADLTASRFVanpftaGQRMYRTGDIARWHADGSIQYIGRADDq 1939
Cdd:PRK07529  398 RVVilddaGRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL------EDGWLNTGDLGRIDADGYFWLTGRAKD- 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1940 LKIR-GQRIELGEIEQQLrliSGLDVVVH--AISSEQNKANVQLVAYLQTT--APVDIDQLKKQLAKHLP---AymVPTH 2011
Cdd:PRK07529  470 LIIRgGHNIDPAAIEEAL---LRHPAVALaaAVGRPDAHAGELPVAYVQLKpgASATEAELLAFARDHIAeraA--VPKH 544
                         570       580
                  ....*....|....*....|
gi 490930577 2012 YMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK07529  545 VRILDALPKTAVGKIFKPAL 564
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
1680-2031 3.17e-24

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: 108.33  E-value: 3.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVMVSHQ---AIVNRilWMQSEYPLSATDTILQKTPCTFDVS---VWEFFWSylVGARLVIAPidaHR 1753
Cdd:cd05958   102 LAFTSGTTGAPKATMHFHRdplASADR--YAVNVLRLREDDRFVGSPPLAFTFGlggVLLFPFG--VGASGVLLE---EA 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1754 DPLALLSLIQKYQVTTLHFVPSMLAvfenAATEILSSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEA 1833
Cdd:cd05958   175 TPDLLLSAIARYKPTVLFTAPTAYR----AMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEM 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1834 avdvsymdatlgLH------PEESCV-AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGhqlAMGYLHRADLTASRFVA 1906
Cdd:cd05958   251 ------------FHifisarPGDARPgATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQ 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1907 NPFTAgqrmyrTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQlrLISGLDVVVHAISSEQNKANVQLV-AYL- 1984
Cdd:cd05958   316 GGWNI------TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDV--LLQHPAVAECAVVGHPDESRGVVVkAFVv 387
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1985 ----QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05958   388 lrpgVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
1559-2031 5.70e-24

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: 108.71  E-value: 5.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1559 SFSEVRLQVCALAQQLQRA-GVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:cd05928    43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 kDLAAIVH------PSIAT------------FAFNELFDETKVDLSSYKTTvitPQHPAYLIYTSGTTGQPKgvMVSHQ- 1698
Cdd:cd05928   123 -ELAPEVDsvasecPSLKTkllvseksrdgwLNFKELLNEASTEHHCVETG---SQEPMAIYFTSGTTGSPK--MAEHSh 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1699 ------AIVNRILWMQseypLSATDTILqktpCTFDVSVWEFFWSYLVGARLVIAPIDAHR----DPLALLSLIQKYQVT 1768
Cdd:cd05928   197 sslglgLKVNGRYWLD----LTASDIMW----NTSDTGWIKSAWSSLFEPWIQGACVFVHHlprfDPLVILKTLSSYPIT 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1769 TLHFVPSmlaVFENAATEILSSAQRQSLPICrvFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVdvsyMDATL-GLH 1847
Cdd:cd05928   269 TFCGAPT---VYRMLVQQDLSSYKFPSLQHC--VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGL----ICANFkGMK 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1848 PEESCVAIGYPVWNTQlyILDQYLRPVPVGVDGELYL-----AGHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIA 1922
Cdd:cd05928   340 IKPGSMGKASPPYDVQ--IIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGD-------FYLTGDRG 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1923 RWHADGSIQYIGRADDQLKIRGQRIELGEIEQQlrLISGLDVVVHAISS-------EQNKANVQLVAYLQTTAPvdiDQL 1995
Cdd:cd05928   411 IMDEDGYFWFMGRADDVINSSGYRIGPFEVESA--LIEHPAVVESAVVSspdpirgEVVKAFVVLAPQFLSHDP---EQL 485
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 490930577 1996 KKQLAKHLPAYMVPTHY----MLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05928   486 TKELQQHVKSVTAPYKYprkvEFVQELPKTVTGKIQRNEL 525
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1679-2027 6.91e-24

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: 105.93  E-value: 6.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1679 YLIYTSGTTGQPKGVMVSHQAIVnRILW----MQSEYPLSATDTILQKT-----------PCTFDVSVWEFFWSYLVGAR 1743
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEDIF-RMLMggadFGTGEFTPSEDAHKAAAaaagtvmfpapPLMHGTGSWTAFGGLLGGQT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1744 LVIapIDAHRDPLALLSLIQKYQVTTLHFVPSMLAvfeNAATEILSSAQRQSLPICRVFCSGEALPTALAKS-FTEHF-S 1821
Cdd:cd05924    86 VVL--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMA---RPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQgLLELVpN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1822 CELHNLYGPTEAAVDVSYMDATLGlHPEESCVAIgypvwNTQLYILDQYLRPVPVGVDGELYLA--GHqLAMGYLHRADL 1899
Cdd:cd05924   161 ITLVDAFGSSETGFTGSGHSAGSG-PETGPFTRA-----NPDTVVLDDDGRVVPPGSGGVGWIArrGH-IPLGYYGDEAK 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1900 TASRFvanPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANV 1978
Cdd:cd05924   234 TAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVyDVLVVGRPDERWGQEV 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 490930577 1979 QLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:cd05924   311 VAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
474-981 9.16e-24

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: 108.82  E-value: 9.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  474 NVLDifyEQVKKYPERTAIV--SGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSG 551
Cdd:cd17634    57 NALD---RHLRENGDRTAIIyeGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  552 ASFLPLDLDYPIDRMQMMCEDANPLFVLTT-----------------QALAQQLPQNIQQLHLDQEGV------------ 602
Cdd:cd17634   134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITAdggvragrsvplkknvdDALNPNVTSVEHVIVLKRTGSdidwqegrdlww 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  603 QTQIRKQDASDIPAenrKFDFQDVAYVIFTSGSTGRPKGVMNTHG--------SLLNLILSHKPTIYWpvleavneRFPD 674
Cdd:cd17634   214 RDLIAKASPEHQPE---AMNAEDPLFILYTSGTTGKPKGVLHTTGgylvyaatTMKYVFDYGPGDIYW--------CTAD 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  675 RPLRAAHthsfsfdsSWLQVFWMLWGQELHIFD-ENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGL-FVENQHHP 752
Cdd:cd17634   283 VGWVTGH--------SYLLYGPLACGATTLLYEgVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDdAIEGTDRS 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  753 SLILIGGEAAPLA------LWQQLNAQ--PALfahNLYGPTEY-----TVDTFRAELKQ--TARPVIGnpignTQAYVLD 817
Cdd:cd17634   355 SLRILGSVGEPINpeayewYWKKIGKEkcPVV---DTWWQTETggfmiTPLPGAIELKAgsATRPVFG-----VQPAVVD 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  818 RHLQRCPTGVIGELYISGF--GIANGYLGRADlsaaRFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYR 895
Cdd:cd17634   427 NEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHR 502
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  896 VEIGEVENALSILTNV-ESAVV-IAEPINNShRLLGYCVVKDIELDektSEQLSQQYLSQLRQNLPEYMVPSALTVMSEF 973
Cdd:cd17634   503 LGTAEIESVLVAHPKVaEAAVVgIPHAIKGQ-APYAYVVLNHGVEP---SPELYAELRNWVRKEIGPLATPDVVHWVDSL 578

                  ....*...
gi 490930577  974 PRNVSGKV 981
Cdd:cd17634   579 PKTRSGKI 586
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
1676-2028 2.08e-23

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: 103.64  E-value: 2.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1676 HPAYLIYTSGTTGQPKGVMVSHQAivnrilWMQS------EYPLSATDTILQKTPCTFDVSVWEFFWSYLVGaRLVIapI 1749
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERS------WIESfvcnedLFNISGEDAILAPGPLSHSLFLYGAISALYLG-GTFI--G 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1750 DAHRDPLALLSLIQKYQVTTLHFVPSMLavfenaatEILSSAQRQSLPICRVFCSGEALPTALAKSFTEHF-SCELHNLY 1828
Cdd:cd17633    72 QRKFNPKSWIRKINQYNATVIYLVPTML--------QALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFY 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1829 GPTEAAVdVSYmdatlgLHPEESCVA--IGYPVWNTQLYILDQylrpvPVGVDGELYLAGHQLAMGYLHRADLTASRFva 1906
Cdd:cd17633   144 GTSELSF-ITY------NFNQESRPPnsVGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNPDGW-- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1907 npftagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD--VVVHAISSEQNKANVQLVAYL 1984
Cdd:cd17633   210 ---------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEeaIVVGIPDARFGEIAVALYSGD 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 490930577 1985 QTTAPvdidQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:cd17633   281 KLTYK----QLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1558-2031 2.16e-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: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 106.06  E-value: 2.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 KDLAaivhpSIATFAFNELFdetkvdlssykttvitpqhpayliyTSGTTGQPKGVMVSHQAIVNRILWMqsEYPLSATD 1717
Cdd:cd05973    81 ANRH-----KLDSDPFVMMF-------------------------TSGTTGLPKGVPVPLRALAAFGAYL--RDAVDLRP 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 tilqktpctfDVSVWEFF---WSY-LVGArlVIAPIdAHRDPLALLS----------LIQKYQVTTLHFVPSMLAVFENA 1783
Cdd:cd05973   129 ----------EDSFWNAAdpgWAYgLYYA--ITGPL-ALGHPTILLEggfsvestwrVIERLGVTNLAGSPTAYRLLMAA 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1784 ATEilsSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSymdatlGLHPEESCV---AIGYPVW 1860
Cdd:cd05973   196 GAE---VPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLA------NHHALEHPVhagSAGRAMP 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1861 NTQLYILDQYLRPVPVGVDGELYLAGHQLAM----GYLHRADLTASrfvanpftagQRMYRTGDIARWHADGSIQYIGRA 1936
Cdd:cd05973   267 GWRVAVLDDDGDELGPGEPGRLAIDIANSPLmwfrGYQLPDTPAID----------GGYYLTGDTVEFDPDGSFSFIGRA 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1937 DDQLKIRGQRIELGEIEQQlrLISGLDVVVHAI-------SSEQNKANVQLVA-YLQTTAPVDIDQL--KKQLAKHlpAY 2006
Cdd:cd05973   337 DDVITMSGYRIGPFDVESA--LIEHPAVAEAAVigvpdpeRTEVVKAFVVLRGgHEGTPALADELQLhvKKRLSAH--AY 412
                         490       500
                  ....*....|....*....|....*
gi 490930577 2007 MVPTHYmlVEQFPLSHNGKLDRKAL 2031
Cdd:cd05973   413 PRTIHF--VDELPKTPSGKIQRFLL 435
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1532-2033 2.43e-23

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 106.89  E-value: 2.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARITPEQTAL--SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:PRK05852   16 PRIADLVEVAATRLPEAPALvvTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKFMLQDAKSKLVI------GEQKDLAAIVHPSIATFAFNELFDETKVDLSSYKTTVITPQHP------ 1677
Cdd:PRK05852   96 VPLDPALPIAEQRVRSQAAGARVVLidadgpHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATStpeglr 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 ---AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAP----ID 1750
Cdd:PRK05852  176 pddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPargrFS 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1751 AHR--DPLALLSLIQKYQVTTLHFVpsmlaVFENAATEiLSSAQRQSLPICRVfCSGeALPTALAKSFTEHFSCELHNLY 1828
Cdd:PRK05852  256 AHTfwDDIKAVGATWYTAVPTIHQI-----LLERAATE-PSGRKPAALRFIRS-CSA-PLTAETAQALQTEFAAPVVCAF 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1829 GPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNT--QLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTAsrfvA 1906
Cdd:PRK05852  328 GMTEATHQVTTTQIEGIGQTENPVVSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITA----A 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1907 NpFTAGqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQ 1985
Cdd:PRK05852  404 N-FTDG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNvMEAAVFGVPDQLYGEAVAAVIVPR 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 490930577 1986 TTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK05852  481 ESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1682-2028 2.62e-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.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 103.90  E-value: 2.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1682 YTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTP---CtFDVSVweffwSYLV----GARLViaPIDAHRD 1754
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPlfhC-FGSVL-----GVLAclthGATMV--FPSPSFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1755 PLALLSLIQKYQVTTLHFVPSMlavFEnaatEILSSAQRQSLPICRV---FCSGEALPTALAKSFTE--HFScELHNLYG 1829
Cdd:cd05917    81 PLAVLEAIEKEKCTALHGVPTM---FI----AELEHPDFDKFDLSSLrtgIMAGAPCPPELMKRVIEvmNMK-DVTIAYG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1830 PTEAAvDVSYMdATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVP-VGVDGELYLAGHQLAMGYLHRADLTASRFvanp 1908
Cdd:cd05917   153 MTETS-PVSTQ-TRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAI---- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1909 ftAGQRMYRTGDIARWHADGSIQYIGRADDQLkIRG-QRIELGEIEQQL-RLISGLDVVVHAISSEqnKANVQLVAY--L 1984
Cdd:cd05917   227 --DGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLhTHPKVSDVQVVGVPDE--RYGEEVCAWirL 301
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 490930577 1985 QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:cd05917   302 KEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
1530-2050 2.80e-23

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 106.79  E-value: 2.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLReQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:PRK07786   16 RQNWVNQLAR-HALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKFMLQDAKSKLVIGEQ--KDLAAIVH---PSIAT------------FAFNELFDETKVDLSSYKttvI 1672
Cdd:PRK07786   95 VPVNFRLTPPEIAFLVSDCGAHVVVTEAalAPVATAVRdivPLLSTvvvaggssddsvLGYEDLLAEAGPAHAPVD---I 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1673 TPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTI-LQKTPCTFDVSVWEFFWSYLVGARLVIAPIDA 1751
Cdd:PRK07786  172 PNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVgFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGA 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1752 HrDPLALLSLIQKYQVTTLHFVPSMLAVFENAATeilssAQRQSLPIcRVFCSGEA-LPTALAKSFTEHF-SCELHNLYG 1829
Cdd:PRK07786  252 F-DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQ-----ARPRDLAL-RVLSWGAApASDTLLRQMAATFpEAQILAAFG 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1830 PTEAAvDVSYM----DA--TLGlhpeescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASR 1903
Cdd:PRK07786  325 QTEMS-PVTCMllgeDAirKLG--------SVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEA 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1904 FVANPFtagqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQlrLISGLDVV-VHAISSEQNK---ANVQ 1979
Cdd:PRK07786  396 FAGGWF-------HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENV--LASHPDIVeVAVIGRADEKwgeVPVA 466
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1980 LVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSAF 2050
Cdd:PRK07786  467 VAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGACVNVERRSASAGF 537
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
625-986 3.27e-23

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: 103.18  E-value: 3.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHgslLNLILShkptiywpvLEAVNERFPDRP-------LRAAHThsfsfdsSWLQVF-- 695
Cdd:cd17630     1 RLATVILTSGSTGTPKAVVHTA---ANLLAS---------AAGLHSRLGFGGgdswllsLPLYHV-------GGLAILvr 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  696 WMLWGQELHIFDENmrrdaFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGEAAPLALWQQLnAQPA 775
Cdd:cd17630    62 SLLAGAELVLLERN-----QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERA-ADRG 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  776 LFAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQAYVLDRhlqrcptgviGELYISGFGIANGYLgradlsAARFVA 855
Cdd:cd17630   136 IPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYL------RGQLVP 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  856 NPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKD 935
Cdd:cd17630   200 EFNEDG--WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVP----DEELGQRPVAV 273
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 490930577  936 IELDEKTSEQLSQQYLSQLrqnLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17630   274 IVGRGPADPAELRAWLKDK---LARFKLPKRIYPVPELPRTGGGKVDRRAL 321
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
503-986 3.96e-23

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: 105.28  E-value: 3.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQ 582
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  583 ALAqqlpqniqqlhldqegvqtqirkqdasdipaenRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILS------- 655
Cdd:cd05969    81 ELY---------------------------------ERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTgkyvldl 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  656 HKPTIYWpvleavnerfpdrplraaHTHsfsfDSSWLQ-VFWMLWGQELH----IFDENmRRDAFGLVQEIQQRQIDTLD 730
Cdd:cd05969   128 HPDDIYW------------------CTA----DPGWVTgTVYGIWAPWLNgvtnVVYEG-RFDAESWYGIIERVKVTVWY 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  731 LPPSFCAQMMTNGLFVENQH---HPSLILIGGEAA-PLALWQQLNAQPALFaHNLYGPTEYTVDTFRAELKQTARP-VIG 805
Cdd:cd05969   185 TAPTAIRMLMKEGDELARKYdlsSLRFIHSVGEPLnPEAIRWGMEVFGVPI-HDTWWQTETGSIMIANYPCMPIKPgSMG 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  806 NPIGNTQAYVLDRHLQRCPTGVIGELYI-SGF-GIANGYLGradlSAARFvANPFEHGqrMYRTGDLVRWNSAGKLEFMG 883
Cdd:cd05969   264 KPLPGVKAAVVDENGNELPPGTKGILALkPGWpSMFRGIWN----DEERY-KNSFIDG--WYLTGDLAYRDEDGYFWFVG 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  884 RCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIELDE--KTSEQLSQQYLSQLRQNLPEY 961
Cdd:cd05969   337 RADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKP----DPLRGEIIKAFISLKEgfEPSDELKEEIINFVRQKLGAH 412
                         490       500
                  ....*....|....*....|....*
gi 490930577  962 MVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05969   413 VAPREIEFVDNLPKTRSGKIMRRVL 437
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
470-986 4.07e-23

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: 105.91  E-value: 4.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  470 EQYNNVLDIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLN 549
Cdd:cd05959     1 EKYNAATLVDLNLNEGRGDKTAFIDDAG----SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  550 SGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQniqQLHLDQEGVQTQIRKQDASDIPAENRKFDF------ 623
Cdd:cd05959    77 AGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAA---ALTKSEHTLVVLIVSGGAGPEAGALLLAELvaaeae 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  624 ---------QDVAYVIFTSGSTGRPKGVMNTHGSllnlilshkptIYW-------PVLeAVNERfpDRPLRAAHT-HSFS 686
Cdd:cd05959   154 qlkpaathaDDPAFWLYSSGSTGRPKGVVHLHAD-----------IYWtaelyarNVL-GIRED--DVCFSAAKLfFAYG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  687 FDSSWLqvFWMLWGQELHIFDENMRRDAFglVQEIQQRQIDTLDLPPSFCAQMMTN-GLFVENQHHPSLILIGGEAAPLA 765
Cdd:cd05959   220 LGNSLT--FPLSVGATTVLMPERPTPAAV--FKRIRRYRPTVFFGVPTLYAAMLAApNLPSRDLSSLRLCVSAGEALPAE 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  766 LWQQLNAqpaLFAHNLY---GPTE----YTVDTFRA-ELKQTARPVIGnpignTQAYVLDRHLQRCPTGVIGELYISGFG 837
Cdd:cd05959   296 VGERWKA---RFGLDILdgiGSTEmlhiFLSNRPGRvRYGTTGKPVPG-----YEVELRDEDGGDVADGEPGELYVRGPS 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  838 IANGYLGRADLSAARFVANpfehgqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVV 916
Cdd:cd05959   368 SATMYWNNRDKTRDTFQGE-------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVlEAAVV 440
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490930577  917 iaePINNSHRLL---GYCVVKD-IELDEKTSEQLsQQYlsqLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05959   441 ---GVEDEDGLTkpkAFVVLRPgYEDSEALEEEL-KEF---VKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
1557-1965 6.47e-23

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: 104.75  E-value: 6.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGE 1636
Cdd:cd17640     5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 --QKDLAAIvhpsiatfafnelfdetkvdlssykttvitpqhpaylIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLS 1714
Cdd:cd17640    85 ndSDDLATI-------------------------------------IYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1715 ATDTILQKTPctfdvsVWEFF---WSYLVGARLVIapiDAHRDPLALLSLIQKYQVTTLHFVPSML-AVFENAATEIL-S 1789
Cdd:cd17640   128 PGDRFLSILP------IWHSYersAEYFIFACGCS---QAYTSIRTLKDDLKRVKPHYIVSVPRLWeSLYSGIQKQVSkS 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1790 SAQRQSLPICRVF--------CSGEALPTALAKsFTEHFSCELHNLYGPTEAAVDVSymdatLGLHPEESCVAIGYPVWN 1861
Cdd:cd17640   199 SPIKQFLFLFFLSggifkfgiSGGGALPPHVDT-FFEAIGIEVLNGYGLTETSPVVS-----ARRLKCNVRGSVGRPLPG 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1862 TQLYILDQYLR-PVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQL 1940
Cdd:cd17640   273 TEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAKDTI 346
                         410       420
                  ....*....|....*....|....*....
gi 490930577 1941 KIR-GQRIELGEIEQQL---RLISGLDVV 1965
Cdd:cd17640   347 VLSnGENVEPQPIEEALmrsPFIEQIMVV 375
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
1677-2028 7.73e-23

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: 102.34  E-value: 7.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 PAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSE-YPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIApiDAHRDP 1755
Cdd:cd17635     3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG--GENTTY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1756 LALLSLIQKYQVTTLHFVPSMLAVFENAATEILssaqrQSLPICRVFCSGEALPTALAKSFTEHF-SCELHNLYGPTE-- 1832
Cdd:cd17635    81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSAN-----ATVPSLRLIGYGGSRAIAADVRFIEATgLTNTAQVYGLSEtg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1833 AAVDVSYMDATLGLHpeescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtag 1912
Cdd:cd17635   156 TALCLPTDDDSIEIN------AVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1913 qrmyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLvaYLQTTAPVD 1991
Cdd:cd17635   227 ----NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVqECACYEISDEEFGELVGL--AVVASAELD 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 490930577 1992 ---IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:cd17635   301 enaIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK07798 PRK07798
acyl-CoA synthetase; Validated
1533-2027 9.31e-23

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 104.97  E-value: 9.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI 1612
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1613 DLQHPTERIKFMLQDAksklvigeqkDLAAIVHPSiatfAFNELFDETKVDLSSYKTTV--------------------I 1672
Cdd:PRK07798   84 NYRYVEDELRYLLDDS----------DAVALVYER----EFAPRVAEVLPRLPKLRTLVvvedgsgndllpgavdyedaL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1673 TPQHPA-----------YLIYTSGTTGQPKGVMVSHQAIV----NRILWMQSEYPLSATDTILQKTPCTFDV-------- 1729
Cdd:PRK07798  150 AAGSPErdfgerspddlYLLYTGGTTGMPKGVMWRQEDIFrvllGGRDFATGEPIEDEEELAKRAAAGPGMRrfpapplm 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1730 ---SVWEFFWSYLVGARLVIAPiDAHRDPLALLSLIQKYQVTTLHFV------PsMLAVFENAATEILSSAQrqslpicr 1800
Cdd:PRK07798  230 hgaGQWAAFAALFSGQTVVLLP-DVRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEARGPYDLSSLF-------- 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1801 VFCSGEALPTALAKS-FTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYpvwNTQLyiLDQYLRPVPVGV 1878
Cdd:PRK07798  300 AIASGGALFSPSVKEaLLELLpNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGP---RTVV--LDEDGNPVEPGS 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1879 DGELYLA--GHqLAMGYLHRADLTASRFvanPFTAGQRMYRTGDIARWHADGSIQYIGRadDQLKIR--GQRIELGEIEQ 1954
Cdd:PRK07798  375 GEIGWIArrGH-IPLGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEE 448
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1955 QLRLISGL-DVVVHAISSEQ-NKANVQLVAyLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:PRK07798  449 ALKAHPDVaDALVVGVPDERwGQEVVAVVQ-LREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1102-1405 9.82e-23

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: 103.94  E-value: 9.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1102 PLLPLQKGMLFLSQVE-NQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElaeEPVFIYSLHPTQAWPVQ 1180
Cdd:cd20484     3 PLSEGQKGLWMLQKMSpEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEE---DGVPFQKIEPSKPLSFQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1181 ---FCSVTPDLLEQTIQEALQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQ-- 1254
Cdd:cd20484    80 eedISSLKESEIIAYLREKAKEPFVLENgP--LMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQgk 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1255 ---QLPVLEHSYETVI---KALSGRDHETSKVIWQRDLADLQP-LILFNQ-----AQQAVQET-SYRLSAELGAKLQHKL 1321
Cdd:cd20484   158 qptLASSPASYYDFVAweqDMLAGAEGEEHRAYWKQQLSGTLPiLELPADrprssAPSFEGQTyTRRLPSELSNQIKSFA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1322 RQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRsaPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVE 1401
Cdd:cd20484   238 RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGR--PEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLD 315

                  ....
gi 490930577 1402 HLEH 1405
Cdd:cd20484   316 GLDH 319
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
1558-2028 1.20e-22

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: 104.06  E-value: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLV-IGE 1636
Cdd:cd05914     8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIfVSD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 QKDLAAIvhpsiatfafnelfdetkvdlssykttvitpqhpaylIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSAT 1716
Cdd:cd05914    88 EDDVALI-------------------------------------NYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKG 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1717 DTILQKTP------CTFDvsvweFFWSYLVGARLVIApidaHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSS 1790
Cdd:cd05914   131 DKILSILPlhhiypLTFT-----LLLPLLNGAHVVFL----DKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPK 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1791 A------QRQSLPI--------------------CRVFCSGEA-LPTALAKSFTEHFSCELHNlYGPTEAAVDVSYmdat 1843
Cdd:cd05914   202 LtlkkfkFKLAKKInnrkirklafkkvheafggnIKEFVIGGAkINPDVEEFLRTIGFPYTIG-YGMTETAPIISY---- 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1844 lglHPEESCV--AIGYPVWNTQLYILDqylrPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDI 1921
Cdd:cd05914   277 ---SPPNRIRlgSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDL 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1922 ARWHADGSIQYIGRADDQLKI-RGQRIELGEIEQQlrlISGLDVVVHAISSEQNKaNVQLVAYLQTTA--------PVDI 1992
Cdd:cd05914   344 GKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAK---INNMPFVLESLVVVQEK-KLVALAYIDPDFldvkalkqRNII 419
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 490930577 1993 DQLK----KQLAKHLPAYMVPTHYMLV-EQFPLSHNGKLDR 2028
Cdd:cd05914   420 DAIKwevrDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1570-2049 1.36e-22

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 105.88  E-value: 1.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAG-AAYLPIDLQHPTERiKFMLQDAKSKLVI--GEQKDLAAivhP 1646
Cdd:PRK06060   43 LGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGvMAFLANPELHRDDH-ALAARNTEPALVVtsDALRDRFQ---P 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1647 SIATFAFNELFDETKVDLSSYKttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWM-QSEYPLSATDTILQKTPC 1725
Cdd:PRK06060  119 SRVAEAAELMSEAARVAPGGYE--PMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKALRLTPEDTGLCSARM 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1726 TFDVSVWEFFWSYL-VGARLVIAPIDAHRDPLALLSliQKYQVTTLHFVPSMLAvfenaatEILSSAQRQSLPICR-VFC 1803
Cdd:PRK06060  197 YFAYGLGNSVWFPLaTGGSAVINSAPVTPEAAAILS--ARFGPSVLYGVPNFFA-------RVIDSCSPDSFRSLRcVVS 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1804 SGEALPTALAKSFTEHFScELHNLYGPTEAAVDVSYMDATLGlhpEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELY 1883
Cdd:PRK06060  268 AGEALELGLAERLMEFFG-GIPILDGIGSTEVGQTFVSNRVD---EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLW 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1884 LAGHQLAMGYLHRADltasrfvanPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEqqlRLISGLD 1963
Cdd:PRK06060  344 VRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVE---RLIIEDE 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1964 VVVHA--ISSEQNKANVQLVAYLQTTAPVDIDQ-----LKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL----- 2031
Cdd:PRK06060  412 AVAEAavVAVRESTGASTLQAFLVATSGATIDGsvmrdLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqsp 491
                         490
                  ....*....|....*...
gi 490930577 2032 PQPHLTPSNTEKQYATSA 2049
Cdd:PRK06060  492 TKPIWELSLTEPGSGVRA 509
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
503-986 3.19e-22

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: 102.04  E-value: 3.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDypidrmqmmcedanplfvLTTQ 582
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR------------------LTPN 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  583 ALAQQLpqniqqlhldqegvqtqirkqdasdipaENRKFDFQDVAYVIFTSGSTGRPKGVMNT---H-----GSLLNLIL 654
Cdd:cd05912    64 ELAFQL----------------------------KDSDVKLDDIATIMYTSGTTGKPKGVQQTfgnHwwsaiGSALNLGL 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  655 SHKPTiyWpvLEAVnerfpdrPLraahthsfsFDSSWLQVFW--MLWGQELHIFDenmRRDAFGLVQEIQQRQIDTLdlp 732
Cdd:cd05912   116 TEDDN--W--LCAL-------PL---------FHISGLSILMrsVIYGMTVYLVD---KFDAEQVLHLINSGKVTII--- 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  733 pSFCAQMMTNGLFVENQHHPS---LILIGGEAAPLALWQQLnAQPALFAHNLYGPTEYT--VDTFRAELKQTARPVIGNP 807
Cdd:cd05912   170 -SVVPTMLQRLLEILGEGYPNnlrCILLGGGPAPKPLLEQC-KEKGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKP 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  808 IGNTQAYVldRHLQRCPTGViGELYISGFGIANGYLGRADLSAARFVANPFEhgqrmyrTGDLVRWNSAGKLEFMGRCDD 887
Cdd:cd05912   248 LFPVELKI--EDDGQPPYEV-GEILLKGPNVTKGYLNRPDATEESFENGWFK-------TGDIGYLDEEGFLYVLDRRSD 317
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  888 QIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNshrlLGYCVVKDIELDEKTSEQlsqQYLSQLRQNLPEYMVPSAL 967
Cdd:cd05912   318 LIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDK----WGQVPVAFVVSERPISEE---ELIAYCSEKLAKYKVPKKI 390
                         490
                  ....*....|....*....
gi 490930577  968 TVMSEFPRNVSGKVDKKAL 986
Cdd:cd05912   391 YFVDELPRTASGKLLRHEL 409
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
503-986 3.94e-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: 101.79  E-value: 3.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQ 582
Cdd:cd05935     2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  583 ALaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkpTIYW 662
Cdd:cd05935    82 EL---------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQ---SAVW 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  663 PVLEAVNERFPDRPLraahTHSFSFDSSWLQVfwMLWGQE---LHIFDENMRRDAfglvqeiqqrqIDTLDLPPSFCAQM 739
Cdd:cd05935   120 TGLTPSDVILACLPL----FHVTGFVGSLNTA--VYVGGTyvlMARWDRETALEL-----------IEKYKVTFWTNIPT 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  740 MTNGLF--VENQHH--PSLILIGGEAAPL--ALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQA 813
Cdd:cd05935   183 MLVDLLatPEFKTRdlSSLKVLTGGGAPMppAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDA 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  814 YVLD-RHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVanpFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIR 892
Cdd:cd05935   263 RVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVS 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  893 GYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEKTSEQLSQQYlsqLRQNLPEYMVPSALTVMSE 972
Cdd:cd05935   340 GFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIIEW---AREQMAAYKYPREVEFVDE 416
                         490
                  ....*....|....
gi 490930577  973 FPRNVSGKVDKKAL 986
Cdd:cd05935   417 LPRSASGKILWRLL 430
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
1545-2031 3.99e-22

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: 103.93  E-value: 3.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1545 TPEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAylpidlqH-- 1616
Cdd:cd05967    64 RGDQIALiydspvTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAI-------Hsv 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 ------PTE---RIkfmlQDAKSKLVIG-----------EQKDL--AAI---VHPSIATFAFNElfDETKVDLSSYKTTV 1671
Cdd:cd05967   137 vfggfaAKElasRI----DDAKPKLIVTascgiepgkvvPYKPLldKALelsGHKPHHVLVLNR--PQVPADLTKPGRDL 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1672 ----------------ITPQHPAYLIYTSGTTGQPKGVMVS---HQAIVNrilW-MQSEYPLSATDTILqktpCTFDVSv 1731
Cdd:cd05967   211 dwsellakaepvdcvpVAATDPLYILYTSGTTGKPKGVVRDnggHAVALN---WsMRNIYGIKPGDVWW----AASDVG- 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1732 WEFFWSYLV------GARLVI---APiDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEIlSSAQRQSLPICRV- 1801
Cdd:cd05967   283 WVVGHSYIVygpllhGATTVLyegKP-VGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDG-KYIKKYDLSSLRTl 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1802 FCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAiGYPVWNTQLYILDQYLRPVPVGVDGE 1881
Cdd:cd05967   361 FLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEPLPIKAGSP-GKPVPGYQVQVLDEDGEPVGPNELGN 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1882 LYLAGhQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlRLISG 1961
Cdd:cd05967   440 IVIKL-PLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE--SVLSH 516
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 1962 LDVVVHAI--SSEQNKANVQLVAY-LQTTAPVDIDQLKKQLAKH----LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05967   517 PAVAECAVvgVRDELKGQVPLGLVvLKEGVKITAEELEKELVALvreqIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
624-983 1.18e-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: 98.87  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  624 QDVAYVIFTSGSTGRPKGVMNTHGSL---LNLILSHkptiywpVLEAVNERFPDRPLRAAHthsfSFDSSWLQVFwMLWG 700
Cdd:cd17635     1 EDPLAVIFTSGTTGEPKAVLLANKTFfavPDILQKE-------GLNWVVGDVTYLPLPATH----IGGLWWILTC-LIHG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  701 QELHIFDENMRRDAFglVQEIQQRQIDTLDLPPSFCAQMmTNGLFVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFA 778
Cdd:cd17635    69 GLCVTGGENTTYKSL--FKILTTNAVTTTCLVPTLLSKL-VSELKSANATVPSLrlIGYGGSRAIAADVRFIEATGLTNT 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  779 HNLYGPTEytvdTFRAELKQTARPVI-----GNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARF 853
Cdd:cd17635   146 AQVYGLSE----TGTALCLPTDDDSIeinavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  854 VANPFehgqrmyRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVV 933
Cdd:cd17635   222 IDGWV-------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV 294
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 490930577  934 KDIELDEKTSEQLSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:cd17635   295 ASAELDENAIRALKH----TIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1538-2031 1.26e-21

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 101.09  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1538 LREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQ-RAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:PRK06839    8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKDLAAI--------VHPSIATFAFNELFDETKVDLSSYkttviTPQHPAYLIYTSGTTG 1688
Cdd:PRK06839   88 TENELIFQLKDSGTTVLFVEKTFQNMAlsmqkvsyVQRVISITSLKEIEDRKIDNFVEK-----NESASFIICYTSGTTG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1689 QPKGVMVSHQAI----VNRILWMQseypLSATDTILQKTPCTFDVSVWEF-FWSYLVGARLVIApidAHRDPLALLSLIQ 1763
Cdd:PRK06839  163 KPKGAVLTQENMfwnaLNNTFAID----LTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVIIVP---RKFEPTKALSMIE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQVTTLHFVPSMLAVFENAateilSSAQRQSLPICRVFCSGEA-LPTALAKSFTEHfSCELHNLYGPTEAAVDVsYMDA 1842
Cdd:PRK06839  236 KHKVTVVMGVPTIHQALINC-----SKFETTNLQSVRWFYNGGApCPEELMREFIDR-GFLFGQGFGMTETSPTV-FMLS 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1843 tlglhpEESCV----AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASrfvanpfTAGQRMYRT 1918
Cdd:PRK06839  309 ------EEDARrkvgSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE-------TIQDGWLCT 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1919 GDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKK 1997
Cdd:PRK06839  376 GDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVyEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIE 455
                         490       500       510
                  ....*....|....*....|....*....|....
gi 490930577 1998 QLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06839  456 HCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
PLN02246 PLN02246
4-coumarate--CoA ligase
1556-2031 2.40e-21

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 100.83  E-value: 2.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1556 HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG 1635
Cdd:PLN02246   49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1636 EQ------KDLAAIVHPSIAT--------FAFNELfdeTKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIV 1701
Cdd:PLN02246  129 QScyvdklKGLAEDDGVTVVTiddppegcLHFSEL---TQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLV 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1702 NRIL-WMQSEYP---LSATDTILQKTPcTFDV----SVweFFWSYLVGARLVIAPidaHRDPLALLSLIQKYQVTTLHFV 1773
Cdd:PLN02246  206 TSVAqQVDGENPnlyFHSDDVILCVLP-MFHIyslnSV--LLCGLRVGAAILIMP---KFEIGALLELIQRHKVTIAPFV 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1774 PS-MLAVFENAATEI--LSSAqrqslpicRVFCSGEAlptALAKSFTEHFSCELHNL-----YGPTEAAvDVSYMDATLG 1845
Cdd:PLN02246  280 PPiVLAIAKSPVVEKydLSSI--------RMVLSGAA---PLGKELEDAFRAKLPNAvlgqgYGMTEAG-PVLAMCLAFA 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1846 LHPEE----SCvaiGYPVWNTQLYILDqylrP-----VPVGVDGELYLAGHQLAMGYLHRADLTAsrfvanpftagqrmy 1916
Cdd:PLN02246  348 KEPFPvksgSC---GTVVRNAELKIVD----PetgasLPRNQPGEICIRGPQIMKGYLNDPEATA--------------- 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1917 RTGDIARWHADGSIQYIGRaDDQL----------KIRGQRIELGEIEQQlrLISGLDVVVHAISSEQNKANVQL-VAYLQ 1985
Cdd:PLN02246  406 NTIDKDGWLHTGDIGYIDD-DDELfivdrlkeliKYKGFQVAPAELEAL--LISHPSIADAAVVPMKDEVAGEVpVAFVV 482
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 490930577 1986 TTAPVDI--DQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PLN02246  483 RSNGSEIteDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
1570-2035 3.59e-21

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 99.98  E-value: 3.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDlQHPT-ERIKFMLQDAKSKLVIGEQkDLAAIVHPSI 1648
Cdd:PRK08276   24 LAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPIN-WHLTaAEIAYIVDDSGAKVLIVSA-ALADTAAELA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1649 ATF----AFNELFDETKVDLSSYKTTVitPQHPAYLI----------YTSGTTGQPKGVMVSHQAIvnrilwmQSEYPLS 1714
Cdd:PRK08276  102 AELpagvPLLLVVAGPVPGFRSYEEAL--AAQPDTPIadetagadmlYSSGTTGRPKGIKRPLPGL-------DPDEAPG 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1715 ATDTILQKTPCTFDVSVweffwsYLVGARLV-IAP---------------IDAHRDPLALLSLIQKYQVTTLHFVPSM-- 1776
Cdd:PRK08276  173 MMLALLGFGMYGGPDSV------YLSPAPLYhTAPlrfgmsalalggtvvVMEKFDAEEALALIERYRVTHSQLVPTMfv 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1777 --LAvfenaateiLSSAQRQSLPIC---RVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAvDVSYMDATLGL-HPEe 1850
Cdd:PRK08276  247 rmLK---------LPEEVRARYDVSslrVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGG-GVTVITSEDWLaHPG- 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1851 scvAIGYPvWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVanpftaGQRMYRTGDIARWHADGSI 1930
Cdd:PRK08276  316 ---SVGKA-VLGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN------PHGWVTVGDVGYLDEDGYL 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1931 QYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVV----HAISSEQNKANVQLVAylQTTAPVDI-DQLKKQLAKHLP 2004
Cdd:PRK08276  386 YLTDRKSDMIISGGVNIYPQEIENLLVTHPKvADVAVfgvpDEEMGERVKAVVQPAD--GADAGDALaAELIAWLRGRLA 463
                         490       500       510
                  ....*....|....*....|....*....|.
gi 490930577 2005 AYMVPTHYMLVEQFPLSHNGKLDRKALPQPH 2035
Cdd:PRK08276  464 HYKCPRSIDFEDELPRTPTGKLYKRRLRDRY 494
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
1530-2040 6.09e-21

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 99.87  E-value: 6.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:PLN02860    5 SQAHICQCLTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKF-MLQDAKSKLVIGEQKDLAAIVH-----PSIATFAF-NELFDETKVDLSSYKTT------VITPQH 1676
Cdd:PLN02860   85 APLNYRWSFEEAKSaMLLVRPVMLVTDETCSSWYEELqndrlPSLMWQVFlESPSSSVFIFLNSFLTTemlkqrALGTTE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 PAY--------LI-YTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIA 1747
Cdd:PLN02860  165 LDYawapddavLIcFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1748 P-IDAHrdplALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSlpICRVFCSGEALPTALAKSFTEHFSC-ELH 1825
Cdd:PLN02860  245 PkFDAK----AALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPS--VRKILNGGGSLSSRLLPDAKKLFPNaKLF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1826 NLYGPTEAAVDVSYM---DATL-----------------GLHPEESCVaiGYPVWNTQLYI-LDQYLRpvpvgvDGELYL 1884
Cdd:PLN02860  319 SAYGMTEACSSLTFMtlhDPTLespkqtlqtvnqtksssVHQPQGVCV--GKPAPHVELKIgLDESSR------VGRILT 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1885 AGHQLAMGYLHRADLTASRFVANPFTAgqrmyrTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LD 1963
Cdd:PLN02860  391 RGPHVMLGYWGQNSETASVLSNDGWLD------TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGvAS 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1964 VVVHAISSEQNKANVQLVAYLQ---TTAPVDIDQLKKQLA------------KHLPAYMVPTHYML-VEQFPLSHNGK-- 2025
Cdd:PLN02860  465 VVVVGVPDSRLTEMVVACVRLRdgwIWSDNEKENAKKNLTlssetlrhhcreKNLSRFKIPKLFVQwRKPFPLTTTGKir 544
                         570
                  ....*....|....*...
gi 490930577 2026 ---LDRKALPQPHLTPSN 2040
Cdd:PLN02860  545 rdeVRREVLSHLQSLPSN 562
PRK07787 PRK07787
acyl-CoA synthetase; Validated
1547-2034 8.18e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 98.52  E-value: 8.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1547 EQTALSDENHQLSFSEVRLQVCALAQQLQRAgvqagDIVAV-ALPrSVKLSIAILAVIEAGAAYLPIDLQH-PTERiKFM 1624
Cdd:PRK07787   15 IADAVRIGGRVLSRSDLAGAATAVAERVAGA-----RRVAVlATP-TLATVLAVVGALIAGVPVVPVPPDSgVAER-RHI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1625 LQDAKSKLVIGE-QKDLAAIvhPSIatfafnelfdetKVDL---SSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAI 1700
Cdd:PRK07787   88 LADSGAQAWLGPaPDDPAGL--PHV------------PVRLharSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRILWMQSEYPLSATDTILQKTPcTFDVS--VWEFFWSYLVGARLV----IAPiDAHRDPLALLSliqkyqvtTLHF-V 1773
Cdd:PRK07787  154 AADLDALAEAWQWTADDVLVHGLP-LFHVHglVLGVLGPLRIGNRFVhtgrPTP-EAYAQALSEGG--------TLYFgV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1774 PSM---LAVFENAAtEILSSAqrqslpicRVFCSGEA-LPTALAKSFTEHFSCELHNLYGPTEAAVDVS-YMDAtlglhp 1848
Cdd:PRK07787  224 PTVwsrIAADPEAA-RALRGA--------RLLVSGSAaLPVPVFDRLAALTGHRPVERYGMTETLITLStRADG------ 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1849 EESCVAIGYPVWNTQLYILDQYLRPVPVGVD--GELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHA 1926
Cdd:PRK07787  289 ERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDP 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1927 DGSIQYIGR-ADDQLKIRGQRIELGEIEQQlrLISGLDVVVHAISSE------QnkanvQLVAYLQTTAPVDIDQLKKQL 1999
Cdd:PRK07787  363 DGMHRIVGReSTDLIKSGGYRIGAGEIETA--LLGHPGVREAAVVGVpdddlgQ-----RIVAYVVGADDVAADELIDFV 435
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 490930577 2000 AKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQP 2034
Cdd:PRK07787  436 AQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
1533-2031 9.88e-21

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: 98.89  E-value: 9.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQAR------ITPEQTALSDENhqLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAG 1606
Cdd:cd05906    11 TLLELLLRAAErgptkgITYIDADGSEEF--QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1607 aaYLPIDL---------QHPTERIKFMLQDAKSKLVIGEQKDLAAI-------VHPSIATFAFNELFDEtkvdLSSYKTT 1670
Cdd:cd05906    89 --FVPAPLtvpptydepNARLRKLRHIWQLLGSPVVLTDAELVAEFagletlsGLPGIRVLSIEELLDT----AADHDLP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1671 VITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPctFD--VSVWEF--FWSYLvGARLVI 1746
Cdd:cd05906   163 QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVP--LDhvGGLVELhlRAVYL-GCQQVH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1747 APIDA-HRDPLALLSLIQKYQVtTLHFVPS-MLAVFENAATEIlsSAQRQSLPICRVFCS-GEALPTALAKSFTEHFscE 1823
Cdd:cd05906   240 VPTEEiLADPLRWLDLIDRYRV-TITWAPNfAFALLNDLLEEI--EDGTWDLSSLRYLVNaGEAVVAKTIRRLLRLL--E 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1824 LHNL--------YGPTE--AAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGY 1893
Cdd:cd05906   315 PYGLppdairpaFGMTEtcSGVIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGY 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1894 LHRADLTASRFVANPFtagqrmYRTGDIArWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISGLDVVVH------ 1967
Cdd:cd05906   395 YNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPsftaaf 464
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1968 AISSEQNKANVQLVAYLQTTAPVD-----IDQLKKQLAKHL---PAYMVPTHYmlvEQFPLSHNGKLDRKAL 2031
Cdd:cd05906   465 AVRDPGAETEELAIFFVPEYDLQDalsetLRAIRSVVSREVgvsPAYLIPLPK---EEIPKTSLGKIQRSKL 533
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
502-893 2.34e-20

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: 97.69  E-value: 2.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  502 HLSFAELAVKVNQLTRFLQENGARKQTVIAGAiPRSIDSVVVMLSVLNSGASFLPLDLDYP---IDRMQMMCEDANPLFV 578
Cdd:cd05931    24 TLTYAELDRRARAIAARLQAVGKPGDRVLLLA-PPGLDFVAAFLGCLYAGAIAVPLPPPTPgrhAERLAAILADAGPRVV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  579 LTTQALAQQLPQniqQLHLDQEGVQTQIRKQDASDI----PAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLL-Nli 653
Cdd:cd05931   103 LTTAAALAAVRA---FAASRPAAGTPRLLVVDLLPDtsaaDWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLaN-- 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  654 lshkptiywpvLEAVNERFPDRPlraaHTHSFsfdsSWLQVF--------------------WM----------LWGQEL 703
Cdd:cd05931   178 -----------VRQIRRAYGLDP----GDVVV----SWLPLYhdmgligglltplysggpsvLMspaaflrrplRWLRLI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  704 ------HIFDENMrrdAFGL-VQEIQQRQIDTLDLppsfcaqmmtnglfvenqHHPSLILIGGE---AAPLALWQQ---- 769
Cdd:cd05931   239 sryratISAAPNF---AYDLcVRRVRDEDLEGLDL------------------SSWRVALNGAEpvrPATLRRFAEafap 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  770 --LNAQpALFAHnlYG-------------PTEYTVDTF-RAELKQTARPVI------------GNPIGNTQAYVLDR-HL 820
Cdd:cd05931   298 fgFRPE-AFRPS--YGlaeatlfvsggppGTGPVVLRVdRDALAGRAVAVAaddpaarelvscGRPLPDQEVRIVDPeTG 374
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490930577  821 QRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDL-VRWNsaGKLEFMGRCDDQIKIRG 893
Cdd:cd05931   375 RELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLgFLHD--GELYITGRLKDLIIVRG 446
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
1529-2028 2.66e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 97.54  E-value: 2.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1529 VRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRL--QVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAG 1606
Cdd:PRK12583   15 LLTQTIGDAFDATVARFPDREALVVRHQALRYTWRQLadAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1607 AAYLPIDLQHPTERIKFMLQDAKSKLVIG----EQKDLAAIVH---PSIATFAFNELFDE-------------------- 1659
Cdd:PRK12583   95 AILVNINPAYRASELEYALGQSGVRWVICadafKTSDYHAMLQellPGLAEGQPGALACErlpelrgvvslapapppgfl 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1660 ------------TKVDLSSyKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIlWMQSEyPLSATDTILQKTPctf 1727
Cdd:PRK12583  175 awhelqargetvSREALAE-RQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNG-YFVAE-SLGLTEHDRLCVP--- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1728 dVSVWEFFWSYL-------VGARLVIaPIDAHrDPLALLSLIQKYQVTTLHFVPSMLaVFEnaateiLSSAQRQSLPICR 1800
Cdd:PRK12583  249 -VPLYHCFGMVLanlgcmtVGACLVY-PNEAF-DPLATLQAVEEERCTALYGVPTMF-IAE------LDHPQRGNFDLSS 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1801 V---FCSGEALPTALAKSFTEHFSC-ELHNLYGPTEAAvDVSYMDATlgLHPEESCVA-IGYPVWNTQLYILDQYLRPVP 1875
Cdd:PRK12583  319 LrtgIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETS-PVSLQTTA--ADDLERRVEtVGRTQPHLEVKVVDPDGATVP 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1876 VGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrMYrTGDIARWHADGSIQYIGRADDQLkIR-GQRIELGEIEQ 1954
Cdd:PRK12583  396 RGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMI-IRgGENIYPREIEE 468
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 1955 QLRLISGL-DVVVHAISSEqnKANVQLVAY--LQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:PRK12583  469 FLFTHPAVaDVQVFGVPDE--KYGEEIVAWvrLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
480-920 2.74e-20

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: 97.31  E-value: 2.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  480 YEQVKKYPERTAIVSGerPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDL 559
Cdd:cd05904    12 FLFASAHPSRPALIDA--ATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  560 DYPIDRMQMMCEDANPLFVLTTQALAQQLPQN------IQQLHLDQEGVQTQIRKQDASDIPAENRKFDfqDVAYVIFTS 633
Cdd:cd05904    90 LSTPAEIAKQVKDSGAKLAFTTAELAEKLASLalpvvlLDSAEFDSLSFSDLLFEADEAEPPVVVIKQD--DVAALLYSS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  634 GSTGRPKGVMNTHGSLLNLILSHKPtiywpvLEAVNERFPDR-----PLraahTHSFSFdsSWLQVFWMLWGQELHIfde 708
Cdd:cd05904   168 GTTGRSKGVMLTHRNLIAMVAQFVA------GEGSNSDSEDVflcvlPM----FHIYGL--SSFALGLLRLGATVVV--- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  709 nMRR-DAFGLVQEIQQRQIDTLDL-PPSFCAqmMTNGLFVENQHHPSLILIGGEAAPLalwqqlnaQPAL---FAHNL-- 781
Cdd:cd05904   233 -MPRfDLEELLAAIERYKVTHLPVvPPIVLA--LVKSPIVDKYDLSSLRQIMSGAAPL--------GKELieaFRAKFpn 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  782 ------YGPTEYT--VDTFRAELKQTARPV-IGNPIGNTQAYVLD----RHLqrcPTGVIGELYISGFGIANGYLGRADL 848
Cdd:cd05904   302 vdlgqgYGMTESTgvVAMCFAPEKDRAKYGsVGRLVPNVEAKIVDpetgESL---PPNQTGELWIRGPSIMKGYLNNPEA 378
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577  849 SAARFVanpfehGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:cd05904   379 TAATID------KEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYP 444
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
1533-2031 3.58e-20

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 97.06  E-value: 3.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSDENHQLSFSEVRLQvcALAQQLQRA-------GVQAGDIVAVALPRSVKLSIAILAVIEA 1605
Cdd:PRK08008    8 HLRQMWDDLADVYGHKTALIFESSGGVVRRYSYL--ELNEEINRTanlfyslGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1606 GAAYLPIDLQHPTERIKFMLQDAKSKLVIGE-----------QKDLAAIVHPSIA---------TFAFNELFDETKVDLS 1665
Cdd:PRK08008   86 GAIMVPINARLLREESAWILQNSQASLLVTSaqfypmyrqiqQEDATPLRHICLTrvalpaddgVSSFTQLKAQQPATLC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1666 syKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTP-------CTFDVSVweffwsY 1738
Cdd:PRK08008  166 --YAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPafhidcqCTAAMAA------F 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1739 LVGARLVIAPIDAHRdplALLSLIQKYQVTTLHFVPSMLavfenaATEILSSAQrqslPICRVFCSGE-----ALPTALA 1813
Cdd:PRK08008  238 SAGATFVLLEKYSAR---AFWGQVCKYRATITECIPMMI------RTLMVQPPS----ANDRQHCLREvmfylNLSDQEK 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1814 KSFTEHFSCELHNLYGPTEAAVDVsymdatLGLHP--EESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYL---AGHQ 1888
Cdd:PRK08008  305 DAFEERFGVRLLTSYGMTETIVGI------IGDRPgdKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKT 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1889 LAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISG----LDV 1964
Cdd:PRK08008  379 IFKEYYLDPKATAKVLEADGW------LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELEN---IIAThpkiQDI 449
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1965 VV----HAISSEQNKANVQLVAylqtTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK08008  450 VVvgikDSIRDEAIKAFVVLNE----GETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
1541-2031 7.94e-20

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 96.55  E-value: 7.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1541 QARITPEQTAL---SDENHQ---LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAA------ 1608
Cdd:TIGR02188   66 HLEARPDKVAIiweGDEPGEvrkITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIhsvvfg 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1609 -YLPIDLQhptERIkfmlQDAKSKLVI--------GEQKDLAAIVHPSIA------------------TFAFNE----LF 1657
Cdd:TIGR02188  146 gFSAEALA---DRI----NDAGAKLVItadeglrgGKVIPLKAIVDEALEkcpvsvehvlvvrrtgnpVVPWVEgrdvWW 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1658 DETKVDLSSY-KTTVITPQHPAYLIYTSGTTGQPKGVMVShqaivnrilwmQSEYPLSATDTilQKTpcTFDVSVWEFFW 1736
Cdd:TIGR02188  219 HDLMAKASAYcEPEPMDSEDPLFILYTSGSTGKPKGVLHT-----------TGGYLLYAAMT--MKY--VFDIKDGDIFW 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1737 -----------SYLV------GARLVI---APidAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSL 1796
Cdd:TIGR02188  284 ctadvgwitghSYIVygplanGATTVMfegVP--TYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSL 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1797 picRVFCS-GEALptalaksftehfSCE----LHNLYGPTEAA-VDVSYMDATLG--LHPEESCVAI-----GYPVWNTQ 1863
Cdd:TIGR02188  362 ---RLLGSvGEPI------------NPEawmwYYKVVGKERCPiVDTWWQTETGGimITPLPGATPTkpgsaTLPFFGIE 426
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1864 LYILDQYLRPVPvGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:TIGR02188  427 PAVVDEEGNPVE-GPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVS 505
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  1944 GQRIELGEIEQQlrLISGLDV----VV---HAISSEqnkANVQLVAYLQTTAPVD--IDQLKKQLAKHLPAYMVPTHYML 2014
Cdd:TIGR02188  506 GHRLGTAEIESA--LVSHPAVaeaaVVgipDDIKGQ---AIYAFVTLKDGYEPDDelRKELRKHVRKEIGPIAKPDKIRF 580
                          570
                   ....*....|....*..
gi 490930577  2015 VEQFPLSHNGKLDRKAL 2031
Cdd:TIGR02188  581 VPGLPKTRSGKIMRRLL 597
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
1101-1501 1.19e-19

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: 94.36  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQ-SNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElAEEPVFIYSlhPTQAWPV 1179
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEgSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWID--PYTPVPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTPD-----LLEQTIQEALQQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ--T 1252
Cdd:cd19533    79 RHIDLSGDpdpegAAQQWMQEDLRKPLPLDND-PLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTAllK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1253 NQQLPV-LEHSYETVI---KALSGRDH-ETSKVIWQRDLADLQPLILFNQAQQAVQETSYRLSAELGAKLQHKLRQQ--- 1324
Cdd:cd19533   158 GRPAPPaPFGSFLDLVeeeQAYRQSERfERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAELPPELTRTLLEAaea 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1325 -GITLNVFMQMIWAmtlnIYAHR----EDIVFGTPVSGRsapINGLEQQI-GLFLNTIPVRVKLNMQQTLWEQLPQL--- 1395
Cdd:cd19533   238 hGASWPSFFIALVA----AYLHRltgaNDVVLGVPVMGR---LGAAARQTpGMVANTLPLRLTVDPQQTFAELVAQVsre 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1396 -------QQLHVEHLEHDgLGLSAIQQliaqgNLFDSLLVVENYpdnQYlQQKLGDAAiskLTNRGYSHYP---LALLVI 1465
Cdd:cd19533   311 lrsllrhQRYRYEDLRRD-LGLTGELH-----PLFGPTVNYMPF---DY-GLDFGGVV---GLTHNLSSGPtndLSIFVY 377
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 490930577 1466 P--DH---QIElLLEQRGVIDQPE---HfLERMIQLIEIALNEP 1501
Cdd:cd19533   378 DrdDEsglRID-FDANPALYSGEDlarH-QERLLRLLEEAAADP 419
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
1100-1464 1.33e-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: 94.04  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNgdiDPVRLQ---QALITVLKRHpqlgghfD-------SELAEEPVfi 1168
Cdd:cd19544     1 IYPLAPLQEGILFHHLLAEEGDpYLLRSLLAFD---SRARLDaflAALQQVIDRH-------DilrtailWEGLSEPV-- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1169 yslhptQA-W-----PVQFCSVTP--DLLEQTIQ--EALQQPIHLDQ-PygLIRATLIQHAPEQS-ELLIMVHHLLTDgw 1236
Cdd:cd19544    69 ------QVvWrqaelPVEELTLDPgdDALAQLRArfDPRRYRLDLRQaP--LLRAHVAEDPANGRwLLLLLFHHLISD-- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1237 STPL-FLQDFIKAYQQTN-QQLPVLEhSYETVI-KALSGRDHETSKVIWQRDLADL-QPLILFNQAQ-----QAVQETSY 1307
Cdd:cd19544   139 HTSLeLLLEEIQAILAGRaAALPPPV-PYRNFVaQARLGASQAEHEAFFREMLGDVdEPTAPFGLLDvqgdgSDITEARL 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1308 RLSAELGAKLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNmQQT 1387
Cdd:cd19544   218 ALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRS 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1388 LWEQLPQLQQLHVEHLEHDGLGLSAIQQ---LIAQGNLFDSLLvveNY---PDNQYLQQKLGDAAISKLTNRGYSHYPLA 1461
Cdd:cd19544   297 VREAVRQTHARLAELLRHEHASLALAQRcsgVPAPTPLFSALL---NYrhsAAAAAAAALAAWEGIELLGGEERTNYPLT 373

                  ...
gi 490930577 1462 LLV 1464
Cdd:cd19544   374 LSV 376
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
1525-2031 1.36e-19

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 95.47  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1525 TQYyvrqSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIE 1604
Cdd:PRK07059   20 SQY----PSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLR 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1605 AGAA-------YLPIDLQHP-----TERIkFMLQDAKSKL------------VIGEQKDL----AAIVH----------P 1646
Cdd:PRK07059   96 AGYVvvnvnplYTPRELEHQlkdsgAEAI-VVLENFATTVqqvlaktavkhvVVASMGDLlgfkGHIVNfvvrrvkkmvP 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1647 --SIATF-AFNELFDETKVdlSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL----WMQSEYPLSATDTI 1719
Cdd:PRK07059  175 awSLPGHvRFNDALAEGAR--QTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLqmeaWLQPAFEKKPRPDQ 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1720 LQkTPCT------FDVSVwEFFWSYLVGARLVIAPidAHRDPLALLSLIQKYQVttlHFVPSMLAVFeNAateILSSAQR 1793
Cdd:PRK07059  253 LN-FVCAlplyhiFALTV-CGLLGMRTGGRNILIP--NPRDIPGFIKELKKYQV---HIFPAVNTLY-NA---LLNNPDF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1794 QSL---PICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAA--VDVSYMDATlglhpeESCVAIGYPVWNTQLYILD 1868
Cdd:PRK07059  322 DKLdfsKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSpvATCNPVDAT------EFSGTIGLPLPSTEVSIRD 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1869 QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIE 1948
Cdd:PRK07059  396 DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVY 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1949 LGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVDiDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:PRK07059  470 PNEIEEVVASHPGvLEVAAVGVPDEHSGEAVKLFVVKKDPALTE-EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKIL 548

                  ....
gi 490930577 2028 RKAL 2031
Cdd:PRK07059  549 RREL 552
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
1542-2033 1.39e-19

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 94.55  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQ--DAKSKLVIGEQKDLAAIVHPSIATFAfnelfDETKVDLSsykttvitPQHPAYLIYTSGTTGQPKGVMVSHQA 1699
Cdd:PRK09029   93 EELLPslTLDFALVLEGENTFSALTSLHLQLVE-----GAHAVAWQ--------PQRLATMTLTSGSTGLPKAAVHTAQA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1700 IVNRILWMQSEYPLSATDTILQKTPcTFDVS----VWEffWsYLVGARLVIapidahRDPLALLSLIQkyQVTTLHFVPS 1775
Cdd:PRK09029  160 HLASAEGVLSLMPFTAQDSWLLSLP-LFHVSgqgiVWR--W-LYAGATLVV------RDKQPLEQALA--GCTHASLVPT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 MLavfenaaTEILSSAQrQSLPICRVFCSGEALPTALAKSFTEH-FSCELHnlYGPTEAA--VDVSYMDATLGlhpeesc 1852
Cdd:PRK09029  228 QL-------WRLLDNRS-EPLSLKAVLLGGAAIPVELTEQAEQQgIRCWCG--YGLTEMAstVCAKRADGLAG------- 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1853 vaIGYPVWNTQLYIldqylrpvpvgVDGELYLAGHQLAMGYLHRADLTasrfvanPFTAGQRMYRTGDIARWHaDGSIQY 1932
Cdd:PRK09029  291 --VGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGELTI 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1933 IGRADDQLKIRGQRIELGEIEqqlRLISGLDVVVHAISSEQnkANVQL----VAYLQTTAPVDIDQLKKQLAKHLPAYMV 2008
Cdd:PRK09029  350 LGRLDNLFFSGGEGIQPEEIE---RVINQHPLVQQVFVVPV--ADAEFgqrpVAVVESDSEAAVVNLAEWLQDKLARFQQ 424
                         490       500
                  ....*....|....*....|....*
gi 490930577 2009 PTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK09029  425 PVAYYLLPPELKNGGIKISRQALKE 449
PLN02574 PLN02574
4-coumarate--CoA ligase-like
1546-2031 2.31e-19

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 94.52  E-value: 2.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSD--ENHQLSFSEVRLQVCALAQQL-QRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID-LQHPTErI 1621
Cdd:PLN02574   53 NGDTALIDssTGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNpSSSLGE-I 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGEQKD---LAAIVHPSIATfAFNELFDETKVDLSSYKTT-----------VITPQHPAYLIYTSGTT 1687
Cdd:PLN02574  132 KKRVVDCSVGLAFTSPENvekLSPLGVPVIGV-PENYDFDSKRIEFPKFYELikedfdfvpkpVIKQDDVAAIMYSSGTT 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1688 GQPKGVMVSHQAIVNRI-LWMQ---SEYPLSATDTILQKTPCTFDVSVWEFFWSYLV---GARLVIAPIDAHRdplaLLS 1760
Cdd:PLN02574  211 GASKGVVLTHRNLIAMVeLFVRfeaSQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLslgSTIVVMRRFDASD----MVK 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1761 LIQKYQVTTLHFVPSMLAVFENAAteilSSAQRQSLPICRVFCSGEA-LPTALAKSFTEHFS-CELHNLYGPTE-AAVdv 1837
Cdd:PLN02574  287 VIDRFKVTHFPVVPPILMALTKKA----KGVCGEVLKSLKQVSCGAApLSGKFIQDFVQTLPhVDFIQGYGMTEsTAV-- 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1838 symdATLGLHPEE--SCVAIGYPVWNTQLYILDQYLRP-VPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqr 1914
Cdd:PLN02574  361 ----GTRGFNTEKlsKYSSVGLLAPNMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW----- 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1915 mYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQlrLISGLDVVVHAISSEQNKA----NVQLVAYLQTTApV 1990
Cdd:PLN02574  432 -LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAV--LISHPEIIDAAVTAVPDKEcgeiPVAFVVRRQGST-L 507
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 490930577 1991 DIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PLN02574  508 SQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
1532-2031 2.88e-19

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 94.44  E-value: 2.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQR-AGVQAGDIVAVALPRSVKLSIAILAVIEAG---- 1606
Cdd:PRK05677   24 PNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGlivv 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1607 ---AAYLPIDLQHpteriKFMLQDAKSKLVIGEQKDLAAIV-----------------HPSIATFAFNELFDETKVDLSS 1666
Cdd:PRK05677  104 ntnPLYTAREMEH-----QFNDSGAKALVCLANMAHLAEKVlpktgvkhvivtevadmLPPLKRLLINAVVKHVKKMVPA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1667 YK-------TTVI--------TPQHP-----AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQseyPLSAT------DTIL 1720
Cdd:PRK05677  179 YHlpqavkfNDALakgagqpvTEANPqaddvAVLQYTGGTTGVAKGAMLTHRNLVANMLQCR---ALMGSnlnegcEILI 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1721 QKTPC------TFDVSVweffwSYLVGARLVIapIDAHRDPLALLSLIQKYQVT------TLhFVpsmlAVFENAATEIL 1788
Cdd:PRK05677  256 APLPLyhiyafTFHCMA-----MMLIGNHNIL--ISNPRDLPAMVKELGKWKFSgfvglnTL-FV----ALCNNEAFRKL 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1789 S-SAQRQSLPicrvfcSGEALPTALAKSFTEHFSCELHNLYGPTEAA--VDVSYMDAT-LGlhpeescvAIGYPVWNTQL 1864
Cdd:PRK05677  324 DfSALKLTLS------GGMALQLATAERWKEVTGCAICEGYGMTETSpvVSVNPSQAIqVG--------TIGIPVPSTLC 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:PRK05677  390 KVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSG 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1945 QRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHN 2023
Cdd:PRK05677  464 FNVYPNELEDVLAALPGvLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNV 543

                  ....*...
gi 490930577 2024 GKLDRKAL 2031
Cdd:PRK05677  544 GKILRREL 551
PRK06145 PRK06145
acyl-CoA synthetase; Validated
484-986 3.92e-19

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 93.41  E-value: 3.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  484 KKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPI 563
Cdd:PRK06145   13 RRTPDRAALVYRD----QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  564 DRMQMMCEDANPLFVLTTQALAQQLPQNIQQLHLDqEGVQTQIRKQDASDIP-AENRKFDFQDVAYVIFTSGSTGRPKGV 642
Cdd:PRK06145   89 DEVAYILGDAGAKLLLVDEEFDAIVALETPKIVID-AAAQADSRRLAQGGLEiPPQAAVAPTDLVRLMYTSGTTDRPKGV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  643 MNTHGSLlnlilshkptiYWPVLE---AVNERFPDRPLRAAHT-HSFSFDSSWLQVFWMlwGQELHIfdenMRR-DAFGL 717
Cdd:PRK06145  168 MHSYGNL-----------HWKSIDhviALGLTASERLLVVGPLyHVGAFDLPGIAVLWV--GGTLRI----HREfDPEAV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  718 VQEIQQRQIDTLDLPPSFCAQMMTnglfVENQHHPSL-----ILIGGEAAPlalWQQLNAQPALFAH----NLYGPTEyT 788
Cdd:PRK06145  231 LAAIERHRLTCAWMAPVMLSRVLT----VPDRDRFDLdslawCIGGGEKTP---ESRIRDFTRVFTRaryiDAYGLTE-T 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  789 V--DTFRAELKQTAR-PVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmy 865
Cdd:PRK06145  303 CsgDTLMEAGREIEKiGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF------- 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  866 RTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINN-SHRLLGYCVVKD---IELDEK 941
Cdd:PRK06145  376 RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERITAVVVLNPgatLTLEAL 455
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 490930577  942 TseqlsqqylSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK06145  456 D---------RHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1107-1387 5.07e-19

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: 92.13  E-value: 5.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1107 QKGMLFLSQ-VENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHF--DSELAEepvfiyslhPTQA----WPV 1179
Cdd:cd19532     8 QSRFWFLQQyLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGE---------PMQGvlasSPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTPDLlEQTIQEALQQpIHlDQPYGL-----IRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQqtNQ 1254
Cdd:cd19532    79 RLEHVQISD-EAEVEEEFER-LK-NHVYDLesgetMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN--GQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1255 QLPVLEHSY----ETVIKALSGRDHETSKVIWQRDLADL-QPLILFNQAQQAV---------QETSYRLSAELGAKLQHK 1320
Cdd:cd19532   154 PLLPPPLQYldfaARQRQDYESGALDEDLAYWKSEFSTLpEPLPLLPFAKVKSrppltrydtHTAERRLDAALAARIKEA 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1321 LRQQGIT-LNVFMQMIWAMtLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQT 1387
Cdd:cd19532   234 SRKLRVTpFHFYLAALQVL-LARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQT 298
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
1554-2038 8.37e-19

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: 92.11  E-value: 8.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1554 ENHQLSFSEVRLQVCALAQQLQRA-GVQAGDIVAVALPRSVKLSIAILAVIEAGAAylpidlqhpTERIKFMLQDAkskl 1632
Cdd:cd05937     2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------PAFINYNLSGD---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1633 vigeqkdlaAIVHpsiatfafnelfdetKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVShqaivNRILWMQSEyp 1712
Cdd:cd05937    69 ---------PLIH---------------CLKLSGSRFVIVDPDDPAILIYTSGTTGLPKAAAIS-----WRRTLVTSN-- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1713 LSATDTILQKTPCTFD--------VSVWEFFWSYLVGARLVIAPIDAHRDplaLLSLIQKYQVTTLHFVPSMLAVFENAA 1784
Cdd:cd05937   118 LLSHDLNLKNGDRTYTcmplyhgtAAFLGACNCLMSGGTLALSRKFSASQ---FWKDVRDSGATIIQYVGELCRYLLSTP 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1785 TEILSSAQRqslpiCRVfCSGEALPTALAKSFTEHFSC-ELHNLYGPTE---AAVDVSYMDATLGlhpeescvAIGYPVW 1860
Cdd:cd05937   195 PSPYDRDHK-----VRV-AWGNGLRPDIWERFRERFNVpEIGEFYAATEgvfALTNHNVGDFGAG--------AIGHHGL 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1861 NTQLYILDQYL-------------RP-------VPVGVDGE----LYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMY 1916
Cdd:cd05937   261 IRRWKFENQVVlvkmdpetddpirDPktgfcvrAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYF 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1917 RTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQNK-----ANVQLVAYLQTTAPV 1990
Cdd:cd05937   341 RTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDiAEANVYGVKVPGHDgragcAAITLEESSAVPTEF 420
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 490930577 1991 DIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTP 2038
Cdd:cd05937   421 TKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
1557-2009 8.53e-19

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: 92.03  E-value: 8.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAaylpidlqhPTERIKFMLQdaksklvige 1636
Cdd:cd05940     3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA---------VAALINYNLR---------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 qkdLAAIVHpsiatfafnelfdetKVDLSSYKTTVITPqhpAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSAT 1716
Cdd:cd05940    64 ---GESLAH---------------CLNVSSAKHLVVDA---ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1717 DTILQKTPCTFDVSVWEFFWSYLV-GARLVIAPIDAHRDplaLLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRqs 1795
Cdd:cd05940   123 DVLYTCLPLYHSTALIVGWSACLAsGATLVIRKKFSASN---FWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHK-- 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1796 lpiCRVFCsGEALPTALAKSFTEHFSC-ELHNLYGPTE---AAVDVSYMDATLGLHPEESCVAIGYPV----WNTQLYIL 1867
Cdd:cd05940   198 ---VRMIF-GNGLRPDIWEEFKERFGVpRIAEFYAATEgnsGFINFFGKPGAIGRNPSLLRKVAPLALvkydLESGEPIR 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1868 DQ--YLRPVPVGVDGELYLAGHQLA--MGYLHRADLTASRfVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:cd05940   274 DAegRCIKVPRGEPGLLISRINPLEpfDGYTDPAATEKKI-LRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWK 352
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1944 GQRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAY-LQTTAPVDIDQLKKQLAKHLPAYMVP 2009
Cdd:cd05940   353 GENVSTTEVAAVLGAFPGvEEANVYGVQVPGTDGRAGMAAIvLQPNEEFDLSALAAHLEKNLPGYARP 420
PRK07470 PRK07470
acyl-CoA synthetase; Validated
1534-2031 8.56e-19

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 92.80  E-value: 8.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:PRK07470    9 LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHPTERIKFMLQDAKSKLVIGEQ--KDLAAIVHPSIATFAFNELFDETKVDLS-----------SYKTTVITPQHPAYL 1680
Cdd:PRK07470   89 FRQTPDEVAYLAEASGARAMICHAdfPEHAAAVRAASPDLTHVVAIGGARAGLDyealvarhlgaRVANAAVDHDDPCWF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1681 IYTSGTTGQPKGVMVSHQ----AIVNRILWMqseYP-LSATDTILQKTPCTFDVSVweffwSYLV----GARLVIAPIDA 1751
Cdd:PRK07470  169 FFTSGTTGRPKAAVLTHGqmafVITNHLADL---MPgTTEQDASLVVAPLSHGAGI-----HQLCqvarGAATVLLPSER 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1752 HrDPLALLSLIQKYQVTTLHFVPSMLAVFenaaTEILSSAQRQ--SL--------PICRvfcsgEALPTALAKsftehFS 1821
Cdd:PRK07470  241 F-DPAEVWALVERHRVTNLFTVPTILKML----VEHPAVDRYDhsSLryviyagaPMYR-----ADQKRALAK-----LG 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1822 CELHNLYGPTEAAVDVSYMDATlgLHPEE--------SCvaiGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGY 1893
Cdd:PRK07470  306 KVLVQYFGLGEVTGNITVLPPA--LHDAEdgpdarigTC---GFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGY 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1894 LHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLrlisgldvVVHAISSEQ 1973
Cdd:PRK07470  381 YNNPEANAKAFRDGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKL--------LTHPAVSEV 445
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 1974 NKANVQ---------LVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK07470  446 AVLGVPdpvwgevgvAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
PRK08316 PRK08316
acyl-CoA synthetase; Validated
477-986 1.01e-18

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 92.30  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  477 DIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:PRK08316   15 DILRRSARRYPDKTALVFGDR----SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  557 L-------DLDYPIDrmqmmceDANPLFVLTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDAS-------------DIPA 616
Cdd:PRK08316   91 VnfmltgeELAYILD-------HSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPggwldfadwaeagSVAE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  617 ENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkpTIYWPVLEAvnerfPDRPLraahtHSFS-FDSSWLQVF 695
Cdd:PRK08316  164 PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVS---CIVAGDMSA-----DDIPL-----HALPlYHCAQLDVF 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  696 WM--LW-GQELHIFDenmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMtnglfvenqHHP--------SL--ILIGGEAA 762
Cdd:PRK08316  231 LGpyLYvGATNVILD---APDPELILRTIEAERITSFFAPPTVWISLL---------RHPdfdtrdlsSLrkGYYGASIM 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  763 PLALWQQLNAQ-PALFAHNLYGPTE----YTVdtFRAElKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGF 836
Cdd:PRK08316  299 PVEVLKELRERlPGLRFYNCYGQTEiaplATV--LGPE-EHLRRPgSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSP 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  837 GIANGYLGRADLSAArfvanPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVV 916
Cdd:PRK08316  376 QLMLGYWDDPEKTAE-----AFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAV 448
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577  917 IAEPinnsHRLLGYCVVKDIELdeKTSEQLS-QQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK08316  449 IGLP----DPKWIEAVTAVVVP--KAGATVTeDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
PRK07788 PRK07788
acyl-CoA synthetase; Validated
485-988 1.01e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 92.68  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  485 KYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIaGAIPR-SIDSVVVMLSVLNSGASFLPLDLDYPI 563
Cdd:PRK07788   61 RAPDRAALIDERGT----LTYAELDEQSNALARGLLALGVRAGDGV-AVLARnHRGFVLALYAAGKVGARIILLNTGFSG 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  564 DRMQMMC--EDANPLFV---LTtqALAQQLPQNIQQLH---LDQEGVQTQ----------IRKQDASDIPAEnRKFDFQd 625
Cdd:PRK07788  136 PQLAEVAarEGVKALVYddeFT--DLLSALPPDLGRLRawgGNPDDDEPSgstdetlddlIAGSSTAPLPKP-PKPGGI- 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  626 vayVIFTSGSTGRPKGVMNTHGSLLN---LILSHKPtiyWPVLEAVNerfpdrpLRAAHTHSFSFdsSWLQVFWMLwGQE 702
Cdd:PRK07788  212 ---VILTSGTTGTPKGAPRPEPSPLAplaGLLSRVP---FRAGETTL-------LPAPMFHATGW--AHLTLAMAL-GST 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  703 LhifdeNMRR--DAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPS---LILIGGEAAPLALWQQLNAQ--PA 775
Cdd:PRK07788  276 V-----VLRRrfDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSslkIIFVSGSALSPELATRALEAfgPV 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  776 LfaHNLYGPTEYTVDTF--RAELKQ---TA-RPVIGnpignTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADls 849
Cdd:PRK07788  351 L--YNLYGSTEVAFATIatPEDLAEapgTVgRPPKG-----VTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRD-- 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  850 aarfvaNPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIAEPINNSHRLL 928
Cdd:PRK07788  422 ------KQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVvEAAVIGVDDEEFGQRLR 493
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  929 GYCVVKDIEldEKTSEQLsQQYLsqlRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:PRK07788  494 AFVVKAPGA--ALDEDAI-KDYV---RDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
PRK08162 PRK08162
acyl-CoA synthetase; Validated
1528-1956 1.35e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 92.32  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1528 YVRQSTLQQLLReQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGA 1607
Cdd:PRK08162   15 YVPLTPLSFLER-AAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 AYLPIDLQHPTERIKFMLQDAKSKLVIGEQkDLAAIVHPSIAtfafneLFDETK-----VDLSSYKTT----------VI 1672
Cdd:PRK08162   94 VLNTLNTRLDAASIAFMLRHGEAKVLIVDT-EFAEVAREALA------LLPGPKplvidVDDPEYPGGrfigaldyeaFL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1673 TPQHPAY-------------LIYTSGTTGQPKGVMVSHQ-----AIVNRILWMQSEYPlsatdTILQKTPcTFDVSVWEF 1734
Cdd:PRK08162  167 ASGDPDFawtlpadewdaiaLNYTSGTTGNPKGVVYHHRgaylnALSNILAWGMPKHP-----VYLWTLP-MFHCNGWCF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1735 FWSYLVGA------RLViapidahrDPLALLSLIQKYQVTtlHF-----VPSMLAvfeNAATEILSSAQRQslpiCRVFC 1803
Cdd:PRK08162  241 PWTVAARAgtnvclRKV--------DPKLIFDLIREHGVT--HYcgapiVLSALI---NAPAEWRAGIDHP----VHAMV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1804 SGEALPTA-LAKsfTEHFSCELHNLYGPTEaavdvSYMDATLGL-HPEESCVAIG------------YPVwNTQLYILD- 1868
Cdd:PRK08162  304 AGAAPPAAvIAK--MEEIGFDLTHVYGLTE-----TYGPATVCAwQPEWDALPLDeraqlkarqgvrYPL-QEGVTVLDp 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1869 QYLRPVPvgVD----GELYLAGHQLAMGYLHRADLTASRFvanpftAGQrMYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:PRK08162  376 DTMQPVP--ADgetiGEIMFRGNIVMKGYLKNPKATEEAF------AGG-WFHTGDLAVLHPDGYIKIKDRSKDIIISGG 446
                         490
                  ....*....|..
gi 490930577 1945 QRIELGEIEQQL 1956
Cdd:PRK08162  447 ENISSIEVEDVL 458
PRK09274 PRK09274
peptide synthase; Provisional
1538-1935 1.48e-18

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 91.88  E-value: 1.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1538 LREQARITPEQTALSDENH----------QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGA 1607
Cdd:PRK09274   12 LPRAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 AYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAA----------IVH------------PSIATFafnelfdETKVDLS 1665
Cdd:PRK09274   92 VPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKAHLArrlfgwgkpsVRRlvtvggrllwggTTLATL-------LRDGAAA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1666 SYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILqktpCTFDVSVwefFWSYLVGARLV 1745
Cdd:PRK09274  165 PFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDL----PTFPLFA---LFGPALGMTSV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1746 IAPIDAHR----DPLALLSLIQKYQVTTLhFV-PSMLAVFENAATeilssAQRQSLP-ICRVFCSGEALPTALAKSFTEH 1819
Cdd:PRK09274  238 IPDMDPTRpatvDPAKLFAAIERYGVTNL-FGsPALLERLGRYGE-----ANGIKLPsLRRVISAGAPVPIAVIERFRAM 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1820 FS--CELHNLYGPTEaAVDVSY--MDATLGLHPEES------CVaiGYPVWNTQLYILD---------QYLRPVPVGVDG 1880
Cdd:PRK09274  312 LPpdAEILTPYGATE-ALPISSieSREILFATRAATdngagiCV--GRPVDGVEVRIIAisdapipewDDALRLATGEIG 388
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1881 ELYLAGHQLAMGYLHRADLTASRFVANPftAGQRMYRTGDIARWHADGSIQYIGR 1935
Cdd:PRK09274  389 EIVVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGR 441
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
1541-2031 1.82e-18

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: 92.24  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1541 QARITPEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILA---------VIEA 1605
Cdd:cd05966    62 HLKERGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLAcarigavhsVVFA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1606 G--AAYLpidlqhpTERIkfmlQDAKSKLVI--------GEQKDLAAIVH------PSI----------ATFAFNE---- 1655
Cdd:cd05966   142 GfsAESL-------ADRI----NDAQCKLVItadggyrgGKVIPLKEIVDealekcPSVekvlvvkrtgGEVPMTEgrdl 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1656 LFDETKVDLSSY-KTTVITPQHPAYLIYTSGTTGQPKGVMVSHqaivnrilwmqSEYPLSATDTilQKTpcTFDVSVWEF 1734
Cdd:cd05966   211 WWHDLMAKQSPEcEPEWMDSEDPLFILYTSGSTGKPKGVVHTT-----------GGYLLYAATT--FKY--VFDYHPDDI 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1735 FW-----------SYLV------GARLVI---APidAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQ 1794
Cdd:cd05966   276 YWctadigwitghSYIVygplanGATTVMfegTP--TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLS 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1795 SLpicRVFCS-GEAL-PTALaKSFTEH---FSCELHNLYGPTEAAvdvSYMDATL-GLHPEE--SCvaiGYPVWNTQLYI 1866
Cdd:cd05966   354 SL---RVLGSvGEPInPEAW-MWYYEVigkERCPIVDTWWQTETG---GIMITPLpGATPLKpgSA---TRPFFGIEPAI 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1867 LDQYLRPVPVGVDGelYLAGHQ----LAMGyLHRADltaSRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKI 1942
Cdd:cd05966   424 LDEEGNEVEGEVEG--YLVIKRpwpgMART-IYGDH---ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINV 497
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1943 RGQRIELGEIEQQlrLISGLDV----VV---HAIsseqnKANVqLVAYL-----QTTAPVDIDQLKKQLAKHLPAYMVPT 2010
Cdd:cd05966   498 SGHRLGTAEVESA--LVAHPAVaeaaVVgrpHDI-----KGEA-IYAFVtlkdgEEPSDELRKELRKHVRKEIGPIATPD 569
                         570       580
                  ....*....|....*....|.
gi 490930577 2011 HYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05966   570 KIQFVPGLPKTRSGKIMRRIL 590
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1557-1935 2.01e-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: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 90.98  E-value: 2.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGE 1636
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 QKDLaaivhpsiatfafnelfdetkvdlssykttvitpqHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSAT 1716
Cdd:cd05910    82 PKAD-----------------------------------EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPG 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1717 DTILQKTP--CTFDVsvweffwsyLVGARLVIAPIDAHR----DPLALLSLIQKYQVTTLHFVPSMLAVFENAAteilsS 1790
Cdd:cd05910   127 EVDLATFPlfALFGP---------ALGLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARYC-----A 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1791 AQRQSLP-ICRVFCSGEALPTALAKSFTEHFS--CELHNLYGPTEA----AVDVSYMDATLGLHPEE-SCVAIGYPVWNT 1862
Cdd:cd05910   193 QHGITLPsLRRVLSAGAPVPIALAARLRKMLSdeAEILTPYGATEAlpvsSIGSRELLATTTAATSGgAGTCVGRPIPGV 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1863 QLYILD---------QYLRPVPVGVDGELYLAGHQLAMGYLHRADltASRFVANPFTAGQRMYRTGDIARWHADGSIQYI 1933
Cdd:cd05910   273 RVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPV--ATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFC 350

                  ..
gi 490930577 1934 GR 1935
Cdd:cd05910   351 GR 352
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
475-986 2.35e-18

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: 90.85  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  475 VLDIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQtviagaiprsiDSVVVMLsvlnsgasf 554
Cdd:cd05920    17 LGDLLARSAARHPDRIAVVDGDR----RLTYRELDRRADRLAAGLRGLGIRPG-----------DRVVVQL--------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  555 lPLDLDypidrmqmmcedanplFVLTTQALAQQ-------LPQniqQLHLDQEGVQTQIRKQdASDIPAENRKFDFQ--- 624
Cdd:cd05920    73 -PNVAE----------------FVVLFFALLRLgavpvlaLPS---HRRSELSAFCAHAEAV-AYIVPDRHAGFDHRala 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 --------DVAYVIFTSGSTGRPKGVMNTHGSLLNLI--------LSHKpTIYWPVLEAvnerfpdrplraahTHSFSFD 688
Cdd:cd05920   132 relaesipEVALFLLSGGTTGTPKLIPRTHNDYAYNVrasaevcgLDQD-TVYLAVLPA--------------AHNFPLA 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  689 SSwlQVFWMLWGQELHIFDENMRRD-AFGLvqeIQQRQIDTLDLPPSFcAQMMTNGLFVENQHHPSLILIGGEAAPLAlw 767
Cdd:cd05920   197 CP--GVLGTLLAGGRVVLAPDPSPDaAFPL---IEREGVTVTALVPAL-VSLWLDAAASRRADLSSLRLLQVGGARLS-- 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  768 qqlnAQPALFAHNLYGPTEYTVdtF-RAE--LKQTArpvIGNP---IGNTQAY---------VLDRHLQRCPTGVIGELY 832
Cdd:cd05920   269 ----PALARRVPPVLGCTLQQV--FgMAEglLNYTR---LDDPdevIIHTQGRpmspddeirVVDEEGNPVPPGEEGELL 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  833 ISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVE 912
Cdd:cd05920   340 TRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVH 413
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  913 SAVVIAEPinnsHRLLG-----YCVVKDIELDektseqlsqqyLSQLRQNLPE-----YMVPSALTVMSEFPRNVSGKVD 982
Cdd:cd05920   414 DAAVVAMP----DELLGerscaFVVLRDPPPS-----------AAQLRRFLRErglaaYKLPDRIEFVDSLPLTAVGKID 478

                  ....
gi 490930577  983 KKAL 986
Cdd:cd05920   479 KKAL 482
PRK07514 PRK07514
malonyl-CoA synthase; Validated
487-986 2.73e-18

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 90.71  E-value: 2.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIvsgERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:PRK07514   16 RDAPFI---ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAEL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  567 QMMCEDANP-LFVLTT------QALAQQLP-QNIQQLHLDQEGVQTQIRKQDASDIPAENRKFDfqDVAYVIFTSGSTGR 638
Cdd:PRK07514   93 DYFIGDAEPaLVVCDPanfawlSKIAAAAGaPHVETLDADGTGSLLEAAAAAPDDFETVPRGAD--DLAAILYTSGTTGR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  639 PKGVMNTHGSLL-NLILSHKptiYWpvleavneRF-PDRPLRAA----HTHSFsFDSSWLQVFW---MLWgqeLHIFD-- 707
Cdd:PRK07514  171 SKGAMLSHGNLLsNALTLVD---YW--------RFtPDDVLIHAlpifHTHGL-FVATNVALLAgasMIF---LPKFDpd 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  708 ---ENMRR-DAFGLVQEIQQRQIDTLDLPPSFCAQMMtngLFvenqhhpslilIGGEAAPLA----LWQQLNAQPALfah 779
Cdd:PRK07514  236 avlALMPRaTVMMGVPTFYTRLLQEPRLTREAAAHMR---LF-----------ISGSAPLLAethrEFQERTGHAIL--- 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  780 NLYGPTEYTVDT---FRAElkqtARP-VIGNPIGNTQAYVLDRHL-QRCPTGVIGELYISGFGIANGYLGRADLSAARFV 854
Cdd:PRK07514  299 ERYGMTETNMNTsnpYDGE----RRAgTVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFR 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  855 ANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAvVIAEPinnsHRLLGYCVV 933
Cdd:PRK07514  375 ADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVvESA-VIGVP----HPDFGEGVT 443
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  934 ------KDIELDEKTseqlsqqYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK07514  444 avvvpkPGAALDEAA-------ILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1678-2031 2.84e-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: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 89.08  E-value: 2.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPcTFDV--SVWEFFWSYLVGARLVIAPIDAHRDP 1755
Cdd:cd05944     5 AAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLP-LFHVngSVVTLLTPLASGAHVVLAGPAGYRNP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1756 LA---LLSLIQKYQVTTLHFVPSMLAvfenAATEILSSAQRQSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTE 1832
Cdd:cd05944    84 GLfdnFWKLVERYRITSLSTVPTVYA----ALLQVPVNADISSLRF--AMSGAAPLPVELRARFEDATGLPVVEGYGLTE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1833 A--AVDVSYMDATLGLhpeeSCVAIGYPVWNTQLYILD---QYLRPVPVGVDGELYLAGHQLAMGYLHRADltasrfvAN 1907
Cdd:cd05944   158 AtcLVAVNPPDGPKRP----GSVGLRLPYARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYLYTEG-------NK 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1908 PFTAGQRMYRTGDIARWHADGSIQYIGRADDqLKIR-GQRIELGEIEQQlrLISGLDV-VVHAISSEQNKANVQLVAYLQ 1985
Cdd:cd05944   227 NAFVADGWLNTGDLGRLDADGYLFITGRAKD-LIIRgGHNIDPALIEEA--LLRHPAVaFAGAVGQPDAHAGELPVAYVQ 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 490930577 1986 TT--APVDIDQLKKQLAKHLPAY-MVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05944   304 LKpgAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
475-986 3.85e-18

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 90.88  E-value: 3.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  475 VLDIFYEQVKKYPERTAIVS--GERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGA 552
Cdd:PRK13295   26 INDDLDACVASCPDKTAVTAvrLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  553 SFLPLdldYPIDRMQ----MMCEDANPLFVL-----------TTQALAQQLPQNIQQLHLDQEG------VQTQIRKQDA 611
Cdd:PRK13295  106 VLNPL---MPIFRERelsfMLKHAESKVLVVpktfrgfdhaaMARRLRPELPALRHVVVVGGDGadsfeaLLITPAWEQE 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  612 SDIPA--ENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILshkptiywPVLEAVNERFPDRPLRA---AHTHSFS 686
Cdd:PRK13295  183 PDAPAilARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIV--------PYAERLGLGADDVILMAspmAHQTGFM 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  687 F---------DSSWLQVFWmlwgqelhifdenmrrDAFGLVQEIQQRQID-TLDLPPsFCAQMMTNglfVENQHH--PSL 754
Cdd:PRK13295  255 YglmmpvmlgATAVLQDIW----------------DPARAAELIRTEGVTfTMASTP-FLTDLTRA---VKESGRpvSSL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  755 --ILIGGEAAPLALWQQlnAQPALFAH--NLYGPTE---YTVDTFRAELKQtARPVIGNPIGNTQAYVLDRHLQRCPTGV 827
Cdd:PRK13295  315 rtFLCAGAPIPGALVER--ARAALGAKivSAWGMTEngaVTLTKLDDPDER-ASTTDGCPLPGVEVRVVDADGAPLPAGQ 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  828 IGELYISGFGIANGYLGRADLSAARFvanpfehgQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIRG-YRVEIGEVENALS 906
Cdd:PRK13295  392 IGRLQVRGCSNFGGYLKRPQLNGTDA--------DGWFDTGDLARIDADGYIRISGRSKDVI-IRGgENIPVVEIEALLY 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  907 ILTNVESAVVIAEPinnsHRLLG----YCVV----KDIELDEKT----SEQLSQQYLsqlrqnlpeymvPSALTVMSEFP 974
Cdd:PRK13295  463 RHPAIAQVAIVAYP----DERLGeracAFVVprpgQSLDFEEMVeflkAQKVAKQYI------------PERLVVRDALP 526
                         570
                  ....*....|..
gi 490930577  975 RNVSGKVDKKAL 986
Cdd:PRK13295  527 RTPSGKIQKFRL 538
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
1547-1956 3.90e-18

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 90.72  E-value: 3.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1547 EQTAL----SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIK 1622
Cdd:PRK04319   59 DKVALryldASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1623 FMLQDAKSK-----------------------LVIGEQKDLAAivhpsiATFAFNELFDETKvdlSSYKTTVITPQHPAY 1679
Cdd:PRK04319  139 DRLEDSEAKvlittpallerkpaddlpslkhvLLVGEDVEEGP------GTLDFNALMEQAS---DEFDIEWTDREDGAI 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVMVSHQAIVNRilWMQSEYPLSatdtiLQKTP---CTFDVSvWEFFWSY------LVGARLViapID 1750
Cdd:PRK04319  210 LHYTSGSTGKPKGVLHVHNAMLQH--YQTGKYVLD-----LHEDDvywCTADPG-WVTGTSYgifapwLNGATNV---ID 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1751 AHR-DPLALLSLIQKYQVTTLHFVPSMLAVFENAATEIlssAQRQSLPICRVFCS-GEAL-PTAL--AKsftEHFSCELH 1825
Cdd:PRK04319  279 GGRfSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDL---VKKYDLSSLRHILSvGEPLnPEVVrwGM---KVFGLPIH 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1826 NLYGPTE--AAVDVSY--MDATLGlhpeescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAM--GYLHRADL 1899
Cdd:PRK04319  353 DNWWMTEtgGIMIANYpaMDIKPG--------SMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMmrGIWNNPEK 424
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 1900 TASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL 1956
Cdd:PRK04319  425 YESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKL 474
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
1534-2031 5.93e-18

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 90.09  E-value: 5.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHPTERIKFMLQDAKSKLV------------IGEQKDLAAIVHPSIATF---AFNELFD---------ETKVDLS---- 1665
Cdd:PRK06710  106 PLYTERELEYQLHDSGAKVIlcldlvfprvtnVQSATKIEHVIVTRIADFlpfPKNLLYPfvqkkqsnlVVKVSESetih 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1666 -------SYKTTVITPQHP----AYLIYTSGTTGQPKGVMVSHQAIV-NRILWMQSEYPLSATDTILqktpctfdVSVWE 1733
Cdd:PRK06710  186 lwnsvekEVNTGVEVPCDPendlALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVV--------LGVLP 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1734 FFWSYLVGARLVIAPIDAHR-------DPLALLSLIQKYQVTTLHFVPSMLAVFENAAteILSSAQRQSLPICrvfCSGE 1806
Cdd:PRK06710  258 FFHVYGMTAVMNLSIMQGYKmvlipkfDMKMVFEAIKKHKVTLFPGAPTIYIALLNSP--LLKEYDISSIRAC---ISGS 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1807 A-LPTALAKSFTEHFSCELHNLYGPTEAAvDVSYMDAtlgLHPEESCVAIGYPVWNTQLYILD----QYLRPvpvGVDGE 1881
Cdd:PRK06710  333 ApLPVEVQEKFETVTGGKLVEGYGLTESS-PVTHSNF---LWEKRVPGSIGVPWPDTEAMIMSletgEALPP---GEIGE 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1882 LYLAGHQLAMGYLHRADLTASrfvanpfTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG 1961
Cdd:PRK06710  406 IVVKGPQIMKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEK 478
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1962 L-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06710  479 VqEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
503-988 6.64e-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: 89.11  E-value: 6.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLdldypidrmqmmcedanplFVlttq 582
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPL-------------------FT---- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  583 ALAqqlPQNIQQlHLDQEGVQTQIrkqdasdIPAENR-KFDfQDVAYVIFTSGSTGRPKGV------MNTHGSLLNLILS 655
Cdd:cd05973    58 AFG---PKAIEH-RLRTSGARLVV-------TDAANRhKLD-SDPFVMMFTSGTTGLPKGVpvplraLAAFGAYLRDAVD 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  656 HKP-TIYWPVLE---------AVNErfpdrPLRAAHTH-----SFSFDSSWlqvfwmlwgqelhifdENMRRdaFGlvqe 720
Cdd:cd05973   126 LRPeDSFWNAADpgwayglyyAITG-----PLALGHPTillegGFSVESTW----------------RVIER--LG---- 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  721 iqqrqIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGEAAPLA----LWqqLNAQPALFAHNLYGPTEytVDTFRAEL 796
Cdd:cd05973   179 -----VTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTpeviRW--FDAALGVPIHDHYGQTE--LGMVLANH 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  797 KQTARPV----IGNPIGNTQAYVLDRHLQRCPTGVIGELYI----SGFGIANGYLGRADLSAArfvanpfehgQRMYRTG 868
Cdd:cd05973   250 HALEHPVhagsAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdianSPLMWFRGYQLPDTPAID----------GGYYLTG 319
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  869 DLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVkdIELDEKTSEQLSQ 948
Cdd:cd05973   320 DTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVV--LRGGHEGTPALAD 397
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 490930577  949 QYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:cd05973   398 ELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
625-983 9.21e-18

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: 86.69  E-value: 9.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYwpvLEAVNERFPDRPLraAHTHSFSfdsSWLQVFWMlwGQELH 704
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFN---ISGEDAILAPGPL--SHSLFLY---GAISALYL--GGTFI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  705 IfdenMRR-DAFGLVQEIQQRQIDTLDLPPSfcaqmMTNGLFVENQHHPSL--ILIGGEAAPLALWQQLNAQ-PALFAHN 780
Cdd:cd17633    71 G----QRKfNPKSWIRKINQYNATVIYLVPT-----MLQALARTLEPESKIksIFSSGQKLFESTKKKLKNIfPKANLIE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  781 LYGPTEYTVDTFRAElkQTARPV--IGNPIGNTQAYVLDRHlqrcpTGVIGELYISGFGIANGYLGRADLSAARFvanpf 858
Cdd:cd17633   142 FYGTSELSFITYNFN--QESRPPnsVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW----- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  859 ehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIEL 938
Cdd:cd17633   210 ------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP----DARFGEIAVALYSG 279
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 490930577  939 DEKTSEQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:cd17633   280 DKLTYKQL----KRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
489-986 9.41e-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: 88.69  E-value: 9.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  489 RTAIVSGERpnlqHLSFAELAVKVNQLTRFLQ-ENGARKQTVIAGAIPRSIDSVVVMLSVLNSGA------SFL-PLDLD 560
Cdd:cd05958     1 RTCLRSPER----EWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAiavatmPLLrPKELA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  561 YPIDRmqmmcedANPLFVLTTQALAqqlpqniqqlhldqegvqtqirkqdASDipaenrkfdfqDVAYVIFTSGSTGRPK 640
Cdd:cd05958    77 YILDK-------ARITVALCAHALT-------------------------ASD-----------DICILAFTSGTTGAPK 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  641 GVMNTHGSLLnlilshkptiywpvleAVNERFPDRPLRAAHTH--------SFSFDSSWLQVFWMLWGQELHIFDENMRR 712
Cdd:cd05958   114 ATMHFHRDPL----------------ASADRYAVNVLRLREDDrfvgspplAFTFGLGGVLLFPFGVGASGVLLEEATPD 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  713 DAFGLVQEiqQRQIDTLDLPPSFCAqmMTNGLFVENQHHPSLILI--GGEAAPLALWQQLNAQPALFAHNLYGPTEyTVD 790
Cdd:cd05958   178 LLLSAIAR--YKPTVLFTAPTAYRA--MLAHPDAAGPDLSSLRKCvsAGEALPAALHRAWKEATGIPIIDGIGSTE-MFH 252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  791 TFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGfgiANGYLGRADLSAARFVANPFEHgqrmyrTGD 869
Cdd:cd05958   253 IFISARPGDARPgATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQGGWNI------TGD 323
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  870 LVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNshRLL---GYCVVKDielDEKTSEQL 946
Cdd:cd05958   324 TYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDES--RGVvvkAFVVLRP---GVIPGPVL 398
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 490930577  947 SQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05958   399 ARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
PRK08308 PRK08308
acyl-CoA synthetase; Validated
1562-2032 1.02e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 88.17  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1562 EVRLQVCALAQQLQRAgvqAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVigeqkdla 1641
Cdd:PRK08308   15 DLRLQRYEEMEQFQEA---AGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGL-------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1642 aivhpsiatfafneLFDETKVDLSSYKTTviTPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQ 1721
Cdd:PRK08308   84 --------------LYGESDFTKLEAVNY--LAEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1722 KTPCTFdvsvweffwSY------LVGARLVIAP-IDAHRDPLALLSLIQKYQVTTLHFVPSMLavfenaatEILSSAQRQ 1794
Cdd:PRK08308  148 ACPVTH---------SYglicgvLAALTRGSKPvIITNKNPKFALNILRNTPQHILYAVPLML--------HILGRLLPG 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1795 SLPICRVFCSGEALPTALAKSFTEHfSCELHNLYGPTEAAvdvsymdatlglhpeesCVAIGYPVwntqlyildqylrpv 1874
Cdd:PRK08308  211 TFQFHAVMTSGTPLPEAWFYKLRER-TTYMMQQYGCSEAG-----------------CVSICPDM--------------- 257
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1875 pvgvdgelylAGHqLAMGY-LHRADLTASRFVANP----FTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIEL 1949
Cdd:PRK08308  258 ----------KSH-LDLGNpLPHVSVSAGSDENAPeeivVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYP 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1950 GEIEQQLRLISGL-DVVV----HAISSEQNKAnvQLVAylqtTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNG 2024
Cdd:PRK08308  327 IEVEDVMLRLPGVqEAVVyrgkDPVAGERVKA--KVIS----HEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANG 400

                  ....*...
gi 490930577 2025 KLDRKALP 2032
Cdd:PRK08308  401 KVSRKLLE 408
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
1680-2028 1.18e-17

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: 86.55  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPcTFDVSVWEF-FWSYLVGARLVIAPidaHRDPLAL 1758
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLP-LFHIAGLNLaLATFHAGGANVVME---KFDPAEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1759 LSLIQKYQVTTLHFVPSMLAVFENAATEilSSAQRQSLPICrvfcSGEALPtALAKSFTEHFSCELHNLYGPTEAAVDVS 1838
Cdd:cd17637    81 LELIEEEKVTLMGSFPPILSNLLDAAEK--SGVDLSSLRHV----LGLDAP-ETIQRFEETTGATFWSLYGQTETSGLVT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1839 YMDAtlglhpEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFvanpftagqR--MY 1916
Cdd:cd17637   154 LSPY------RERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---------RngWH 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1917 RTGDIARWHADGSIQYIGR--ADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDID 1993
Cdd:cd17637   219 HTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIaEVCVIGVPDPKWGEGIKAVCVLKPGATLTAD 298
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 490930577 1994 QLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:cd17637   299 ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
475-1003 1.19e-17

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 89.04  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  475 VLDIFYEQVKKYPERTAIVS--GERpnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGA 552
Cdd:PRK06087   25 LADYWQQTARAMPDKIAVVDnhGAS-----YTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  553 SFLPL-------DLDYPIDRMQ---MMCED--ANPLFVLTTQALAQQLPQNIQQLHLDQEGVQT------QIRKQD---A 611
Cdd:PRK06087  100 VSVPLlpswreaELVWVLNKCQakmFFAPTlfKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATsslslsQIIADYeplT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  612 SDIPAenrkfDFQDVAYVIFTSGSTGRPKGVMNTHGsllNLILSHKPtiYWPVLEAvnerfpdrplraahthsfsfdsSW 691
Cdd:PRK06087  180 TAITT-----HGDELAAVLFTSGTEGLPKGVMLTHN---NILASERA--YCARLNL----------------------TW 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  692 LQVFWM------------------LWGQE---LHIFdenmrRDAFGLVQEIQQRQIDTLDLPPsFCAQMMTNglfVENQH 750
Cdd:PRK06087  228 QDVFMMpaplghatgflhgvtapfLIGARsvlLDIF-----TPDACLALLEQQRCTCMLGATP-FIYDLLNL---LEKQP 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  751 H--PSL--ILIGGEAAPLALWQQLNAQPALFAhNLYGPTEYTVDTFRAELKQTARPVI--GNPIGNTQAYVLDRHLQRCP 824
Cdd:PRK06087  299 AdlSALrfFLCGGTTIPKKVARECQQRGIKLL-SVYGSTESSPHAVVNLDDPLSRFMHtdGYAAAGVEIKVVDEARKTLP 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  825 TGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDqIKIRG-YRVEIGEVEN 903
Cdd:PRK06087  378 PGCEGEEASRGPNVFMGYLDEPELTARALDEEGW------YYSGDLCRMDEAGYIKITGRKKD-IIVRGgENISSREVED 450
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  904 ALSILTNVESAVVIAEPINN-SHRLLGYCVVKDIELDEKTSEQLSqqYLSqlRQNLPEYMVPSALTVMSEFPRNVSGKVD 982
Cdd:PRK06087  451 ILLQHPKIHDACVVAMPDERlGERSCAYVVLKAPHHSLTLEEVVA--FFS--RKRVAKYKYPEHIVVIDKLPRTASGKIQ 526
                         570       580
                  ....*....|....*....|.
gi 490930577  983 KKALPKPQIRAHSRMAETPEQ 1003
Cdd:PRK06087  527 KFLLRKDIMRRLTQDVCEEIE 547
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
21-265 1.33e-17

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 84.71  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   21 LASTQLGIFladHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELNNQVQFQIEEFDF 100
Cdd:COG4908     1 LSPAQKRFL---FLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  101 CHLTPKKAQQRLWDWMPSDRQcaKSLKAGETQLFRQVLF-TTHDKVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQEGK 179
Cdd:COG4908    78 SALPEPEREAELEELVAEEAS--RPFDLARGPLLRAALIrLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  180 DLSVSPF-IGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLST-HHLAAKTTATFVKHQLRFSTGILEQIQALA 257
Cdd:COG4908   156 PPPLPELpIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTdRPRPAVQTFRGATLSFTLPAELTEALKALA 235

                  ....*...
gi 490930577  258 AQTKLALN 265
Cdd:COG4908   236 KAHGATVN 243
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
625-982 1.35e-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: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 87.05  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHG----SLLNLILSHKP---TIYWPVLEAVNE----RFPDRPLraahTHSfsfDSSWLQ 693
Cdd:cd05924     4 DDLYILYTGGTTGMPKGVMWRQEdifrMLMGGADFGTGeftPSEDAHKAAAAAagtvMFPAPPL----MHG---TGSWTA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  694 VFWMLWGQELHIFDEnmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHH-PSLILIGGEAAPLALW---QQ 769
Cdd:cd05924    77 FGGLLGGQTVVLPDD--RFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDlSSLFAISSGGALLSPEvkqGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  770 LNAQPALFAHNLYGPTE-----YTVDTFRAELKQTARPVignpigNTQAYVLDRHLQRCPTGVIGELYISGFG-IANGYL 843
Cdd:cd05924   155 LELVPNITLVDAFGSSEtgftgSGHSAGSGPETGPFTRA------NPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYY 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  844 GRADLSAARFvanPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinn 923
Cdd:cd05924   229 GDEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRP--- 302
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  924 SHRlLGYCVVKDIELDEKTSEQLsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVD 982
Cdd:cd05924   303 DER-WGQEVVAVVQLREGAGVDL-EELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
487-986 1.44e-17

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: 88.72  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGERpnlQH-LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPL-------D 558
Cdd:cd05923    15 PDACAIADPAR---GLrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALInprlkaaE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  559 LDYPIDRMQM----MCEDANPlfvltTQALAQQLpqnIQQLHLDQEgVQTQIRKQDASDIPAenRKFDFQDVAYVIFTSG 634
Cdd:cd05923    92 LAELIERGEMtaavIAVDAQV-----MDAIFQSG---VRVLALSDL-VGLGEPESAGPLIED--PPREPEQPAFVFYTSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  635 STGRPKGV-------------MNTHGSLL----NLILSHKPtIYWPVleavnerfpdrPLRAAHTHSFSFDSSWLQVfwm 697
Cdd:cd05923   161 TTGLPKGAvipqraaesrvlfMSTQAGLRhgrhNVVLGLMP-LYHVI-----------GFFAVLVAALALDGTYVVV--- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  698 lwgqelhifDENMRRDAFGLvqeIQQRQIDTLDLPPSFCAQMMTNGLF----VENQHHpslILIGGEAAPLALWQQLN-A 772
Cdd:cd05923   226 ---------EEFDPADALKL---IEQERVTSLFATPTHLDALAAAAEFaglkLSSLRH---VTFAGATMPDAVLERVNqH 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  773 QPALFAhNLYGPTEYTVDTFRAELKQTARpviGNPIGNTQ---AYVLDRHLQRCPTGVIGELYISGFGIA--NGYLGRAD 847
Cdd:cd05923   291 LPGEKV-NIYGTTEAMNSLYMRDARTGTE---MRPGFFSEvriVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPE 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  848 LSAARFVanpfehgQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRL 927
Cdd:cd05923   367 ATAKKLQ-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQS 439
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  928 LGYCVVkdIELDEKTSEQLSQQYLSqlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05923   440 VTACVV--PREGTLSADELDQFCRA---SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
1101-1380 2.56e-17

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: 87.09  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRH-------PQLGGhfdselaeEPV-FIysL 1171
Cdd:cd19540     2 IPLSFAQQRLWFLNRLDGPSAaYNIPLALRLTGALDVDALRAALADVVARHeslrtvfPEDDG--------GPYqVV--L 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1172 HPTQAWP-VQFCSVTPDLLEQTIQEALQQPIHL--DQPyglIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKA 1248
Cdd:cd19540    72 PAAEARPdLTVVDVTEDELAARLAEAARRGFDLtaELP---LRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1249 Y----QQTNQQLPVLEHSYetvikA--------LSGRDHETSKVI------WQRDLADL-QPLIL-FNQAQQAVQetSYR 1308
Cdd:cd19540   149 YaarrAGRAPDWAPLPVQY-----AdyalwqreLLGDEDDPDSLAarqlayWRETLAGLpEELELpTDRPRPAVA--SYR 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1309 -------LSAELGAKLQHKLRQQGITLnvFM--QMIWAMTLniyaHR----EDIVFGTPVSGRSAPinGLEQQIGLFLNT 1375
Cdd:cd19540   222 ggtveftIDAELHARLAALAREHGATL--FMvlHAALAVLL----SRlgagDDIPIGTPVAGRGDE--ALDDLVGMFVNT 293

                  ....*
gi 490930577 1376 IPVRV 1380
Cdd:cd19540   294 LVLRT 298
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1530-2031 4.22e-17

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 87.42  E-value: 4.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRA-GVQAGDIVAVALPRSVKLSIAILAVIEAGAA 1608
Cdd:PRK08974   21 RYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1609 -------YLPIDLQHpterikfMLQDAKSKlvigeqkdlaAIVhpSIATFA--FNELFDETKVD----------LSSYKT 1669
Cdd:PRK08974  101 vvnvnplYTPRELEH-------QLNDSGAK----------AIV--IVSNFAhtLEKVVFKTPVKhviltrmgdqLSTAKG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1670 TV---------------------------------------ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSE 1710
Cdd:PRK08974  162 TLvnfvvkyikrlvpkyhlpdaisfrsalhkgrrmqyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1711 Y-PLSATDTILQKTPC----TFDVSVWEFFWSYLVGARLVIA-PidahRDPLALLSLIQKYQVTTLHFVPSMLavfeNAa 1784
Cdd:PRK08974  242 YgPLLHPGKELVVTALplyhIFALTVNCLLFIELGGQNLLITnP----RDIPGFVKELKKYPFTAITGVNTLF----NA- 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1785 teILSSAQRQSLPICRVFCS---GEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEescvAIGYPVWN 1861
Cdd:PRK08974  313 --LLNNEEFQELDFSSLKLSvggGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSG----SIGLPVPS 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1862 TQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASrFVANPFTAgqrmyrTGDIARWHADGSIQYIGRADDQLK 1941
Cdd:PRK08974  387 TEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGWLA------TGDIAVMDEEGFLRIVDRKKDMIL 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1942 IRGQRIELGEIEQQLRLISG-LDVVV----HAISSEQNKANVqlvayLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVE 2016
Cdd:PRK08974  460 VSGFNVYPNEIEDVVMLHPKvLEVAAvgvpSEVSGEAVKIFV-----VKKDPSLTEEELITHCRRHLTGYKVPKLVEFRD 534
                         570
                  ....*....|....*
gi 490930577 2017 QFPLSHNGKLDRKAL 2031
Cdd:PRK08974  535 ELPKSNVGKILRREL 549
PRK13382 PRK13382
bile acid CoA ligase;
779-989 4.39e-17

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 87.12  E-value: 4.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  779 HNLYGPTEY------TVDTFRAELKQTARPVIGnpignTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADlsaar 852
Cdd:PRK13382  341 YNNYNATEAgmiataTPADLRAAPDTAGRPAEG-----TEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGST----- 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  853 fvaNPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIAEPINNSHRLLGYC 931
Cdd:PRK13382  411 ---KDFHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVaEAAVIGVDDEQYGQRLAAFV 485
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577  932 VVKDIEldEKTSEQLSQQylsqLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:PRK13382  486 VLKPGA--SATPETLKQH----VRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK05850 PRK05850
acyl-CoA synthetase; Validated
1532-1998 4.45e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 87.31  E-value: 4.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARITPEQTALS---------DENHQLSFSEVRLQVCALAQQLQRAGVqAGDIVAVALPRSVKLSIAILAV 1602
Cdd:PRK05850    1 SSVPSLLRERASLQPDDAAFTfidyeqdpaGVAETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1603 IEAGAAYLPIDLQHP---TERIKFMLQDAKSKLVIGEQKDLAAIV-----HPSIATFAFNELfDetKVDLSSYKTTVITP 1674
Cdd:PRK05850   80 LQAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLTTSAVVDDVTeyvapQPGQSAPPVIEV-D--LLDLDSPRGSDARP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1675 Q-HP--AYLIYTSGTTGQPKGVMVSHQ-AIVNRILWMQSEYPlsATDTILqkTPCTFDVSvWEFFW---SYLVGarlVIA 1747
Cdd:PRK05850  157 RdLPstAYLQYTSGSTRTPAGVMVSHRnVIANFEQLMSDYFG--DTGGVP--PPDTTVVS-WLPFYhdmGLVLG---VCA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1748 PIDAHRdPLALLS---LIQKyqvttlhfvPS----MLA----VFE---NAATEIlsSAQRQS--------LPICRVFCSG 1805
Cdd:PRK05850  229 PILGGC-PAVLTSpvaFLQR---------PArwmqLLAsnphAFSaapNFAFEL--AVRKTSdddmagldLGGVLGIISG 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1806 -EALPTALAKSFTEHFSceLHNL--------YGPTEAAVDVSymDATLGLHPE--------------ESCVA------IG 1856
Cdd:PRK05850  297 sERVHPATLKRFADRFA--PFNLretairpsYGLAEATVYVA--TREPGQPPEsvrfdyeklsaghaKRCETgggtplVS 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1857 YPV-WNTQLYILD-QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVA-----NPFTAGQRMYRTGDIARWHaDGS 1929
Cdd:PRK05850  373 YGSpRSPTVRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGAtlvdpSPGTPEGPWLRTGDLGFIS-EGE 451
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVvhAISSEQNKANvQLVAylqttapvdIDQLKKQ 1998
Cdd:PRK05850  452 LFIVGRIKDLLIVDGRNHYPDDIEATIQEITGGRVA--AISVPDDGTE-KLVA---------IIELKKR 508
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
1532-2036 6.81e-17

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 86.76  E-value: 6.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARI----------TPEQTALSDENHQLSFSEVRLQVCALAQQLQRA-GVQAGDIVAVALPRSVKLSIAIL 1600
Cdd:PRK05620    3 STMQDVPLSLTRIleygstvhgdTTVTTWGGAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1601 AVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQK--------------------------DLAAIVHPS-IATFAF 1653
Cdd:PRK05620   83 AVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRlaeqlgeilkecpcvravvfigpsdaDSAAAHMPEgIKVYSY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1654 NELFDETKVDlssYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHqaivnRILWMQSeYPLSATDTILQKTPCTFDVSV-- 1731
Cdd:PRK05620  163 EALLDGRSTV---YDWPELDETTAAAICYSTGTTGAPKGVVYSH-----RSLYLQS-LSLRTTDSLAVTHGESFLCCVpi 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1732 -----WEF-FWSYLVGARLVIAPIDAhrDPLALLSLIQKYQVTTLHFVPS-----MLAVFENaateilsSAQRQSLPicR 1800
Cdd:PRK05620  234 yhvlsWGVpLAAFMSGTPLVFPGPDL--SAPTLAKIIATAMPRVAHGVPTlwiqlMVHYLKN-------PPERMSLQ--E 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1801 VFCSGEALPTALAKSFTEHFSCELHNLYGPTEAavdvsymdATLGL--HPeESCVAiGYPVWNtqlYILDQYLRPVPV-- 1876
Cdd:PRK05620  303 IYVGGSAVPPILIKAWEERYGVDVVHVWGMTET--------SPVGTvaRP-PSGVS-GEARWA---YRVSQGRFPASLey 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1877 ----------GVD---GELYLAGHQLAMGYLH----RADLTASRFVANPFTAGQRMY------RTGDIARWHADGSIQYI 1933
Cdd:PRK05620  370 rivndgqvmeSTDrneGEIQVRGNWVTASYYHspteEGGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIH 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1934 GRADDQLKIRGQRIELGEIEQqlrLISGLDVVVHA--ISSEQNK------ANVQLVAYLQTTAPVdIDQLKKQLAKHLPA 2005
Cdd:PRK05620  450 DRARDVIRSGGEWIYSAQLEN---YIMAAPEVVECavIGYPDDKwgerplAVTVLAPGIEPTRET-AERLRDQLRDRLPN 525
                         570       580       590
                  ....*....|....*....|....*....|.
gi 490930577 2006 YMVPTHYMLVEQFPLSHNGKLDRKALPQpHL 2036
Cdd:PRK05620  526 WMLPEYWTFVDEIDKTSVGKFDKKDLRQ-HL 555
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
487-986 1.10e-16

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 85.68  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQ-ENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDR 565
Cdd:PRK06839   16 PDRIAIITEE----EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  566 MQMMCEDANplfvlTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDASDIpaENRKFD-----FQDVAYVI-FTSGSTGRP 639
Cdd:PRK06839   92 LIFQLKDSG-----TTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEI--EDRKIDnfvekNESASFIIcYTSGTTGKP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  640 KG-VMNTHGSLLNLILShkptiywpvLEAVNERFPDR-----PL-RAAHTHSFSFDSswlqvfwMLWGQELHIFDenmRR 712
Cdd:PRK06839  165 KGaVLTQENMFWNALNN---------TFAIDLTMHDRsivllPLfHIGGIGLFAFPT-------LFAGGVIIVPR---KF 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  713 DAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVE-NQHHPSLILIGGEAAPLALWQQLNAQPALFAHNlYGPTEYTVDT 791
Cdd:PRK06839  226 EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETtNLQSVRWFYNGGAPCPEELMREFIDRGFLFGQG-FGMTETSPTV 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  792 FRAELKQTARPV--IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAarfvaNPFEHGqrMYRTGD 869
Cdd:PRK06839  305 FMLSEEDARRKVgsIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATE-----ETIQDG--WLCTGD 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  870 LVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYcVVKDIELDEKTSEQLSQQ 949
Cdd:PRK06839  378 LARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQ----HVKWGE-IPIAFIVKKSSSVLIEKD 452
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 490930577  950 YLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK06839  453 VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
1541-2026 1.53e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 85.45  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1541 QARITPEQTAL--SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPT 1618
Cdd:PRK13390    6 HAQIAPDRPAVivAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1619 ERIKFMLQDAKSKLVIGEQ--KDLAAIV-HPSIATFAFNELFDetkvDLSSYKTTVITPQHP-------AYLIYTSGTTG 1688
Cdd:PRK13390   86 PEADYIVGDSGARVLVASAalDGLAAKVgADLPLRLSFGGEID----GFGSFEAALAGAGPRlteqpcgAVMLYSSGTTG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1689 QPKGVmvshqaivnrilwmQSEYPLSATDT----ILQKTPCTFDVSVWEFFWS----------------YLVGARLVIAp 1748
Cdd:PRK13390  162 FPKGI--------------QPDLPGRDVDApgdpIVAIARAFYDISESDIYYSsapiyhaaplrwcsmvHALGGTVVLA- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 idAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSsaqRQSLPICR-VFCSGEALPTALAKSFTEHFSCELHNL 1827
Cdd:PRK13390  227 --KRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRT---RYDVSSLRaVIHAAAPCPVDVKHAMIDWLGPIVYEY 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1828 YGPTEAAvDVSYMDATLGL-HPEescvAIGYPVWNTqLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTA-SRFV 1905
Cdd:PRK13390  302 YSSTEAH-GMTFIDSPDWLaHPG----SVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAaAQHP 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1906 ANPFTAgqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISS----EQNKANVQL 1980
Cdd:PRK13390  376 AHPFWT-----TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVhDVAVIGVPDpemgEQVKAVIQL 450
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 490930577 1981 VAYLQTTapvdiDQLKKQLAKHLPA----YMVPTHYMLVEQFPLSHNGKL 2026
Cdd:PRK13390  451 VEGIRGS-----DELARELIDYTRSriahYKAPRSVEFVDELPRTPTGKL 495
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
625-983 1.75e-16

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: 83.32  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiyWPVLEAVNErfPDRPLRA-AHTHSFSFDSSWLQVfwMLWGQEL 703
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAA------WADCADLTE--DDRYLIInPFFHTFGYKAGIVAC--LLTGATV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  704 H---IFDenmrrdAFGLVQEIQQRQIDTLDLPPSfcaqmmtngLFVENQHHPSL----------ILIGGEAAPLALWQQL 770
Cdd:cd17638    71 VpvaVFD------VDAILEAIERERITVLPGPPT---------LFQSLLDHPGRkkfdlsslraAVTGAATVPVELVRRM 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  771 NAQ-PALFAHNLYGPTEYTVDTF--RAELKQTARPVIGNPIGNTQAYVLDRhlqrcptgviGELYISGFGIANGYLGRAD 847
Cdd:cd17638   136 RSElGFETVLTAYGLTEAGVATMcrPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPE 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  848 LSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRL 927
Cdd:cd17638   206 ATAEAIDADGWLH------TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEV 279
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577  928 LGYCVV--KDIELDEktseqlsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:cd17638   280 GKAFVVarPGVTLTE-------EDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
PRK05691 PRK05691
peptide synthase; Validated
1532-2134 4.78e-16

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 85.61  E-value: 4.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARITPEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGvQAGDIVAVALPRSVKLSIAILAVIEA 1605
Cdd:PRK05691    9 LTLVQALQRRAAQTPDRLALrfladdPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1606 GA----AYLPIDL-QHPTERIKFMLQDAKSKLVI---GEQKDLAAIVHPSIAtfAFNELFDETKVDLS---SYKTTVITP 1674
Cdd:PRK05691   88 GViavpAYPPESArRHHQERLLSIIADAEPRLLLtvaDLRDSLLQMEELAAA--NAPELLCVDTLDPAlaeAWQEPALQP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1675 QHPAYLIYTSGTTGQPKGVMVSHQAIV-NRILWMQS-EYPLSATDTILQKTPCTFDVSvweffwsyLVGARL-------- 1744
Cdd:PRK05691  166 DDIAFLQYTSGSTALPKGVQVSHGNLVaNEQLIRHGfGIDLNPDDVIVSWLPLYHDMG--------LIGGLLqpifsgvp 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1745 --VIAPIDAHRDPLALLSLIQKYQvTTLHFVPSMlaVFENAATEILSSA-QRQSLPICRVFCSG-EALPTALAKSFTEHF 1820
Cdd:PRK05691  238 cvLMSPAYFLERPLRWLEAISEYG-GTISGGPDF--AYRLCSERVSESAlERLDLSRWRVAYSGsEPIRQDSLERFAEKF 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1821 S-C-----ELHNLYGPTEAAVDVS-------------YMDATLGLHPEE-------SCvaiGYPVWNTQLYILD-QYLRP 1873
Cdd:PRK05691  315 AaCgfdpdSFFASYGLAEATLFVSggrrgqgipalelDAEALARNRAEPgtgsvlmSC---GRSQPGHAVLIVDpQSLEV 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1874 VPVGVDGELYLAGHQLAMGYLHRADLTASRFVANpftAGQRMYRTGDIArWHADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:PRK05691  392 LGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH---DGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1954 QQLRliSGLDVV----VHAISSEQNKAN-----VQLVAYLQTTAPVD--IDQLKKQLAKhlpAYM-VPTHYMLVE--QFP 2019
Cdd:PRK05691  468 KTVE--REVEVVrkgrVAAFAVNHQGEEgigiaAEISRSVQKILPPQalIKSIRQAVAE---ACQeAPSVVLLLNpgALP 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2020 LSHNGKLDRKALPQPH---------LTPSNTEKQYATSA-----FEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVM 2085
Cdd:PRK05691  543 KTSSGKLQRSACRLRLadgsldsyaLFPALQAVEAAQTAasgdeLQARIAAIWCEQLKVEQ-VAADDHFFLLGGNSIAAT 621
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 490930577 2086 KLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQERLAEVEQTGMQPI 2134
Cdd:PRK05691  622 QVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAQAAIARL 670
PRK09088 PRK09088
acyl-CoA synthetase; Validated
482-986 6.08e-16

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 83.32  E-value: 6.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  482 QVKKYPERTA---IVSGERpnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLD 558
Cdd:PRK09088    4 HARLQPQRLAavdLALGRR-----WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  559 LDYPIDRMQMMCEDANPLFVLTTQALAQQLPQNiqqlhLDQEGVQTQIrkqDASDiPAENRKFDFQDVAYVIFTSGSTGR 638
Cdd:PRK09088   79 WRLSASELDALLQDAEPRLLLGDDAVAAGRTDV-----EDLAAFIASA---DALE-PADTPSIPPERVSLILFTSGTSGQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  639 PKGVMNTHGSLLNLilshkptiywpvleAVNerFpDRPLRAAHTHSFSFDSSWLQVFWMLwgqelhifdENMR------- 711
Cdd:PRK09088  150 PKGVMLSERNLQQT--------------AHN--F-GVLGRVDAHSSFLCDAPMFHIIGLI---------TSVRpvlavgg 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  712 ----RDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLfvenQHHPSL----------ILIGG--EAAPLALWQQLNAQPA 775
Cdd:PRK09088  204 silvSNGFEPKRTLGRLGDPALGITHYFCVPQMAQAF----RAQPGFdaaalrhltaLFTGGapHAAEDILGWLDDGIPM 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  776 LFAhnlYGPTE------YTVDTFRAELKQTArpvIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLS 849
Cdd:PRK09088  280 VDG---FGMSEagtvfgMSVDCDVIRAKAGA---AGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQAT 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  850 AARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVV-IAEPINNShrl 927
Cdd:PRK09088  354 ARAFTGDGW------FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIrECAVVgMADAQWGE--- 424
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  928 LGYCVVKDIELDEKTSEQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK09088  425 VGYLAIVPADGAPLDLERI----RSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
455-986 6.34e-16

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 83.78  E-value: 6.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  455 TALTQSGIGPRVShpeqynnvlDIFYEQVKKYPERTA-IVSGERPNLqhlSFAELAVKVNQLTRFLQENGARKQTVIAGA 533
Cdd:PRK05852    7 AAPMASDFGPRIA---------DLVEVAATRLPEAPAlVVTADRIAI---SYRDLARLVDDLAGQLTRSGLLPGDRVALR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  534 IPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVL--------TTQALAQQLPQNIQQLHLDQEGVQTQ 605
Cdd:PRK05852   75 MGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLidadgphdRAEPTTRWWPLTVNVGGDSGPSGGTL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  606 IRKQDASDIPAENRKFDF---QDVAYVIFTSGSTGRPKGVMNTHGsllNLILSHKPTIYWPVLEAVNERFPDRPLraAHT 682
Cdd:PRK05852  155 SVHLDAATEPTPATSTPEglrPDDAMIMFTGGTTGLPKMVPWTHA---NIASSVRAIITGYRLSPRDATVAVMPL--YHG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  683 HSF-----SFDSSWLQVFWMLWGQ-ELHIFDENMRRDA---FGLVQEIQQRQIDTLDLPPSfcaqmmtnglfveNQHHPS 753
Cdd:PRK05852  230 HGLiaallATLASGGAVLLPARGRfSAHTFWDDIKAVGatwYTAVPTIHQILLERAATEPS-------------GRKPAA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  754 LILIGGEAAPL------ALWQQLNAqPALFAhnlYGPTEYT--VDTFRAE-LKQTARPVIGN-PIGNT---QAYVLDRHL 820
Cdd:PRK05852  297 LRFIRSCSAPLtaetaqALQTEFAA-PVVCA---FGMTEAThqVTTTQIEgIGQTENPVVSTgLVGRStgaQIRIVGSDG 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  821 QRCPTGVIGELYISGFGIANGYLGRADLSAARFVanpfeHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGE 900
Cdd:PRK05852  373 LPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-----DG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPER 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  901 VENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIeLDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGK 980
Cdd:PRK05852  446 VEGVLASHPNVMEAAVFGVP----DQLYGEAVAAVI-VPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGS 520

                  ....*.
gi 490930577  981 VDKKAL 986
Cdd:PRK05852  521 LDRRAV 526
PRK07638 PRK07638
acyl-CoA synthetase; Validated
481-988 1.15e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 82.52  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  481 EQVKKY----PERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENgARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:PRK07638    5 KEYKKHaslqPNKIAIKENDR----VLTYKDWFESVCKVANWLNEK-ESKNKTIAILLENRIEFLQLFAGAAMAGWTCVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  557 LDLDYPIDRMQMMCEDANPLFVLTTQALAQQLP-QNIQQLHLDQEGVQTQIRKQD-ASDIPAENRKFdfqdvaYVIFTSG 634
Cdd:PRK07638   80 LDIKWKQDELKERLAISNADMIVTERYKLNDLPdEEGRVIEIDEWKRMIEKYLPTyAPIENVQNAPF------YMGFTSG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  635 STGRPKGVMNTHGSLLNlilSHKPTIywpvlEAVNERFPDRPLRAA---HTHsFSFDSswlqVFWMLWGQELHIfdenMR 711
Cdd:PRK07638  154 STGKPKAFLRAQQSWLH---SFDCNV-----HDFHMKREDSVLIAGtlvHSL-FLYGA----ISTLYVGQTVHL----MR 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  712 R-DAFGLVQEIQQRQIDTLDLPPSfcaqmMTNGLFVENQ--HHPSLILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEY 787
Cdd:PRK07638  217 KfIPNQVLDKLETENISVMYTVPT-----MLESLYKENRviENKMKIISSGAKWEAEAKEKIKNIfPYAKLYEFYGASEL 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  788 TVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLsaarfvanPFEHGQRMYR 866
Cdd:PRK07638  292 SFVTALVDEESERRPnSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVL--------ARELNADGWM 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  867 TGDLVRW-NSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIEldektSEQ 945
Cdd:PRK07638  364 TVRDVGYeDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVP----DSYWGEKPVAIIK-----GSA 434
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 490930577  946 LSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:PRK07638  435 TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
477-986 1.26e-15

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: 82.50  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  477 DIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARK-QTVIAgAIPRSIDSVVVMLSVLNSGAsfL 555
Cdd:COG1021    29 DLLRRRAERHPDRIAVVDGER----RLSYAELDRRADRLAAGLLALGLRPgDRVVV-QLPNVAEFVIVFFALFRAGA--I 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  556 PL---------DLDYPIDRMQ---MMCEDANPLFvlTTQALAQQLPQNIQQL-HL----DQEGVQ--TQIRKQDASDIPA 616
Cdd:COG1021   102 PVfalpahrraEISHFAEQSEavaYIIPDRHRGF--DYRALARELQAEVPSLrHVlvvgDAGEFTslDALLAAPADLSEP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  617 ENrkfDFQDVAYVIFTSGSTGRPKGVMNTHGS-LLNLILS------HKPTIYWPVLEAVnerfpdrplraahtHSFSFdS 689
Cdd:COG1021   180 RP---DPDDVAFFQLSGGTTGLPKLIPRTHDDyLYSVRASaeicglDADTVYLAALPAA--------------HNFPL-S 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  690 S--WLQVFW------MLwgqelhifdENMRRD-AFGLvqeIQQRQIDTLDLPPSFcAQMMTNglFVENQHH--PSL--IL 756
Cdd:COG1021   242 SpgVLGVLYaggtvvLA---------PDPSPDtAFPL---IERERVTVTALVPPL-ALLWLD--AAERSRYdlSSLrvLQ 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  757 IGGeaAPLAlwQQLNAQ--PAL--FAHNLYGPTE----YTvdtfraelkqtaRPviGNP---IGNTQAY---------VL 816
Cdd:COG1021   307 VGG--AKLS--PELARRvrPALgcTLQQVFGMAEglvnYT------------RL--DDPeevILTTQGRpispddevrIV 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  817 DRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIkIRGyrv 896
Cdd:COG1021   369 DEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG--- 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  897 eiGE------VENALSILTNVESAVVIAEPinnsHRLLG-----YCVVKDIELdekTSEQLsQQYLSQlrQNLPEYMVPS 965
Cdd:COG1021   439 --GEkiaaeeVENLLLAHPAVHDAAVVAMP----DEYLGerscaFVVPRGEPL---TLAEL-RRFLRE--RGLAAFKLPD 506
                         570       580
                  ....*....|....*....|.
gi 490930577  966 ALTVMSEFPRNVSGKVDKKAL 986
Cdd:COG1021   507 RLEFVDALPLTAVGKIDKKAL 527
PRK06188 PRK06188
acyl-CoA synthetase; Validated
483-920 1.39e-15

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 82.34  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  483 VKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPL----- 557
Cdd:PRK06188   22 LKRYPDRPALVLGDT----RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALhplgs 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  558 --DLDYPID--RMQMMCEDANPlFVLTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDASDIPAENRKFDF-QDVAYVIFT 632
Cdd:PRK06188   98 ldDHAYVLEdaGISTLIVDPAP-FVERALALLARVPSLKHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALpPDIAGLAYT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  633 SGSTGRPKGVMNTHGSLLNLILSHKPTIYWPvleaVNERFpdrpLRAAhthSFSFDSSWLQVFWMLWGQELHI---FDEn 709
Cdd:PRK06188  177 GGTTGKPKGVMGTHRSIATMAQIQLAEWEWP----ADPRF----LMCT---PLSHAGGAFFLPTLLRGGTVIVlakFDP- 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  710 mrrDAFglVQEIQQRQIDTLDLPPSfcaqmMTNGLFvenQHHPS---------LILIGGEA-APLALWQQLNAQPALFAH 779
Cdd:PRK06188  245 ---AEV--LRAIEEQRITATFLVPT-----MIYALL---DHPDLrtrdlssleTVYYGASPmSPVRLAEAIERFGPIFAQ 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  780 nLYGPTE--YTVDTFRAELKQTARPVI----GNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARF 853
Cdd:PRK06188  312 -YYGQTEapMVITYLRKRDHDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF 390
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577  854 vANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:PRK06188  391 -RDGWLH------TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVP 450
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
1683-2003 1.40e-15

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 81.73  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1683 TSGTTGQPKGVMVSHQAI------VNRILWMQseyPLSATDTILqktpCTFDVSVWEFFWSYLVGAR----LVIaPIDAh 1752
Cdd:COG1541    91 SSGTTGKPTVVGYTRKDLdrwaelFARSLRAA---GVRPGDRVQ----NAFGYGLFTGGLGLHYGAErlgaTVI-PAGG- 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1753 RDPLALLSLIQKYQVTTLHFVPSMLAVfenaateILSSAQRQ-----SLPICRVFCSGEALPTALAKSFTEHFSCELHNL 1827
Cdd:COG1541   162 GNTERQLRLMQDFGPTVLVGTPSYLLY-------LAEVAEEEgidprDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDI 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1828 YGPTEAAVDVSYMDATL-GLHpeescvaigypVWNTQLY--ILD-QYLRPVPVGVDGELYlaghqlamgylhradltasr 1903
Cdd:COG1541   235 YGLTEVGPGVAYECEAQdGLH-----------IWEDHFLveIIDpETGEPVPEGEEGELV-------------------- 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1904 fvanpFTAGQRM------YRTGDIARWHADGS--------IQYI-GRADDQLKIRGQRIELGEIEQQLRLISGLD----V 1964
Cdd:COG1541   284 -----VTTLTKEamplirYRTGDLTRLLPEPCpcgrthprIGRIlGRADDMLIIRGVNVFPSQIEEVLLRIPEVGpeyqI 358
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 490930577 1965 VVhaissEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHL 2003
Cdd:COG1541   359 VV-----DREGGLDELTVRVELAPGASLEALAEAIAAAL 392
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
561-986 2.05e-15

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 82.04  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  561 YPIDRmQMMCEDANPL---FVLTTQALAQQLPQNIQQLhLDQEGVQTQIRKQDASDipaenrkfdfqDVAYVIFTSGSTG 637
Cdd:PRK08008  120 YPMYR-QIQQEDATPLrhiCLTRVALPADDGVSSFTQL-KAQQPATLCYAPPLSTD-----------DTAEILFTSGTTS 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  638 RPKGVMNTHGSLL----------NLilsHKPTIYWPVLEAVNERFPDRPLRAAhthsFSFDSSWLQV-------FWmlwg 700
Cdd:PRK08008  187 RPKGVVITHYNLRfagyysawqcAL---RDDDVYLTVMPAFHIDCQCTAAMAA----FSAGATFVLLekysaraFW---- 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  701 qelhifdenmrrdafglvqeiqqRQIDTLDLPPSFCAQMMTNGLFV------ENQHHPSLILIG---GEAAPLALWQQLN 771
Cdd:PRK08008  256 -----------------------GQVCKYRATITECIPMMIRTLMVqppsanDRQHCLREVMFYlnlSDQEKDAFEERFG 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  772 AQpaLFahNLYGPTEYTVDTFRAELKQTAR-PVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGF---GIANGYLGRAD 847
Cdd:PRK08008  313 VR--LL--TSYGMTETIVGIIGDRPGDKRRwPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPK 388
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  848 LSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAepinnshrl 927
Cdd:PRK08008  389 ATAKVLEADGWLH------TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVG--------- 453
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577  928 lgycvVKDIELDE--------KTSEQLSQ-QYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK08008  454 -----IKDSIRDEaikafvvlNEGETLSEeEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK07798 PRK07798
acyl-CoA synthetase; Validated
474-982 2.06e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 81.86  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  474 NVLDIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGAS 553
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDR----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  554 FLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQlpqnIQQLHLDQEGVQTQIRKQDASDIPAENRKFDFQDVA------ 627
Cdd:PRK07798   80 PVNVNYRYVEDELRYLLDDSDAVALVYEREFAPR----VAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALaagspe 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  628 -----------YVIFTSGSTGRPKGVMNTHGSL-------LNLILSHKPTIYWPVLEAVNE-----RFPDRPLRAAHTHS 684
Cdd:PRK07798  156 rdfgerspddlYLLYTGGTTGMPKGVMWRQEDIfrvllggRDFATGEPIEDEEELAKRAAAgpgmrRFPAPPLMHGAGQW 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  685 FSFDSswlqvfwMLWGQELhIFDENMRRDAFGLVQEIQQRQ---------------IDTLDLPPSFCAqmmtnglfvenq 749
Cdd:PRK07798  236 AAFAA-------LFSGQTV-VLLPDVRFDADEVWRTIEREKvnvitivgdamarplLDALEARGPYDL------------ 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  750 hhPSLILIGGEAAPL--ALWQQLNAQ-PALFAHNLYGPTE----YTVDTFRAELKqTARPVIgNPIGNTQayVLDRHLQR 822
Cdd:PRK07798  296 --SSLFAIASGGALFspSVKEALLELlPNVVLTDSIGSSEtgfgGSGTVAKGAVH-TGGPRF-TIGPRTV--VLDEDGNP 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  823 CPTG--VIGELYISGFgIANGYLGRADLSAARF-VANpfehGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIG 899
Cdd:PRK07798  370 VEPGsgEIGWIARRGH-IPLGYYKDPEKTAETFpTID----GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPE 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  900 EVENALSILTNVESAVVIAEPinnSHRlLGYCVVKDIELDEKTSEQLsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSG 979
Cdd:PRK07798  445 EVEEALKAHPDVADALVVGVP---DER-WGQEVVAVVQLREGARPDL-AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAG 519

                  ...
gi 490930577  980 KVD 982
Cdd:PRK07798  520 KAD 522
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
21-437 4.84e-15

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: 79.80  E-value: 4.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   21 LASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIEL-NNQVQFQIEEFD 99
Cdd:cd19536     4 LSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVvHRQAQVPVTELD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  100 FCHLTPKKAQQRLWdwmpSDRQCAKSLKAGETQLFRQVLF--TTHDKVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQE 177
Cdd:cd19536    84 LTPLEEQLDPLRAY----KEETKIRRFDLGRAPLVRAALVrkDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  178 GKDLSVSPFIGVNEVISERQAYENSHQfkiDQAFWKAYCEDLPSPislSTHHLAAKTTATFVKH-QLRFSTGILEQIQAL 256
Cdd:cd19536   160 YKPLSLPPAQPYRDFVAHERASIQQAA---SERYWREYLAGATLA---TLPALSEAVGGGPEQDsELLVSVPLPVRSRSL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  257 AAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRL-GSKAIRSTL-PTVNVLPVKFKVAEkDSWVSLAQHVQEQLR 334
Cdd:cd19536   234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSeETTGAERLLgLFLNTLPLRVTLSE-ETVEDLLKRAQEQEL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  335 EIRPHQKYDaeqiLRDLNSIDIHERMYGPILNYKAFDQD----LVIDGEKVKTH--HISTGPIDDFEFSFIVQDHELIIE 408
Cdd:cd19536   313 ESLSHEQVP----LADIQRCSEGEPLFDSIVNFRHFDLDfglpEWGSDEGMRRGllFSEFKSNYDVNLSVLPKQDRLELK 388
                         410       420
                  ....*....|....*....|....*....
gi 490930577  409 LRADSQRYTQDELfnhgQRLTLLLEQALI 437
Cdd:cd19536   389 LAYNSQVLDEEQA----QRLAAYYKSAIA 413
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
799-1075 5.71e-15

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 77.87  E-value: 5.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  799 TARPVIGNPIGNTQAY-VLDRHLQRCPTGVIGElYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAG 877
Cdd:COG3433    13 PDEPPPVIPPAIVQARaLLLIVDLQGYFGGFGG-EGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  878 KLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAE--PINNSHRLLGYCVVKDIELDEKTSEQLSQQYLsqlr 955
Cdd:COG3433    92 GLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLaaLRGAGVGLLLIVGAVAALDGLAAAAALAALDK---- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  956 qnLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQIRAHSRMAETPE--------QQLLCQITASVLKL--DAIGIDDDF 1025
Cdd:COG3433   168 --VPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPApaletaltEEELRADVAELLGVdpEEIDPDDNL 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 490930577 1026 FMTGGDSISAIMLCTQLRQRGYSLRPSDVFQFKTVAAMAPQLTRLDEQQA 1075
Cdd:COG3433   246 FDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
484-981 6.87e-15

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 80.39  E-value: 6.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  484 KKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQ-ENGARK------------QTVIAG-AIPRSiDSVVVMLSVLN 549
Cdd:PRK08314   21 RRYPDKTAIVFYGR----AISYRELLEEAERLAGYLQqECGVRKgdrvllymqnspQFVIAYyAILRA-NAVVVPVNPMN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  550 sgasfLPLDLDYPIdrmqmmcEDANPLFVLTTQALAQQLPQNIQQLHLDQ-------------------EGVQTQIRKQD 610
Cdd:PRK08314   96 -----REEELAHYV-------TDSGARVAIVGSELAPKVAPAVGNLRLRHvivaqysdylpaepeiavpAWLRAEPPLQA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  611 -------------ASDIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkpTIYW------PVLEAVNER 671
Cdd:PRK08314  164 lapggvvawkealAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVG---SVLWsnstpeSVVLAVLPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  672 FpdrplraahtHSFSFDSSWLQVFWMlwGQELHI---FDenmrRDAFGlvQEIQQRQIDTLDLPPSFCAQMMTNGLFvEN 748
Cdd:PRK08314  241 F----------HVTGMVHSMNAPIYA--GATVVLmprWD----REAAA--RLIERYRVTHWTNIPTMVVDFLASPGL-AE 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  749 QHHPSLILIGGEAAPL--ALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQAYVLD-RHLQRCPT 825
Cdd:PRK08314  302 RDLSSLRYIGGGGAAMpeAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPP 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  826 GVIGELYISGFGIANGYLGRADLSAARFVAnpFEhGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENAL 905
Cdd:PRK08314  382 GEVGEIVVHGPQVFKGYWNRPEATAEAFIE--ID-GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLL 458
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  906 SILTNVESAVVIAEPinNSHR---LLGYCVVKDiELDEKTSEqlsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKV 981
Cdd:PRK08314  459 YKHPAIQEACVIATP--DPRRgetVKAVVVLRP-EARGKTTE---EEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
1553-1967 7.65e-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: 79.95  E-value: 7.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1553 DENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGaayLPIDLQHPTerikfmlqdakskl 1632
Cdd:cd17639     1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAT-------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1633 vIGEqkdlAAIVHPsiatfafnelFDETKVdlssykTTVIT---PQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQS 1709
Cdd:cd17639    64 -LGE----DALIHS----------LNETEC------SAIFTdgkPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGD 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1710 EYP--LSATDTILQKTPCT----FDVSVWEFFWsylvGARLviapidAHRDPLALLSLIQK--------YQVTTLHFVPs 1775
Cdd:cd17639   123 RVPelLGPDDRYLAYLPLAhifeLAAENVCLYR----GGTI------GYGSPRTLTDKSKRgckgdlteFKPTLMVGVP- 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 mlAVFENAATEILS-----SAQRQSL------------------PIC----------------RVFCSGEALPTALAKSF 1816
Cdd:cd17639   192 --AIWDTIRKGVLAklnpmGGLKRTLfwtayqsklkalkegpgtPLLdelvfkkvraalggrlRYMLSGGAPLSADTQEF 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1817 TEHFSCELHNLYGPTE---AAVDVSYMDATLGlhpeescvAIGYPVWNTQLYILD------QYLRPVPvgvDGELYLAGH 1887
Cdd:cd17639   270 LNIVLCPVIQGYGLTEtcaGGTVQDPGDLETG--------RVGPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGP 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1888 QLAMGYLHRADLTASRFvanpftAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR-GQRIELGEIEQQLR---LISGLD 1963
Cdd:cd17639   339 NVFKGYYKNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRsnpLVNNIC 412

                  ....
gi 490930577 1964 VVVH 1967
Cdd:cd17639   413 VYAD 416
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
485-987 1.25e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 79.27  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  485 KYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPID 564
Cdd:PRK13383   47 RWPGRTAIIDDDGA----LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSD 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  565 RMQMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDASDIPAENRkfdfqdvaYVIFTSGSTGRPKGVMN 644
Cdd:PRK13383  123 ALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGR--------IVLLTSGTTGKPKGVPR 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  645 THGsllnliLSHKPTIYWPVLEAVNERFPDR-PLRAAHTHSFSFDSSWLQVfwMLWGQEL---HiFDENM--------RR 712
Cdd:PRK13383  195 APQ------LRSAVGVWVTILDRTRLRTGSRiSVAMPMFHGLGLGMLMLTI--ALGGTVLthrH-FDAEAalaqaslhRA 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  713 DAFGLVQEIQQRqidTLDLPPSFCAQmmtNGLfvenqhhPSL--ILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVD 790
Cdd:PRK13383  266 DAFTAVPVVLAR---ILELPPRVRAR---NPL-------PQLrvVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIG 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  791 TFR--AELKQtARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGradlSAARFVANPfehgqrMYRTG 868
Cdd:PRK13383  333 ALAtpADLRD-APETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD----GGGKAVVDG------MTSTG 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  869 DLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINN-SHRLLGYCVVK---DIELDektse 944
Cdd:PRK13383  402 DMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERfGHRLAAFVVLHpgsGVDAA----- 476
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 490930577  945 qlsqQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:PRK13383  477 ----QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1558-1956 1.29e-14

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: 78.76  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 kdlaaivhpsiATFAfnelfdetkvdlssykttvitpQHPAYLIYTSGTTGQPKGVMVSHQAivnrilwmqseYPLSATD 1717
Cdd:cd05974    81 -----------NTHA----------------------DDPMLLYFTSGTTSKPKLVEHTHRS-----------YPVGHLS 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 TI----LQKTPCTFDVS-------VWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaate 1786
Cdd:cd05974   117 TMywigLKPGDVHWNISspgwakhAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRML------ 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1787 ILSSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVsymdatlGLHPEESCVA--IGYPVWNTQL 1864
Cdd:cd05974   191 IQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALV-------GNSPGQPVKAgsMGRPLPGYRV 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YILDQYLRPVPvgvDGELYL---AGHQLAM--GYLHRADLTASrfvanpfTAGQRMYRTGDIARWHADGSIQYIGRADDQ 1939
Cdd:cd05974   264 ALLDPDGAPAT---EGEVALdlgDTRPVGLmkGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDV 333
                         410
                  ....*....|....*..
gi 490930577 1940 LKIRGQRIELGEIEQQL 1956
Cdd:cd05974   334 FKSSDYRISPFELESVL 350
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
470-986 2.05e-14

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 78.77  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  470 EQYNNVLDIFYEQVKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFL-QENGARKQTVIAGAIPRSIDSVVVMLSVL 548
Cdd:PRK08751   22 EQFRTVAEVFATSVAKFADRPAYHSFGKT----ITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  549 -----------------------NSGASFLPLdLDYPIDRMQMMCEDANPLFVLTTQ----------ALAQQLPQNIQQL 595
Cdd:PRK08751   98 ragltvvnvnplytprelkhqliDSGASVLVV-IDNFGTTVQQVIADTPVKQVITTGlgdmlgfpkaALVNFVVKYVKKL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  596 HLDQEgVQTQIRKQDASDIPAENR----KFDFQDVAYVIFTSGSTGRPKGVMNTHGSLL-NLILSHKPTIYWPVLEAVNE 670
Cdd:PRK08751  177 VPEYR-INGAIRFREALALGRKHSmptlQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVaNMQQAHQWLAGTGKLEEGCE 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  671 R-FPDRPLraahTHSFSFDSSWLqVFwMLWGQELHIFDENmrRDAFGLVQEIQQRQidtldlppsFCAQMMTNGLFVENQ 749
Cdd:PRK08751  256 VvITALPL----YHIFALTANGL-VF-MKIGGCNHLISNP--RDMPGFVKELKKTR---------FTAFTGVNTLFNGLL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  750 HHP----------SLILIGGEAAPLAL---WQQLNAQPALFAhnlYGPTEYTVDTFRAELK-QTARPVIGNPIGNTQAYV 815
Cdd:PRK08751  319 NTPgfdqidfsslKMTLGGGMAVQRSVaerWKQVTGLTLVEA---YGLTETSPAACINPLTlKEYNGSIGLPIPSTDACI 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  816 LDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYR 895
Cdd:PRK08751  396 KDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLH------TGDIARMDEQGFVYIVDRKKDMILVSGFN 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  896 VEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVV-KDIELdekTSEQLSqqylSQLRQNLPEYMVPSALTVMSEFP 974
Cdd:PRK08751  470 VYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVkKDPAL---TAEDVK----AHARANLTGYKQPRIIEFRKELP 542
                         570
                  ....*....|..
gi 490930577  975 RNVSGKVDKKAL 986
Cdd:PRK08751  543 KTNVGKILRREL 554
PLN03102 PLN03102
acyl-activating enzyme; Provisional
1537-2031 2.22e-14

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 78.91  E-value: 2.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:PLN03102   19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEqKDLAAIV--------------HPSI--------ATFAFNELFD--------ETKVDLSS 1666
Cdd:PLN03102   99 DATSIAAILRHAKPKILFVD-RSFEPLArevlhllssedsnlNLPVifiheidfPKRPSSEELDyecliqrgEPTPSLVA 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1667 YKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQ-----AIVNRILWMQSEYPLsatdtILQKTPcTFDVSVWEFFWSylVG 1741
Cdd:PLN03102  178 RMFRIQDEHDPISLNYTSGTTADPKGVVISHRgaylsTLSAIIGWEMGTCPV-----YLWTLP-MFHCNGWTFTWG--TA 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1742 ARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSaqrQSLPIcRVFCSGEALPTALAKSfTEHFS 1821
Cdd:PLN03102  250 ARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSP---RSGPV-HVLTGGSPPPAALVKK-VQRLG 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1822 CELHNLYGPTEAAVDV---SYMDATLGLhPEESCVAIGYPVWNTQLYILD------QYLRPVPVG--VDGELYLAGHQLA 1890
Cdd:PLN03102  325 FQVMHAYGLTEATGPVlfcEWQDEWNRL-PENQQMELKARQGVSILGLADvdvknkETQESVPRDgkTMGEIVIKGSSIM 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1891 MGYLHRADLTASRFvanpftaGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLR-----LISGLDVV 1965
Cdd:PLN03102  404 KGYLKNPKATSEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYkypkvLETAVVAM 476
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1966 VHAISSEQNKANVQLVAYlQTTAPVDIDQL---KKQLAKH----LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PLN03102  477 PHPTWGETPCAFVVLEKG-ETTKEDRVDKLvtrERDLIEYcrenLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
PRK07514 PRK07514
malonyl-CoA synthase; Validated
1570-2035 2.32e-14

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 78.38  E-value: 2.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAI-----V 1644
Cdd:PRK07514   41 LANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLskiaaA 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1645 HPSIATFAFNE-----LFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTI 1719
Cdd:PRK07514  121 AGAPHVETLDAdgtgsLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1720 LQKTP------------CTFdvsvweffwsyLVGARLVIAPidaHRDPLALLSLIQkyQVTTLHFVPSMLavfenaaTEI 1787
Cdd:PRK07514  201 IHALPifhthglfvatnVAL-----------LAGASMIFLP---KFDPDAVLALMP--RATVMMGVPTFY-------TRL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1788 LSSAQ--RQSLPICRVFCSGEAlPTaLAKSFTEHFSCELHNL---YGPTEAAVDVSymdatlglHP---EESCVAIGYPV 1859
Cdd:PRK07514  258 LQEPRltREAAAHMRLFISGSA-PL-LAETHREFQERTGHAIlerYGMTETNMNTS--------NPydgERRAGTVGFPL 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1860 WNTQLYILDQYL-RPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADD 1938
Cdd:PRK07514  328 PGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERGYVHIVGRGKD 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1939 qLKIRGqrielG------EIEQqlrLISGLDVVV--------HAISSEQnkanVQLVAYLQTTAPVD----IDQLKKQLA 2000
Cdd:PRK07514  402 -LIISG-----GynvypkEVEG---EIDELPGVVesavigvpHPDFGEG----VTAVVVPKPGAALDeaaiLAALKGRLA 468
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 490930577 2001 KhlpaYMVPTHYMLVEQFPLSHNGKLDRKALPQPH 2035
Cdd:PRK07514  469 R----FKQPKRVFFVDELPRNTMGKVQKNLLREQY 499
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
1556-1953 2.48e-14

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


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 78.59  E-value: 2.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1556 HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQ-HPtERIKFMLQDAKSKLVI 1634
Cdd:PRK07008   38 HRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRlFP-EQIAYIVNHAEDRYVL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1635 GEQKDLAAI--VHPSIATF-AFNELFDETK-----VDLSSYKTtVITPQHPAY------------LIYTSGTTGQPKGVM 1694
Cdd:PRK07008  117 FDLTFLPLVdaLAPQCPNVkGWVAMTDAAHlpagsTPLLCYET-LVGAQDGDYdwprfdenqassLCYTSGTTGNPKGAL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVnrILWMQSEYP----LSATDTILQKTPcTFDVSVWEFFWSY-LVGARLVI-APidaHRDPLALLSLIQKYQVT 1768
Cdd:PRK07008  196 YSHRSTV--LHAYGAALPdamgLSARDAVLPVVP-MFHVNAWGLPYSApLTGAKLVLpGP---DLDGKSLYELIEAERVT 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1769 TLHFVPS---MLAVFENAATEILSSAQrqslpicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAA---VDVSYMDA 1842
Cdd:PRK07008  270 FSAGVPTvwlGLLNHMREAGLRFSTLR-------RTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSplgTLCKLKWK 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1843 TLGLhPEESCVAI----GYPVWNTQLYILDQYLRPVPV-GVD-GELYLAGHQLAMGYLhRADltasrfvANPFTAGqrMY 1916
Cdd:PRK07008  343 HSQL-PLDEQRKLlekqGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYF-RGD-------ASPLVDG--WF 411
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 490930577 1917 RTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:PRK07008  412 PTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIE 448
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
624-988 2.66e-14

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: 78.28  E-value: 2.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  624 QDVAYVIFTSGSTGRPKGVMNTHGSL-LNLILSHKptiYWpvleavnerfpdRPLRAAHTHSFSFDSSWLQVFWML---- 698
Cdd:cd05928   174 QEPMAIYFTSGTTGSPKMAEHSHSSLgLGLKVNGR---YW------------LDLTASDIMWNTSDTGWIKSAWSSlfep 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  699 WGQELHIFDENMRR-DAFGLVQEIQQRQIDTLDLPPS----FCAQMMTNGLFVENQHhpslILIGGEAAPLALWQQLNAQ 773
Cdd:cd05928   239 WIQGACVFVHHLPRfDPLVILKTLSSYPITTFCGAPTvyrmLVQQDLSSYKFPSLQH----CVTGGEPLNPEVLEKWKAQ 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  774 PALFAHNLYGPTEyTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYIS-----GFGIANGYLGRAD 847
Cdd:cd05928   315 TGLDIYEGYGQTE-TGLICANFKGMKIKPgSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPE 393
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  848 LSAARFVANpfehgqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIA-EPINNsh 925
Cdd:cd05928   394 KTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVvESAVVSSpDPIRG-- 464
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577  926 RLLGYCVVKDIELDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:cd05928   465 EVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
PRK06178 PRK06178
acyl-CoA synthetase; Validated
487-986 2.82e-14

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 78.54  E-value: 2.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIV-SGerpnlQHLSFAELAvkvNQLTRF---LQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDldyP 562
Cdd:PRK06178   47 PQRPAIIfYG-----HVITYAELD---ELSDRFaalLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS---P 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  563 IDR-MQMMCE--DANPLFVLTTQALAQ-----------------------------QLPQNIQQLHLDQEGVQTQIRKQD 610
Cdd:PRK06178  116 LFReHELSYElnDAGAEVLLALDQLAPvveqvraetslrhvivtsladvlpaeptlPLPDSLRAPRLAAAGAIDLLPALR 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  611 ASDIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiYWPVleAVNERFPDRPLraahthsfsfdsS 690
Cdd:PRK06178  196 ACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAA-----AYAV--AVVGGEDSVFL------------S 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  691 WLQVFWmlwgqelhIFDENM----------------RRDAFGLVQEIQQRQIDTLdlppsfcaqMMTNGLFVENQHHP-- 752
Cdd:PRK06178  257 FLPEFW--------IAGENFgllfplfsgatlvllaRWDAVAFMAAVERYRVTRT---------VMLVDNAVELMDHPrf 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  753 ------SLILIGGEAAPLAL-------WQQLNAqpALFAHNLYGPTE-YTVDTFRAELkQT------ARPV-IGNPIGNT 811
Cdd:PRK06178  320 aeydlsSLRQVRVVSFVKKLnpdyrqrWRALTG--SVLAEAAWGMTEtHTCDTFTAGF-QDddfdllSQPVfVGLPVPGT 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  812 QAYVLDRHLQR-CPTGVIGELYISGFGIANGYLGRADLSAARFVANpfehgqrMYRTGDLVRWNSAGKLEFMGRCDDQIK 890
Cdd:PRK06178  397 EFKICDFETGElLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLK 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  891 IRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIELdeKTSEQLSQQYLSQ-LRQNLPEYMVPSaLTV 969
Cdd:PRK06178  470 VNGMSVFPSEVEALLGQHPAVLGSAVVGRP----DPDKGQVPVAFVQL--KPGADLTAAALQAwCRENMAVYKVPE-IRI 542
                         570
                  ....*....|....*..
gi 490930577  970 MSEFPRNVSGKVDKKAL 986
Cdd:PRK06178  543 VDALPMTATGKVRKQDL 559
PRK09192 PRK09192
fatty acyl-AMP ligase;
1557-2048 2.86e-14

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 78.51  E-value: 2.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLqhPT---------ERIKFMLQD 1627
Cdd:PRK09192   49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPL--PMgfggresyiAQLRGMLAS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1628 AKSKLVIG--EQKD-LAAIVHPSIATFAF-NELFD---ETKVDLSsykttVITPQHPAYLIYTSGTTGQPKGVMVSHQAI 1700
Cdd:PRK09192  127 AQPAAIITpdELLPwVNEATHGNPLLHVLsHAWFKalpEADVALP-----RPTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRilwmqseypLSA-TDTILQKTPCTFDVSvWEFFwsY----LVGarLVIAPI------------DAHRDPLALLSLIQ 1763
Cdd:PRK09192  202 MAN---------LRAiSHDGLKVRPGDRCVS-WLPF--YhdmgLVG--FLLTPVatqlsvdylptrDFARRPLQWLDLIS 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQvTTLHFVPSMlaVFENAATEIlSSAQRQSLPICR---VFCSGEALPTALAKSFTEHFS-----------CelhnlYG 1829
Cdd:PRK09192  268 RNR-GTISYSPPF--GYELCARRV-NSKDLAELDLSCwrvAGIGADMIRPDVLHQFAEAFApagfddkafmpS-----YG 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1830 PTEAAVDVSYMDATLGLHPEE-----------------------SCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAG 1886
Cdd:PRK09192  339 LAEATLAVSFSPLGSGIVVEEvdrdrleyqgkavapgaetrrvrTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRG 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1887 HQLAMGYLHRADLTASRFVANpftagqrMYRTGDIArWHADGSIQYIGRADDQLKIRGQRIELGEIE----QQLRLISGl 1962
Cdd:PRK09192  419 PSLMSGYFRDEESQDVLAADG-------WLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEwiaeQEPELRSG- 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1963 DVVVHAISSEQNKANVQLVaYLQTTAPVDIDQLKKQLAKHLPAY--------MVPTHYMlveqfPLSHNGKLDRKALPQP 2034
Cdd:PRK09192  490 DAAAFSIAQENGEKIVLLV-QCRISDEERRGQLIHALAALVRSEfgveaaveLVPPHSL-----PRTSSGKLSRAKAKKR 563
                         570
                  ....*....|....
gi 490930577 2035 HLTPSNTEKQYATS 2048
Cdd:PRK09192  564 YLSGAFASLDVAAS 577
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
578-988 2.96e-14

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: 78.09  E-value: 2.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  578 VLTTQALAQQL-PQNIQQLHLDQEGVQTQIRKQDASDIPAENRKFDfqDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSh 656
Cdd:cd05906   122 VLTDAELVAEFaGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPD--DLALLMLTSGSTGFPKAVPLTHRNILARSAG- 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  657 kptiywpvLEAVNERFPDR------PLRAA----HTHSFSFDsswlqvfwmLWGQELHIFDENMRRDAFGLVQEIQQRQI 726
Cdd:cd05906   199 --------KIQHNGLTPQDvflnwvPLDHVgglvELHLRAVY---------LGCQQVHVPTEEILADPLRWLDLIDRYRV 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  727 dTLDLPPSFCAQMMTNGLFVENQHHPSL-----ILIGGEA-------APLALWQQLNAQPALFaHNLYGPTE------YT 788
Cdd:cd05906   262 -TITWAPNFAFALLNDLLEEIEDGTWDLsslryLVNAGEAvvaktirRLLRLLEPYGLPPDAI-RPAFGMTEtcsgviYS 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  789 VDTFRAELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRT 867
Cdd:cd05906   340 RSFPTYDHSQALEFVsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRT 413
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  868 GDLVrWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAepinNSHRLLG-----YCV--VKDIELDE 940
Cdd:cd05906   414 GDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAA----FAVRDPGaeteeLAIffVPEYDLQD 488
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 490930577  941 KTSEQLS--QQYLSQLRQNLPEYMVPSAltvMSEFPRNVSGKVDKKALPK 988
Cdd:cd05906   489 ALSETLRaiRSVVSREVGVSPAYLIPLP---KEEIPKTSLGKIQRSKLKA 535
PLN02654 PLN02654
acetate-CoA ligase
1557-2031 3.45e-14

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 78.40  E-value: 3.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVI-- 1634
Cdd:PLN02654  120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVItc 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1635 -GEQKDLAAIVHPSIATFAFNELFDE-TKVDL-----------------------------SSYKTTV----ITPQHPAY 1679
Cdd:PLN02654  200 nAVKRGPKTINLKDIVDAALDESAKNgVSVGIcltyenqlamkredtkwqegrdvwwqdvvPNYPTKCevewVDAEDPLF 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVM-VSHQAIVNRILWMQSEYPLSATDTILqktpCTFDVSvWEFFWSY------LVGARLVI---APi 1749
Cdd:PLN02654  280 LLYTSGSTGKPKGVLhTTGGYMVYTATTFKYAFDYKPTDVYW----CTADCG-WITGHSYvtygpmLNGATVLVfegAP- 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1750 dAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLpicRVFCS-GEAL-PTALAKSF--TEHFSCELH 1825
Cdd:PLN02654  354 -NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSL---RVLGSvGEPInPSAWRWFFnvVGDSRCPIS 429
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1826 NLYGPTEAAvdvSYMDATL-GLHPEESCVAIgYPVWNTQLYILDQYlrpvPVGVDGEL--YLAGHQLAMGYLHRADLTAS 1902
Cdd:PLN02654  430 DTWWQTETG---GFMITPLpGAWPQKPGSAT-FPFFGVQPVIVDEK----GKEIEGECsgYLCVKKSWPGAFRTLYGDHE 501
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1903 RFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRL--------ISGLDvvvHAISSEQN 1974
Cdd:PLN02654  502 RYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVShpqcaeaaVVGIE---HEVKGQGI 578
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1975 KANVQLVAYLQTTapvdiDQLKKQLA----KHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PLN02654  579 YAFVTLVEGVPYS-----EELRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
625-986 4.05e-14

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 77.88  E-value: 4.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYWPVLEAVNERFPdrPLRAAHTHSFSFDSswlqVFWMLWGQElH 704
Cdd:PRK05677  208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIA--PLPLYHIYAFTFHC----MAMMLIGNH-N 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  705 IFDENmRRDAFGLVQEIQQRQidtldlppsFCAQMMTNGLFVENQHHPS----------LILIGGEAAPLA---LWQQLN 771
Cdd:PRK05677  281 ILISN-PRDLPAMVKELGKWK---------FSGFVGLNTLFVALCNNEAfrkldfsalkLTLSGGMALQLAtaeRWKEVT 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  772 AQPALFAhnlYGPTE----YTVDTFRAELKQTarpvIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRAD 847
Cdd:PRK05677  351 GCAICEG---YGMTEtspvVSVNPSQAIQVGT----IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPE 423
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  848 LSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRL 927
Cdd:PRK05677  424 ATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEA 497
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  928 LGYCVVKdieldeKTSEQLS-QQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK05677  498 IKVFVVV------KPGETLTkEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
486-986 6.57e-14

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: 76.90  E-value: 6.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  486 YPERTaIVSGERPNLQH-LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPID 564
Cdd:cd12119     9 HGDRE-IVSRTHEGEVHrYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  565 RMQMMCEDA-------NPLFVLTTQALAQQLP--QNIQQLHLDQEGVQTQIRKQDASD--IPAENRKFDFQDV----AYV 629
Cdd:cd12119    88 QIAYIINHAedrvvfvDRDFLPLLEAIAPRLPtvEHVVVMTDDAAMPEPAGVGVLAYEelLAAESPEYDWPDFdentAAA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  630 I-FTSGSTGRPKGVMNTHGSLL--NLILSHKPTIYWPVLEAVnerFPDRPLRAAHTHSFSFDSSWLQVFWMLWGQELhif 706
Cdd:cd12119   168 IcYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLGLSESDVV---LPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYL--- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  707 denmrrDAFGLVQEIQQRQidtldlpPSFCA------QMMTNGLFVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFA 778
Cdd:cd12119   242 ------DPASLAELIEREG-------VTFAAgvptvwQGLLDHLEANGRDLSSLrrVVIGGSAVPRSLIEAFEERGVRVI 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  779 HnLYGPTEY----TVDTFRAEL-------KQTARPVIGNPIGNTQAYVLDRHLQRCP-TGV-IGELYISGFGIANGYLgR 845
Cdd:cd12119   309 H-AWGMTETsplgTVARPPSEHsnlsedeQLALRAKQGRPVPGVELRIVDDDGRELPwDGKaVGELQVRGPWVTKSYY-K 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  846 ADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsH 925
Cdd:cd12119   387 NDEESEALTEDGW------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVP----H 456
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577  926 -----RLLGYCVVKDIEldEKTSEQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd12119   457 pkwgeRPLAVVVLKEGA--TVTAEEL----LEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
1540-2009 1.03e-13

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 76.84  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1540 EQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTE 1619
Cdd:PRK08279   45 EAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1620 RIKFMLQDAKSKLVIGEQKDLAAI--------VHPSIATFAFNELFD-ETKVDLSSYKTTV----------ITPQHPAYL 1680
Cdd:PRK08279  125 VLAHSLNLVDAKHLIVGEELVEAFeearadlaRPPRLWVAGGDTLDDpEGYEDLAAAAAGApttnpasrsgVTAKDTAFY 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1681 IYTSGTTGQPKGVMVSHqaivNRIL----WMQSEYPLSATDTILQKTPC---TFDVSVWEffwSYLV-GARLVIAP-IDA 1751
Cdd:PRK08279  205 IYTSGTTGLPKAAVMSH----MRWLkamgGFGGLLRLTPDDVLYCCLPLyhnTGGTVAWS---SVLAaGATLALRRkFSA 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1752 HR---DplallslIQKYQVTTLHFVPSMLAVFENAATEILSSAQRqslpiCRVFCsGEALPTALAKSFTEHFS----CEl 1824
Cdd:PRK08279  278 SRfwdD-------VRRYRATAFQYIGELCRYLLNQPPKPTDRDHR-----LRLMI-GNGLRPDIWDEFQQRFGipriLE- 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1825 hnLYGPTEAAV---DVSYMDATLGLHP--EESCVAI-------GYPVWNTqlyilDQYLRPVPVGVDGELylaghqLAM- 1891
Cdd:PRK08279  344 --FYAASEGNVgfiNVFNFDGTVGRVPlwLAHPYAIvkydvdtGEPVRDA-----DGRCIKVKPGEVGLL------IGRi 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 -------GYLHRADlTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-D 1963
Cdd:PRK08279  411 tdrgpfdGYTDPEA-SEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVeE 489
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 490930577 1964 VVVHAISSEQNKANVQLVAY-LQTTAPVDIDQLKKQLAKHLPAYMVP 2009
Cdd:PRK08279  490 AVVYGVEVPGTDGRAGMAAIvLADGAEFDLAALAAHLYERLPAYAVP 536
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
467-992 1.34e-13

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 76.23  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  467 SHPEQYNNVLDIFYEQVKKYPERTAIVSGERPNLQHL----SFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVV 542
Cdd:PRK06710   10 SYPEEIPSTISYDIQPLHKYVEQMASRYPEKKALHFLgkdiTFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  543 VMLSVL-----------------------NSGAS-FLPLDLDYP---------------IDRMQMMCEDANPLFVLTTQA 583
Cdd:PRK06710   90 GYYGTLlaggivvqtnplytereleyqlhDSGAKvILCLDLVFPrvtnvqsatkiehviVTRIADFLPFPKNLLYPFVQK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  584 LAQQLPQNIQQLHLDQEGVQTQIRKQDASDIPAENRkfdfQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkpTIYWP 663
Cdd:PRK06710  170 KQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPE----NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLM---GVQWL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  664 VLEAVNERFPDRPLRAAHTHSFS--FDSSWLQVFWMLWgqeLHIFDENMrrdafgLVQEIQQRQIDTLDLPPSFCAQMMT 741
Cdd:PRK06710  243 YNCKEGEEVVLGVLPFFHVYGMTavMNLSIMQGYKMVL---IPKFDMKM------VFEAIKKHKVTLFPGAPTIYIALLN 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  742 NGLFVENQHHPSLILIGGEAA-PLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRH 819
Cdd:PRK06710  314 SPLLKEYDISSIRACISGSAPlPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPgSIGVPWPDTEAMIMSLE 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  820 L-QRCPTGVIGELYISGFGIANGYLGRADLSAArFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEI 898
Cdd:PRK06710  394 TgEALPPGEIGEIVVKGPQIMKGYWNKPEETAA-VLQDGWLH------TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYP 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  899 GEVENALSILTNVESAVVIAEPinNSHR---LLGYCVVKDielDEKTSEQLSQQYLsqlRQNLPEYMVPSALTVMSEFPR 975
Cdd:PRK06710  467 REVEEVLYEHEKVQEVVTIGVP--DPYRgetVKAFVVLKE---GTECSEEELNQFA---RKYLAAYKVPKVYEFRDELPK 538
                         570
                  ....*....|....*..
gi 490930577  976 NVSGKVDKKALPKPQIR 992
Cdd:PRK06710  539 TTVGKILRRVLIEEEKR 555
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
1550-2031 1.48e-13

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 76.01  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1550 ALSDENHQLSFSEVRLQVCALAQQLQR-AGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDA 1628
Cdd:PRK12492   42 AFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDS 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1629 KSKLVI-----GE--QKDLA--AIVH----------PSIATFAFNELFDETKVDLSSY--------------------KT 1669
Cdd:PRK12492  122 GARALVylnmfGKlvQEVLPdtGIEYlieakmgdllPAAKGWLVNTVVDKVKKMVPAYhlpqavpfkqalrqgrglslKP 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1670 TVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDtilqktpctfDVSVWEffwsylVGARLVIAP- 1748
Cdd:PRK12492  202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPD----------GQPLMK------EGQEVMIAPl 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 ------------------------IDAHRDPLALLSLIQKYQVTTLHFVPSM-LAVFENAATEILSSAQRQSlpicrVFC 1803
Cdd:PRK12492  266 plyhiyaftancmcmmvsgnhnvlITNPRDIPGFIKELGKWRFSALLGLNTLfVALMDHPGFKDLDFSALKL-----TNS 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1804 SGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVS---YMD-ATLGlhpeescvAIGYPVWNTQLYILDQYLRPVPVGVD 1879
Cdd:PRK12492  341 GGTALVKATAERWEQLTGCTIVEGYGLTETSPVAStnpYGElARLG--------TVGIPVPGTALKVIDDDGNELPLGER 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1880 GELYLAGHQLAMGYLHRADLTASRFVAnpftagQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEqqlrli 1959
Cdd:PRK12492  413 GELCIKGPQVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIE------ 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1960 sglDVVV-H---------AISSEQNKANVQLVAYLQTTApVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRK 2029
Cdd:PRK12492  481 ---DVVMaHpkvancaaiGVPDERSGEAVKLFVVARDPG-LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRR 556

                  ..
gi 490930577 2030 AL 2031
Cdd:PRK12492  557 EL 558
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1579-2031 1.63e-13

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 76.07  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1579 VQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDA-KSKLVIGE------QKDLAAIVHPSIATF 1651
Cdd:PRK08751   73 LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSgASVLVVIDnfgttvQQVIADTPVKQVITT 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1652 AFNELFDETKVDLSSY----------------------------KTTV----ITPQHPAYLIYTSGTTGQPKGVMVSHQA 1699
Cdd:PRK08751  153 GLGDMLGFPKAALVNFvvkyvkklvpeyringairfrealalgrKHSMptlqIEPDDIAFLQYTGGTTGVAKGAMLTHRN 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1700 IVNRIL----WMQSEYPL-SATDTILQKTPctfdvsVWEFFwsYLVGARLVIAPIDA--H-----RDPLALLSLIQKYQV 1767
Cdd:PRK08751  233 LVANMQqahqWLAGTGKLeEGCEVVITALP------LYHIF--ALTANGLVFMKIGGcnHlisnpRDMPGFVKELKKTRF 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1768 TTLHFVPSMLAVFENaaTEILSSAQRQSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLglh 1847
Cdd:PRK08751  305 TAFTGVNTLFNGLLN--TPGFDQIDFSSLKM--TLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTL--- 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1848 pEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHAD 1927
Cdd:PRK08751  378 -KEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW------LHTGDIARMDEQ 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1928 GSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTApVDIDQLKKQLAKHLPAY 2006
Cdd:PRK08751  451 GFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGvLEVAAVGVPDEKSGEIVKVVIVKKDPA-LTAEDVKAHARANLTGY 529
                         490       500
                  ....*....|....*....|....*
gi 490930577 2007 MVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK08751  530 KQPRIIEFRKELPKTNVGKILRREL 554
PRK07867 PRK07867
acyl-CoA synthetase; Validated
1671-2031 2.06e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 75.49  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1671 VITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPctfdvsvweFF--------WSYLVGA 1742
Cdd:PRK07867  148 VADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMP---------LFhsnavmagWAVALAA 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1743 RLVIApIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVfenaateILSSAQR---QSLPIcRVFCSGEALPTALAKsFTEH 1819
Cdd:PRK07867  219 GASIA-LRRKFSASGFLPDVRRYGATYANYVGKPLSY-------VLATPERpddADNPL-RIVYGNEGAPGDIAR-FARR 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1820 FSCELHNLYGPTEAAVDVSYMDATlglhPEEscvAIGYPVWNTQlyILD-QYLRPVPVGVD------------GELY-LA 1885
Cdd:PRK07867  289 FGCVVVDGFGSTEGGVAITRTPDT----PPG---ALGPLPPGVA--IVDpDTGTECPPAEDadgrllnadeaiGELVnTA 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1886 GHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DV 1964
Cdd:PRK07867  360 GPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDAtEV 432
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1965 VVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKH--LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK07867  433 AVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
1566-1935 2.34e-13

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: 75.33  E-value: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1566 QVCALAQQLQRAGVQAG------DIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIgeqkd 1639
Cdd:cd05927    10 EVAERADNIGSALRSLGgkpapaSFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF----- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1640 laaiVHPSIATFAFNELFDETKVDLssYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIlwmqseyplSATDTI 1719
Cdd:cd05927    85 ----CDAGVKVYSLEEFEKLGKKNK--VPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNV---------AGVFKI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1720 LQKTPC--TFDVSVweffwSYLVGA----RLVIAPIDAH--------RDPLALLSLIQKYQVTTLHFVPSML-----AVF 1780
Cdd:cd05927   150 LEILNKinPTDVYI-----SYLPLAhifeRVVEALFLYHgakigfysGDIRLLLDDIKALKPTVFPGVPRVLnriydKIF 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1781 E-------------NAATEI----LSSAQRQSLPI----------------CRVFCSGEALPTALAKSFTEH-FSCELHN 1826
Cdd:cd05927   225 NkvqakgplkrklfNFALNYklaeLRSGVVRASPFwdklvfnkikqalggnVRLMLTGSAPLSPEVLEFLRVaLGCPVLE 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1827 LYGPTE--AAVDVSYMDATLGLHpeescvaIGYPVWNTQLYILD----QYLRPVPVGvDGELYLAGHQLAMGYLHRADLT 1900
Cdd:cd05927   305 GYGQTEctAGATLTLPGDTSVGH-------VGGPLPCAEVKLVDvpemNYDAKDPNP-RGEVCIRGPNVFSGYYKDPEKT 376
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 490930577 1901 ASRFVANPFtagqrmYRTGDIARWHADGSIQYIGR 1935
Cdd:cd05927   377 AEALDEDGW------LHTGDIGEWLPNGTLKIIDR 405
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
1128-1383 2.40e-13

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: 74.53  E-value: 2.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1128 LSLNGDIDPVRLQQALITVLKRHPQLGGHFdSELAEEPVFIYSLHPTQawpVQFCSVTpDLLEQtiqealqqpihLDQPY 1207
Cdd:cd19537    30 CRLSGDVDRDRLASAWNTVLARHRILRSRY-VPRDGGLRRSYSSSPPR---VQRVDTL-DVWKE-----------INRPF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1208 GLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQtNQQLPVLEHSYETVIKALSGRDHETSkvIWQRDLA 1287
Cdd:cd19537    94 DLEREDPIRVFISPDTLLVVMSHIICDLTTLQLLLREVSAAYNG-KLLPPVRREYLDSTAWSRPASPEDLD--FWSEYLS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1288 DLQPLILFNQ-AQQAVQETS--YRLSAELGAKLQHKLRQQGITLNvfmQMIWA---MTLNIYAHREDIVFGTPVSGRSAP 1361
Cdd:cd19537   171 GLPLLNLPRRtSSKSYRGTSrvFQLPGSLYRSLLQFSTSSGITLH---QLALAavaLALQDLSDRTDIVLGAPYLNRTSE 247
                         250       260
                  ....*....|....*....|..
gi 490930577 1362 inGLEQQIGLFLNTIPVRVKLN 1383
Cdd:cd19537   248 --EDMETVGLFLEPLPIRIRFP 267
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
1542-1953 2.46e-13

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 75.42  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPE--QTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPidLQHPTE 1619
Cdd:PRK07768   12 ARTSPRgmVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTM--LHQPTP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1620 RIKFML--QDAKSKL--------VIGEQKDLAAIV--HPSIATFAFNELFDETKVDlssykTTVITPQHPAYLIYTSGTT 1687
Cdd:PRK07768   90 RTDLAVwaEDTLRVIgmigakavVVGEPFLAAAPVleEKGIRVLTVADLLAADPID-----PVETGEDDLALMQLTSGST 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1688 GQPKGVMVSHQAIVNRILWMQSEYPLSA-TDTILQKTPCTFDVSVWEFFWSYL-VGARLV-IAPIDAHRDPLALLSLIQK 1764
Cdd:PRK07768  165 GSPKAVQITHGNLYANAEAMFVAAEFDVeTDVMVSWLPLFHDMGMVGFLTVPMyFGAELVkVTPMDFLRDPLLWAELISK 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1765 YQVTTL---HFVPSMLA-VFENAATEI---LSSaqrqslpiCRVFCSG---------EALPTAlAKSFTEHFSCELhNLY 1828
Cdd:PRK07768  245 YRGTMTaapNFAYALLArRLRRQAKPGafdLSS--------LRFALNGaepidpadvEDLLDA-GARFGLRPEAIL-PAY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1829 GPTEAAVDVSYMDATLGLHPEESC---------------------VAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGH 1887
Cdd:PRK07768  315 GMAEATLAVSFSPCGAGLVVDEVDadllaalrravpatkgntrrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGE 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 1888 QLAMGYlhradLTASRFVanPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:PRK07768  395 SVTPGY-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
1674-2033 3.37e-13

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: 74.83  E-value: 3.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1674 PQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWS--------YLVGARLV 1745
Cdd:cd05908   105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLApliagmnqYLMPTRLF 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1746 IapidahRDPLALLSLIQKYQVTTL---HFVPSMLAVFENAATeilssAQRQSLPICRVFCSG-EALPTALAKSFTEHFS 1821
Cdd:cd05908   185 I------RRPILWLKKASEHKATIVsspNFGYKYFLKTLKPEK-----ANDWDLSSIRMILNGaEPIDYELCHEFLDHMS 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1822 C------ELHNLYGPTEAAVDVSYMDA-----TLGLH--------PEE----------SCVAIGYPVWNTQLYILDQYLR 1872
Cdd:cd05908   254 KyglkrnAILPVYGLAEASVGASLPKAqspfkTITLGrrhvthgePEPevdkkdseclTFVEVGKPIDETDIRICDEDNK 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1873 PVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTagqrmyRTGDIArWHADGSIQYIGRADDQLKIRGQRIELGEI 1952
Cdd:cd05908   334 ILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDI 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1953 EQQLRLISGLD---VVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAY-------MVPthymlVEQFPLSH 2022
Cdd:cd05908   407 ERIAEELEGVElgrVVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRggwqineVLP-----IRRIPKTT 481
                         410
                  ....*....|.
gi 490930577 2023 NGKLDRKALPQ 2033
Cdd:cd05908   482 SGKVKRYELAQ 492
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
1532-2033 4.36e-13

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: 74.49  E-value: 4.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARItPEQTALSDENH--QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:cd17642    18 EQLHKAMKRYASV-PGTIAFTDAHTgvNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVH-PSIATFAFNELFDETKVDLSSYKT--TVITPQHP--------- 1677
Cdd:cd17642    97 APTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNvQKKLKIIKTIIILDSKEDYKGYQClyTFITQNLPpgfneydfk 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 ----------AYLIYTSGTTGQPKGVMVSHQAIVNRIlwmqseypLSATDTIL--QKTPCTFDVSVWEFFWSY------- 1738
Cdd:cd17642   177 ppsfdrdeqvALIMNSSGSTGLPKGVQLTHKNIVARF--------SHARDPIFgnQIIPDTAILTVIPFHHGFgmfttlg 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1739 --LVGARLVIAPidaHRDPLALLSLIQKYQVTTLHFVPSMLAVFenAATEILSSAQRQSLPIcrVFCSGEALPTALAKSF 1816
Cdd:cd17642   249 ylICGFRVVLMY---KFEEELFLRSLQDYKVQSALLVPTLFAFF--AKSTLVDKYDLSNLHE--IASGGAPLSKEVGEAV 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1817 TEHFSCE-LHNLYGPTEAAVDVSymdatlgLHPEESCV--AIGYPVWNTQLYILDQYLRPVpVGVD--GELYLAGHQLAM 1891
Cdd:cd17642   322 AKRFKLPgIRQGYGLTETTSAIL-------ITPEGDDKpgAVGKVVPFFYAKVVDLDTGKT-LGPNerGELCVKGPMIMK 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 GYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQ-QLRLISGLDVVVHAI- 1969
Cdd:cd17642   394 GYVNNPEATKALIDKDGW------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESiLLQHPKIFDAGVAGIp 467
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1970 ---SSEQNKANVQLVAYLQTTAPVDIDQLKKQL--AKHLPAYMVpthymLVEQFPLSHNGKLDRKALPQ 2033
Cdd:cd17642   468 dedAGELPAAVVVLEAGKTMTEKEVMDYVASQVstAKRLRGGVK-----FVDEVPKGLTGKIDRRKIRE 531
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
1672-2031 6.76e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 73.91  E-value: 6.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1672 ITPQHPAYLIYTSGTTGQPKGVMVSHqAIVNRILWMQSE-YPLSATDTILQKTPcTFDVSVWEFFWSYLV--GARLVIAP 1748
Cdd:PRK13388  147 VDAMDPFMLIFTSGTTGAPKAVRCSH-GRLAFAGRALTErFGLTRDDVCYVSMP-LFHSNAVMAGWAPAVasGAAVALPA 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 -IDAHRdplaLLSLIQKYQVTTLHFVPSMLAVfenaateILSSAQR---QSLPICRVFcSGEALPTALAKsFTEHFSCEL 1824
Cdd:PRK13388  225 kFSASG----FLDDVRRYGATYFNYVGKPLAY-------ILATPERpddADNPLRVAF-GNEASPRDIAE-FSRRFGCQV 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1825 HNLYGPTEAAVDVSYMDATlglhPEEScvaIGYPVWNTQLYILDQyLRPVPVGV-D------------GELY-LAGHQLA 1890
Cdd:PRK13388  292 EDGYGSSEGAVIVVREPGT----PPGS---IGRGAPGVAIYNPET-LTECAVARfDahgallnadeaiGELVnTAGAGFF 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1891 MGYLHRADLTASRFvanpftagqR--MYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL-RLISGLDVVVH 1967
Cdd:PRK13388  364 EGYYNNPEATAERM---------RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILlRHPAINRVAVY 434
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 1968 AISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKH--LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK13388  435 AVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL 500
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
1533-1923 7.04e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 73.93  E-value: 7.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSDEN------HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAG 1606
Cdd:PRK12582   50 SIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1607 AAYLPID-----LQHPTERIKFMLQDAKSKLVIGEQ-----KDLAA-------IVHPS-----IATFAFNELFDETKVDL 1664
Cdd:PRK12582  130 VPAAPVSpayslMSHDHAKLKHLFDLVKPRVVFAQSgapfaRALAAldlldvtVVHVTgpgegIASIAFADLAATPPTAA 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1665 SSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTIlqktPCTFDvsvWeFFWSYLVGARL 1744
Cdd:PRK12582  210 VAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPP----PVSLD---W-MPWNHTMGGNA 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1745 VIAP---------IDAHRdPLAllSLIQKyQVTTLHFV-PSmlaVFEN--AATEILSSAQRQSLPICRVFCS-------- 1804
Cdd:PRK12582  282 NFNGllwgggtlyIDDGK-PLP--GMFEE-TIRNLREIsPT---VYGNvpAGYAMLAEAMEKDDALRRSFFKnlrlmayg 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1805 GEALPT-------ALAKSFTEHfSCELHNLYGPTEAAvdvsymDATLGLH-PEESCVAIGYPVWNTQLYIldqylrpVPV 1876
Cdd:PRK12582  355 GATLSDdlyermqALAVRTTGH-RIPFYTGYGATETA------PTTTGTHwDTERVGLIGLPLPGVELKL-------APV 420
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 490930577 1877 GVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIAR 1923
Cdd:PRK12582  421 GDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAAR 461
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
1556-2031 7.05e-13

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 74.02  E-value: 7.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1556 HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG 1635
Cdd:PRK06018   38 VRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1636 EQK---DLAAIVH--PSIATF------------------AFNELFDETKVDlSSYKTtvITPQHPAYLIYTSGTTGQPKG 1692
Cdd:PRK06018  118 DLTfvpILEKIADklPSVERYvvltdaahmpqttlknavAYEEWIAEADGD-FAWKT--FDENTAAGMCYTSGTTGDPKG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1693 VMVSHQA-IVNRILWMQSE-YPLSATDTILQKTPcTFDVSVWEF-FWSYLVGARLVIApiDAHRDPLALLSLIQKYQVTT 1769
Cdd:PRK06018  195 VLYSHRSnVLHALMANNGDaLGTSAADTMLPVVP-LFHANSWGIaFSAPSMGTKLVMP--GAKLDGASVYELLDTEKVTF 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1770 LHFVPSM-LAVFENAATEILssaqrqSLP-ICRVFCSGEALPTALAKSFtEHFSCELHNLYGPTEaavdVSYMDATLGLH 1847
Cdd:PRK06018  272 TAGVPTVwLMLLQYMEKEGL------KLPhLKMVVCGGSAMPRSMIKAF-EDMGVEVRHAWGMTE----MSPLGTLAALK 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1848 PEESCVAI----------GYPVWNTQLYILDQYLRPVPvgVDGE----LYLAGHQLAMGYLhRADltASRFVANPFtagq 1913
Cdd:PRK06018  341 PPFSKLPGdarldvlqkqGYPPFGVEMKITDDAGKELP--WDGKtfgrLKVRGPAVAAAYY-RVD--GEILDDDGF---- 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1914 rmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISGLDVVVHA--ISSEQNKAN------VQLvAYLQ 1985
Cdd:PRK06018  412 --FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEN---LAVGHPKVAEAavIGVYHPKWDerplliVQL-KPGE 485
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 490930577 1986 TTAPVDI-DQLKKQLAKhlpaYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06018  486 TATREEIlKYMDGKIAK----WWMPDDVAFVDAIPHTATGKILKTAL 528
PRK06164 PRK06164
acyl-CoA synthetase; Validated
481-979 7.56e-13

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 73.62  E-value: 7.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  481 EQVKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLD 560
Cdd:PRK06164   18 AHARARPDAVALIDEDRP----LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  561 Y------------------------PID---RMQMMCEDANP----LFVL--TTQALAQQLPQNIQQL--HLDQEGVQTQ 605
Cdd:PRK06164   94 YrshevahilgrgrarwlvvwpgfkGIDfaaILAAVPPDALPplraIAVVddAADATPAPAPGARVQLfaLPDPAPPAAA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  606 IRKQDASDIPAenrkfdfqdVAYVifTSGSTGRPKGVMNTHGSLLnlilSHKptiyWPVLEAVNERfPDRPLRAAHTHSF 685
Cdd:PRK06164  174 GERAADPDAGA---------LLFT--TSGTTSGPKLVLHRQATLL----RHA----RAIARAYGYD-PGAVLLAALPFCG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  686 SFDSSWLQVFwMLWGQELH---IFD-----ENMRRD----AFGlVQEIQQRQIDTLDLPPSFcaqmmtnglfvenqhhPS 753
Cdd:PRK06164  234 VFGFSTLLGA-LAGGAPLVcepVFDaartaRALRRHrvthTFG-NDEMLRRILDTAGERADF----------------PS 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  754 LILIG-----GEAAPLALWQQLNAQPAlfaHNLYGPTEYT--VDTFRAELKQTARPVIGNPIGNTQAYVLDRHLQR---C 823
Cdd:PRK06164  296 ARLFGfasfaPALGELAALARARGVPL---TGLYGSSEVQalVALQPATDPVSVRIEGGGRPASPEARVRARDPQDgalL 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  824 PTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVEN 903
Cdd:PRK06164  373 PDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEH 446
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577  904 ALSILTNVESAVVIAEPINNSHRLLGYCVVKD-IELDEktseqlsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSG 979
Cdd:PRK06164  447 ALEALPGVAAAQVVGATRDGKTVPVAFVIPTDgASPDE-------AGLMAACREALAGFKVPARVQVVEAFPVTESA 516
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
1677-2031 7.89e-13

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: 73.57  E-value: 7.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 PAYLIYTSGTTGQPKGVMVSHQA----IVNRILWmQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPidaH 1752
Cdd:cd05929   127 GWKMLYSGGTTGRPKGIKRGLPGgppdNDTLMAA-ALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLME---K 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1753 RDPLALLSLIQKYQVTTLHFVPSM----LAVFENA-ATEILSSAQRqslpicrVFCSGEALPTALAKSFTEHFSCELHNL 1827
Cdd:cd05929   203 FDPEEFLRLIERYRVTFAQFVPTMfvrlLKLPEAVrNAYDLSSLKR-------VIHAAAPCPPWVKEQWIDWGGPIIWEY 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1828 YGPTEAaVDVSYMDATLGL-HPEescvAIGYPVwNTQLYILDQYLRPVPVGVDGELYLAGHQlAMGYLHRADLTASRFVA 1906
Cdd:cd05929   276 YGGTEG-QGLTIINGEEWLtHPG----SVGRAV-LGKVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNE 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1907 NPFTAgqrmyrTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL-RLISGLDVVV----HAISSEQNKANVQlV 1981
Cdd:cd05929   349 GGWST------LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALiAHPKVLDAAVvgvpDEELGQRVHAVVQ-P 421
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 490930577 1982 AYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05929   422 APGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
467-656 8.69e-13

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: 8.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  467 SHPEQYNNVLDIFYEQVKKYPERTAIVSGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLS 546
Cdd:COG1022     5 SDVPPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  547 VLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLT-TQALAQQLPQNIQQLH-------LDQEGVQTQIRKQDASDIPAEN 618
Cdd:COG1022    85 ILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPslrhivvLDPRGLRDDPRLLSLDELLALG 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 490930577  619 RKFDFQ-------------DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSH 656
Cdd:COG1022   165 REVADPaelearraavkpdDLATIIYTSGTTGRPKGVMLTHRNLLSNARAL 215
PRK07787 PRK07787
acyl-CoA synthetase; Validated
755-989 1.33e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 72.72  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  755 ILIGGEAA-PLALWQQLNAQPALFAHNLYGPTEyTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGV--IGE 830
Cdd:PRK07787  245 LLVSGSAAlPVPVFDRLAALTGHRPVERYGMTE-TLITLSTRADGERRPgWVGLPLAGVETRLVDEDGGPVPHDGetVGE 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  831 LYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGR-CDDQIKIRGYRVEIGEVENALSILT 909
Cdd:PRK07787  324 LQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHP 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  910 NVESAVVIAEPINN-SHRLLGYCV----VKDIELDEKTSEQLSQqylsqlrqnlpeYMVPSALTVMSEFPRNVSGKVDKK 984
Cdd:PRK07787  398 GVREAAVVGVPDDDlGQRIVAYVVgaddVAADELIDFVAQQLSV------------HKRPREVRFVDALPRNAMGKVLKK 465

                  ....*
gi 490930577  985 ALPKP 989
Cdd:PRK07787  466 QLLSE 470
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
625-986 1.36e-12

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 73.16  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKpTIYWPVLeAVNERFPDRPLRAAHThsFSFDSSWLqVFWMLWGQELH 704
Cdd:PRK08974  207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAK-AAYGPLL-HPGKELVVTALPLYHI--FALTVNCL-LFIELGGQNLL 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  705 IFDEnmrRDAFGLVQEIQQRQidtldlppsFCAQMMTNGLF---VENQHHPSL------ILIGG----EAAPLALWQQLN 771
Cdd:PRK08974  282 ITNP---RDIPGFVKELKKYP---------FTAITGVNTLFnalLNNEEFQELdfsslkLSVGGgmavQQAVAERWVKLT 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  772 AQPALFAhnlYGPTE---------YTVDTFRAElkqtarpvIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGY 842
Cdd:PRK08974  350 GQYLLEG---YGLTEcsplvsvnpYDLDYYSGS--------IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGY 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  843 LGRADLSAarfvaNPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPIN 922
Cdd:PRK08974  419 WQRPEATD-----EVIKDG--WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSE 491
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577  923 NSHRLLGYCVV-KDIELdekTSEQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK08974  492 VSGEAVKIFVVkKDPSL---TEEEL----ITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
469-916 1.66e-12

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 72.98  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  469 PEQYNNVLDIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSV- 547
Cdd:PRK08279   33 PDSKRSLGDVFEEAAARHPDRPALLFEDQ----SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLa 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  548 --------LNSGASFLPL----------------DLDYPIDRMQMMCEDANPLFVLTTQALAQqlPQNIQQLHLDQEGVQ 603
Cdd:PRK08279  109 klgavvalLNTQQRGAVLahslnlvdakhlivgeELVEAFEEARADLARPPRLWVAGGDTLDD--PEGYEDLAAAAAGAP 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  604 TQiRKQDASDIPAEnrkfdfqDVAYVIFTSGSTGRPKGVMNTHGSLLN--------LILSHKPTIYWPVleavnerfpdr 675
Cdd:PRK08279  187 TT-NPASRSGVTAK-------DTAFYIYTSGTTGLPKAAVMSHMRWLKamggfgglLRLTPDDVLYCCL----------- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  676 PLraahTHSFSFDSSWLQV-----------------FWmlwgqelhifDENMRRDA--FGLVQEIQqRQIdtLDLPPSfc 736
Cdd:PRK08279  248 PL----YHNTGGTVAWSSVlaagatlalrrkfsasrFW----------DDVRRYRAtaFQYIGELC-RYL--LNQPPK-- 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  737 AQmmtnglfvENQHHPSLIlIGGEAAPlALWQQLNAQpalFA----HNLYGPTE-----YTVDTFR-------AELKQTA 800
Cdd:PRK08279  309 PT--------DRDHRLRLM-IGNGLRP-DIWDEFQQR---FGipriLEFYAASEgnvgfINVFNFDgtvgrvpLWLAHPY 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  801 RPV-----IGNPIGNTqayvlDRHLQRCPTGVIGELY--ISGFGIANGYLGRADlSAARFVANPFEHGQRMYRTGDLVRW 873
Cdd:PRK08279  376 AIVkydvdTGEPVRDA-----DGRCIKVKPGEVGLLIgrITDRGPFDGYTDPEA-SEKKILRDVFKKGDAWFNTGDLMRD 449
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 490930577  874 NSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVV 916
Cdd:PRK08279  450 DGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVV 492
prpE PRK10524
propionyl-CoA synthetase; Provisional
1546-2031 2.21e-12

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 72.67  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAylpidlqHP-- 1617
Cdd:PRK10524   67 PEQLALiavsteTDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAI-------HSvv 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1618 ---------TERIkfmlQDAKSKLVIG------------------EQKDLAA-------IVHPSIATFAFNELFDetkVD 1663
Cdd:PRK10524  140 fggfashslAARI----DDAKPVLIVSadagsrggkvvpykplldEAIALAQhkprhvlLVDRGLAPMARVAGRD---VD 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1664 LSSYKTTVITPQ---------HPAYLIYTSGTTGQPKGVM--VSHQAIVnrilwmqseypLSAT-DTILQKTP-----CT 1726
Cdd:PRK10524  213 YATLRAQHLGARvpvewlesnEPSYILYTSGTTGKPKGVQrdTGGYAVA-----------LATSmDTIFGGKAgetffCA 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1727 FDVSvWEFFWSYLVGARLvIA----------PIdaHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSL 1796
Cdd:PRK10524  282 SDIG-WVVGHSYIVYAPL-LAgmatimyeglPT--RPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSL 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1797 PicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTE-------AAVDVSYMDATLGlhpeescvAIGYPVWNTQLYILDQ 1869
Cdd:PRK10524  358 R--ALFLAGEPLDEPTASWISEALGVPVIDNYWQTEtgwpilaIARGVEDRPTRLG--------SPGVPMYGYNVKLLNE 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1870 YL-RPVPVGVDGELYLAGhQL---AMGYLHRADltaSRFVANPFTA-GQRMYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:PRK10524  428 VTgEPCGPNEKGVLVIEG-PLppgCMQTVWGDD---DRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAG 503
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1945 QRIELGEIEQqlrlisgldvvvhAISSEQNKANVQLV--------------AYLQTTAPVDID--------QLKKQLAKH 2002
Cdd:PRK10524  504 HRLGTREIEE-------------SISSHPAVAEVAVVgvkdalkgqvavafVVPKDSDSLADRearlalekEIMALVDSQ 570
                         570       580
                  ....*....|....*....|....*....
gi 490930577 2003 LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK10524  571 LGAVARPARVWFVSALPKTRSGKLLRRAI 599
PRK05857 PRK05857
fatty acid--CoA ligase;
475-986 2.41e-12

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 72.35  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  475 VLDIFYEQVKKYPERTAIVSGErpNLQHLSFAELAVKVNQLTRFLQENGARKQT---VIAGAIPRSIDSVvvmLSVLNSG 551
Cdd:PRK05857   16 VLDRVFEQARQQPEAIALRRCD--GTSALRYRELVAEVGGLAADLRAQSVSRGSrvlVISDNGPETYLSV---LACAKLG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  552 ASFLPLDLDYPIDRMQMMCEDANPLFVLTTQAL---AQQLPQ---NIQQLHLDQEGVQTQIRKQDASDIPAENRKFDFQD 625
Cdd:PRK05857   91 AIAVMADGNLPIAAIERFCQITDPAAALVAPGSkmaSSAVPEalhSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSED 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  626 VAYVIFTSGSTGRPKGVMNTHGSLLNL--ILSHKPT--IYWPVLEAVNErfpdrPLRAAHTHSFsfdssWLQVFWMLWGQ 701
Cdd:PRK05857  171 PLAMIFTSGTTGEPKAVLLANRTFFAVpdILQKEGLnwVTWVVGETTYS-----PLPATHIGGL-----WWILTCLMHGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  702 ELHIFDENmrrdAFGLVQEIQQRQIDTLDLPPSFCAQMMTNgLFVENQHHPSLILI--GGEAAPLALWQQLNAQPALFAH 779
Cdd:PRK05857  241 LCVTGGEN----TTSLLEILTTNAVATTCLVPTLLSKLVSE-LKSANATVPSLRLVgyGGSRAIAADVRFIEATGVRTAQ 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  780 nLYGPTEY--------TVDTFRAELKQTArpvIGNPIGNTQAYVLDRH------LQRCPTGVIGELYISGFGIANGYLGr 845
Cdd:PRK05857  316 -VYGLSETgctalclpTDDGSIVKIEAGA---VGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWN- 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  846 adlsaarfvaNPFEHGQRM----YRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPI 921
Cdd:PRK05857  391 ----------NPERTAEVLidgwVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD 460
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577  922 NNSHRLLGYCVVKDIELDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK05857  461 EEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
PLN02479 PLN02479
acetate-CoA ligase
1537-2009 2.53e-12

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 72.18  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:PLN02479   25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKD-----------------------LAAIVHPSIATFAFNELFDETKVDLSSYKTTvit 1673
Cdd:PLN02479  105 NAPTIAFLLEHSKSEVVMVDQEFftlaeealkilaekkkssfkpplLIVIGDPTCDPKSLQYALGKGAIEYEKFLET--- 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1674 pQHPAY-------------LIYTSGTTGQPKGVMVSHQ-----AIVNRILWMQSEyplsatDTILQKTPCTFDVSVWEFF 1735
Cdd:PLN02479  182 -GDPEFawkppadewqsiaLGYTSGTTASPKGVVLHHRgaylmALSNALIWGMNE------GAVYLWTLPMFHCNGWCFT 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1736 WSY--LVGARLVIAPIDAHrdplALLSLIQKYQVTTLHFVPSMLAVFENAateilsSAQRQSLPICR---VFCSGEALPT 1810
Cdd:PLN02479  255 WTLaaLCGTNICLRQVTAK----AIYSAIANYGVTHFCAAPVVLNTIVNA------PKSETILPLPRvvhVMTAGAAPPP 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1811 AL-----AKSFTEHFSCELHNLYGPTEAAV-----DVSYMDATLGLHPEESCVAIGYpvwnTQLYILD-QYLRPVPV--G 1877
Cdd:PLN02479  325 SVlfamsEKGFRVTHTYGLSETYGPSTVCAwkpewDSLPPEEQARLNARQGVRYIGL----EGLDVVDtKTMKPVPAdgK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1878 VDGELYLAGHQLAMGYLHRADLTASRFvANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLR 1957
Cdd:PLN02479  401 TMGEIVMRGNMVMKGYLKNPKANEEAF-ANGW------FHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVY 473
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1958 LISG-LDVVVHAISSEQ-NKANVQLVAYLQTTAPVDIDQLKKQLAK----HLPAYMVP 2009
Cdd:PLN02479  474 THPAvLEASVVARPDERwGESPCAFVTLKPGVDKSDEAALAEDIMKfcreRLPAYWVP 531
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
1838-2117 2.53e-12

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 70.16  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1838 SYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGhqLAMGYLHRADLTASRFVANPFTAGQ---R 1914
Cdd:COG3433     3 IATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLG--AGLLLRIRLLAAAARAPFIPVPYPAqpgR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1915 MYRTGDIARWHADGSIQYIGRADDQLKIRG-QRIELGEIEQQLRLISGLDVVVHAISSEQNKANVQLVAYLQTTAPVDID 1993
Cdd:COG3433    81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAeRGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1994 QLKKQLakHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSA-----FEHELTRIFQQILNTD-QN 2067
Cdd:COG3433   161 ALAALD--KVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPAletalTEEELRADVAELLGVDpEE 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 490930577 2068 IGVNEDFFAIGGHSILVMKLAIEIRKVFkRTIPIGQLMSHVTIQRLAALL 2117
Cdd:COG3433   239 IDPDDNLFDLGLDSIRLMQLVERWRKAG-LDVSFADLAEHPTLAAWWALL 287
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1674-2027 3.44e-12

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 72.31  E-value: 3.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1674 PQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPctfdvsvweFFWSYLVGARLViapidahr 1753
Cdd:PRK06814  792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALP---------VFHSFGLTGGLV-------- 854
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1754 dpLALLSLIQKYQV-TTLHF--VPSMlaVFENAATEI------LSSAQRQSLP-----ICRVFCSGEALPTALAKSFTEH 1819
Cdd:PRK06814  855 --LPLLSGVKVFLYpSPLHYriIPEL--IYDTNATILfgtdtfLNGYARYAHPydfrsLRYVFAGAEKVKEETRQTWMEK 930
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1820 FSCELHNLYGPTEAAvdvsymdatlglhPeesCVAIGYPVWN---TQLYIL---DQYLRPVPvGVD--GELYLAGHQLAM 1891
Cdd:PRK06814  931 FGIRILEGYGVTETA-------------P---VIALNTPMHNkagTVGRLLpgiEYRLEPVP-GIDegGRLFVRGPNVML 993
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 GYLhRADltaSRFVANPFTAGqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISGLDV-VVHAIS 1970
Cdd:PRK06814  994 GYL-RAE---NPGVLEPPADG--WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE---LAAELWPdALHAAV 1064
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1971 SEQN-KANVQLVayLQTTAPvDIDQ---LKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:PRK06814 1065 SIPDaRKGERII--LLTTAS-DATRaafLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
627-986 6.40e-12

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 70.96  E-value: 6.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  627 AYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYWPVLEAVNerFPDRPLraahTHSFSFDSswLQVFWMLWG----QE 702
Cdd:PRK07786  177 ALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVG--FVGVPL----FHIAGIGS--MLPGLLLGAptviYP 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  703 LHIFDENMRRDAfglvqeIQQRQIDTLDLPP----SFCAQMMTNGlfvenqHHPSLILIGGEAAPL--ALWQQLNAQ-PA 775
Cdd:PRK07786  249 LGAFDPGQLLDV------LEAEKVTGIFLVPaqwqAVCAEQQARP------RDLALRVLSWGAAPAsdTLLRQMAATfPE 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  776 LFAHNLYGPTEYTVDTFRAELKQTARPV--IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARF 853
Cdd:PRK07786  317 AQILAAFGQTEMSPVTCMLLGEDAIRKLgsVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  854 VANPFEhgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLG---- 929
Cdd:PRK07786  397 AGGWFH-------SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRA----DEKWGevpv 465
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577  930 YCVVKDIELDEKTSEQLSQQylsqLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK07786  466 AVAAVRNDDAALTLEDLAEF----LTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
487-986 9.53e-12

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: 70.60  E-value: 9.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIV-SGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDR 565
Cdd:cd05968    75 RTRPALRwEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEA 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  566 MQMMCEDANPLFVLTTQALAQQ-----LPQNIQQLHLDQEGVQTQI--RKQDASDIPAENR----------------KFD 622
Cdd:cd05968   155 AATRLQDAEAKALITADGFTRRgrevnLKEEADKACAQCPTVEKVVvvRHLGNDFTPAKGRdlsydeeketagdgaeRTE 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  623 FQDVAYVIFTSGSTGRPKGVMNTHGSLlnlilshkptiywpvleavnerfpdrPLRAAHTHSFSF------------DSS 690
Cdd:cd05968   235 SEDPLMIIYTSGTTGKPKGTVHVHAGF--------------------------PLKAAQDMYFQFdlkpgdlltwftDLG 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  691 WLQVFWMLWG-----QELHIFDENMRRDAFGLVQEIQQR-QIDTLDLPPSFCAQMMTNG-LFVENQHHPSLILIGGEAAP 763
Cdd:cd05968   289 WMMGPWLIFGglilgATMVLYDGAPDHPKADRLWRMVEDhEITHLGLSPTLIRALKPRGdAPVNAHDLSSLRVLGSTGEP 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  764 lalWqqlNAQPA--LFAH---------NLYGPTEYTVDTFRAELKQTARPVIGN-PIGNTQAYVLDRHLQRCPtGVIGEL 831
Cdd:cd05968   369 ---W---NPEPWnwLFETvgkgrnpiiNYSGGTEISGGILGNVLIKPIKPSSFNgPVPGMKADVLDESGKPAR-PEVGEL 441
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  832 YISG--FGIANGYLGRADlsaaRFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILT 909
Cdd:cd05968   442 VLLApwPGMTRGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHP 517
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  910 NV-ESAVV-IAEPINNShRLLGYCVVKDielDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05968   518 AVlESAAIgVPHPVKGE-AIVCFVVLKP---GVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
1677-2019 1.08e-11

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: 68.48  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 PAYLIYTSGTTGQPKGVMVSHQAIVNR---ILWMQSeypLSATDTILQKTPcTFDVSVWEF-FWSYLVGARLVIAPidah 1752
Cdd:cd17636     2 PVLAIYTAAFSGRPNGALLSHQALLAQalvLAVLQA---IDEGTVFLNSGP-LFHIGTLMFtLATFHAGGTNVFVR---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1753 R-DPLALLSLIQKYQVT-TLHFVPSMLAVFE-NAATEI-LSSAQRQSLPICRVFCSgEALPTALAKSFtehfscelhNLY 1828
Cdd:cd17636    74 RvDAEEVLELIEAERCThAFLLPPTIDQIVElNADGLYdLSSLRSSPAAPEWNDMA-TVDTSPWGRKP---------GGY 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1829 GPTEaavdVSYMDATLGLHPEESCVAiGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVAnp 1908
Cdd:cd17636   144 GQTE----VMGLATFAALGGGAIGGA-GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1909 ftagqRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTT 1987
Cdd:cd17636   217 -----GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVaDAAVIGVPDPRWAQSVKAIVVLKPG 291
                         330       340       350
                  ....*....|....*....|....*....|..
gi 490930577 1988 APVDIDQLKKQLAKHLPAYMVPTHYMLVEQFP 2019
Cdd:cd17636   292 ASVTEAELIEHCRARIASYKKPKSVEFADALP 323
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
822-986 1.79e-11

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: 69.00  E-value: 1.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  822 RCPTGVIGELYISGF----GIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVE 897
Cdd:cd05937   293 RAPVGEPGEMLGRVPfknrEAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVS 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  898 IGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNV 977
Cdd:cd05937   373 TTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTD 452

                  ....*....
gi 490930577  978 SGKVDKKAL 986
Cdd:cd05937   453 NHKQQKGVL 461
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
1557-1956 2.94e-11

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: 68.65  E-value: 2.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIdlqHPT---ERIKFMLQDAKSK-L 1632
Cdd:cd05932     6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTlnpDTIRYVLEHSESKaL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1633 VIGEQKDLAAIVH------PSIATFAFNEL-FDETKVDL-----SSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSH--- 1697
Cdd:cd05932    83 FVGKLDDWKAMAPgvpeglISISLPPPSAAnCQYQWDDLiaqhpPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFgsf 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1698 ----QAIVNRIlwmqseyPLSATDTILQKTP-CTFDVSVWEFFWSYLVGARLVIA-PIDahrdplALLSLIQKYQVTTLH 1771
Cdd:cd05932   163 awaaQAGIEHI-------GTEENDRMLSYLPlAHVTERVFVEGGSLYGGVLVAFAeSLD------TFVEDVQRARPTLFF 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1772 FVPSMLAVFENAATEILSSAQRQ---SLPI-----------------CRVFCSGEA-LPTALAkSFTEHFSCELHNLYGP 1830
Cdd:cd05932   230 SVPRLWTKFQQGVQDKIPQQKLNlllKIPVvnslvkrkvlkglgldqCRLAGCGSApVPPALL-EWYRSLGLNILEAYGM 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1831 TEaavdvSYMDATLGLHPEESCVAIGYPVWNTQLYILDqylrpvpvgvDGELYLAGHQLAMGYLHRADLTASRFVANPFt 1910
Cdd:cd05932   309 TE-----NFAYSHLNYPGRDKIGTVGNAGPGVEVRISE----------DGEILVRSPALMMGYYKDPEATAEAFTADGF- 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 490930577 1911 agqrmYRTGDIARWHADGSIQYIGRADDQLKI-RGQRIELGEIEQQL 1956
Cdd:cd05932   373 -----LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKL 414
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1102-1408 2.97e-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: 68.06  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1102 PLLPLQKGMLFLSQ-VENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHF---DSELAEEPVFIYSLHptqaW 1177
Cdd:cd20483     3 PMSTFQRRLWFLHNfLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYfegDDFGEQQVLDDPSFH----L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1178 PVQFCSVTPD---LLEQTIQEALQQPIHLDQpyG-LIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ--- 1250
Cdd:cd20483    79 IVIDLSEAADpeaALDQLVRNLRRQELDIEE--GeVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDalr 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1251 -QTNQQlPVLEHSYETVIKALSGRDHETSKVI------WQRDLADLQP---LILF--------NQAQQAVQETSyrLSAE 1312
Cdd:cd20483   157 aGRDLA-TVPPPPVQYIDFTLWHNALLQSPLVqplldfWKEKLEGIPDaskLLPFakaerppvKDYERSTVEAT--LDKE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1313 LGAKLQHKLRQQGITlnVFMQMIWAMTLNIYAH--REDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWE 1390
Cdd:cd20483   234 LLARMKRICAQHAVT--PFMFLLAAFRAFLYRYteDEDLTIGMVDGDRPHP--DFDDLVGFFVNMLPIRCRMDCDMSFDD 309
                         330
                  ....*....|....*...
gi 490930577 1391 QLPQLQQLHVEHLEHDGL 1408
Cdd:cd20483   310 LLESTKTTCLEAYEHSAV 327
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
1554-1948 3.56e-11

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 68.60  E-value: 3.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1554 ENHQLSFSEVRLQVCALAQQLQRAGvQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI-DLQHP--TERIKFMLQDAKS 1630
Cdd:PRK07769   52 VARDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTP 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1631 KlVIGEQKDLAAIVHPSIATFAFNELFDETKVDL------SSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRI 1704
Cdd:PRK07769  131 S-AILTTTDSAEGVRKFFRARPAKERPRVIAVDAvpdevgATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNV 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1705 LWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVI-APIDAHRDP---LALLSLIQKYQVTTLHFVPSMlaVF 1780
Cdd:PRK07769  210 LQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFmSPAAFVRRPgrwIRELARKPGGTGGTFSAAPNF--AF 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1781 ENAATEILSSAQRQSLPICRVFC---SGEALPTALAKSFTEHFS------CELHNLYGPTEAAVDVS-----------YM 1840
Cdd:PRK07769  288 EHAAARGLPKDGEPPLDLSNVKGllnGSEPVSPASMRKFNEAFApyglppTAIKPSYGMAEATLFVSttpmdeeptviYV 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1841 DAT-LGLH-------------PEESCVAIGYPVWNTqlyILD-QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRF- 1904
Cdd:PRK07769  368 DRDeLNAGrfvevpadapnavAQVSAGKVGVSEWAV---IVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFq 444
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1905 ------VANPFTAG----QRMYRTGDIARWHaDGSIQYIGRADDQLKIRG-----QRIE 1948
Cdd:PRK07769  445 nilksrLSESHAEGapddALWVRTGDYGVYF-DGELYITGRVKDLVIIDGrnhypQDLE 502
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
503-986 4.02e-11

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: 67.59  E-value: 4.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLdldypidrmqmmcedanplfvlTTQ 582
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA----------------------TTL 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  583 ALAQQLPQNIQQlhldqeGVQTQIRKQDASDIpaenrkfdfQDVAYVIFTSGSTGRPKGVMNTHGSllnLILSHKPTIYW 662
Cdd:cd05974    59 LTPDDLRDRVDR------GGAVYAAVDENTHA---------DDPMLLYFTSGTTSKPKLVEHTHRS---YPVGHLSTMYW 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  663 PVLEAVNERFP-DRPLRAAHTHSfsfdsswlqVFWMLWGQELHIFDENMRR-DAFGLVQEIQQRQIDTLDLPPSfCAQMM 740
Cdd:cd05974   121 IGLKPGDVHWNiSSPGWAKHAWS---------CFFAPWNAGATVFLFNYARfDAKRVLAALVRYGVTTLCAPPT-VWRML 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  741 TNGLFVENQHHPSLILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQAYVLDRHL 820
Cdd:cd05974   191 IQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDG 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  821 QRCPTGVIGeLYISG---FGIANGYLGRADLSAARFvanpfehGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVE 897
Cdd:cd05974   271 APATEGEVA-LDLGDtrpVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRIS 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  898 IGEVENALSILTNVESAVVIAEPinNSHRLL---GYCVVKDielDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVmSEFP 974
Cdd:cd05974   343 PFELESVLIEHPAVAEAAVVPSP--DPVRLSvpkAFIVLRA---GYEPSPETALEIFRFSRERLAPYKRIRRLEF-AELP 416
                         490
                  ....*....|..
gi 490930577  975 RNVSGKVDKKAL 986
Cdd:cd05974   417 KTISGKIRRVEL 428
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
628-986 4.32e-11

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: 67.79  E-value: 4.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  628 YVIFTSGSTGRPKGVMNTHGSllnlilshkptiywpvleavnERFPDRPLRAAHTHS-FSFDSSWL----------QVFW 696
Cdd:cd05929   129 KMLYSGGTTGRPKGIKRGLPG---------------------GPPDNDTLMAAALGFgPGADSVYLspaplyhaapFRWS 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  697 M---LWGQELHIfdenMRR-DAFGLVQEIQQRQIDTLDLPPSfcaqMMTNGLFV-ENQHH----PSLILIGGEAAPLALW 767
Cdd:cd05929   188 MtalFMGGTLVL----MEKfDPEEFLRLIERYRVTFAQFVPT----MFVRLLKLpEAVRNaydlSSLKRVIHAAAPCPPW 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  768 --QQLNAQPALFAHNLYGPTEYTVDTF-RAELKQTARPVIGNPIGNtQAYVLDRHLQRCPTGVIGELYIS---GFGIANG 841
Cdd:cd05929   260 vkEQWIDWGGPIIWEYYGGTEGQGLTIiNGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFAngpGFEYTND 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  842 YLGRAdlsAARFvanpfEHGqrmYRT-GDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:cd05929   339 PEKTA---AARN-----EGG---WSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVP 407
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577  921 innsHRLLGYCVVKDIE--LDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05929   408 ----DEELGQRVHAVVQpaPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
1542-1923 6.85e-11

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: 67.46  E-value: 6.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDEN-----HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID--- 1613
Cdd:cd05921     5 ARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSpay 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 ---------LQHPTERIK---FMLQDAKSKlvigeQKDLAAIV--HPSIAtFAFNELFDETKVDLSSYKTT--------- 1670
Cdd:cd05921    85 slmsqdlakLKHLFELLKpglVFAQDAAPF-----ARALAAIFplGTPLV-VSRNAVAGRGAISFAELAATpptaavdaa 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1671 --VITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATD--TILQKTPctfdvsvweffWSYLVGARLVI 1746
Cdd:cd05921   159 faAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLP-----------WNHTFGGNHNF 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1747 AP---------IDAHRdPLALL---SLIQKYQV-TTLHF-VPsmlavfenAATEILSSAQRQSLPICR--------VFCS 1804
Cdd:cd05921   228 NLvlynggtlyIDDGK-PMPGGfeeTLRNLREIsPTVYFnVP--------AGWEMLVAALEKDEALRRrffkrlklMFYA 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1805 GEALP-------TALAKSFTEHfSCELHNLYGPTEAAVdvsymDATLGLHPEESCVAIGYPVWNTQlyildqyLRPVPVG 1877
Cdd:cd05921   299 GAGLSqdvwdrlQALAVATVGE-RIPMMAGLGATETAP-----TATFTHWPTERSGLIGLPAPGTE-------LKLVPSG 365
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 490930577 1878 VDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIAR 1923
Cdd:cd05921   366 GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF------YCLGDAAK 405
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
481-986 7.00e-11

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: 67.55  E-value: 7.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  481 EQVKKYPERTAIVSG-----ERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFL 555
Cdd:cd17642    18 EQLHKAMKRYASVPGtiaftDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  556 PLDLDYPIDRMQMMCEDANPLFVLTTQ-------ALAQQLP--QNIQQLHL--DQEGVQTqIRKQDASDIPAENRKFDF- 623
Cdd:cd17642    98 PTNDIYNERELDHSLNISKPTIVFCSKkglqkvlNVQKKLKiiKTIIILDSkeDYKGYQC-LYTFITQNLPPGFNEYDFk 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  624 -------QDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYwpvleaVNERFPDRPLRAA---HtHSFSFDSSwlq 693
Cdd:cd17642   177 ppsfdrdEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIF------GNQIIPDTAILTVipfH-HGFGMFTT--- 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  694 VFWMLWGQE---LHIFDENMrrdafgLVQEIQQRQIDTLDLPPSFCAQMMTNGLfVENQHHPSLILIGGEAAPLA--LWQ 768
Cdd:cd17642   247 LGYLICGFRvvlMYKFEEEL------FLRSLQDYKVQSALLVPTLFAFFAKSTL-VDKYDLSNLHEIASGGAPLSkeVGE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  769 QLNAQPAL-FAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQAYVLDrhlqrCPTGVI------GELYISGFGIANG 841
Cdd:cd17642   320 AVAKRFKLpGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVD-----LDTGKTlgpnerGELCVKGPMIMKG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  842 YLGRADLSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPI 921
Cdd:cd17642   395 YVNNPEATKALIDKDGWLH------SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPD 468
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577  922 NNSHRLLGYCVVKdiELDEKTSEQLSQQYLSQlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17642   469 EDAGELPAAVVVL--EAGKTMTEKEVMDYVAS--QVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
503-986 7.56e-11

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: 67.36  E-value: 7.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFLQENGARKQTViAGAIPRSIDSVVVMLSVLNSGAsfLPLDLDYP--IDRMQMMCEDANPLFVLT 580
Cdd:cd05909     8 LTYRKLLTGAIALARKLAKMTKEGENV-GVMLPPSAGGALANFALALSGK--VPVMLNYTagLRELRACIKLAGIKTVLT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  581 TQALAQQLPQNIQQLHLDQ------EGVQTQIRKQD------ASDIPAENR-------KFDFQDVAYVIFTSGSTGRPKG 641
Cdd:cd05909    85 SKQFIEKLKLHHLFDVEYDarivylEDLRAKISKADkckaflAGKFPPKWLlrifgvaPVQPDDPAVILFTSGSEGLPKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  642 VMNTHGSLL-NlilshkptiywpvLEAVNERFP----DRPLRAAHT-HSFSFDSSwlqvFWMLWGQELHIFDENMRRDAF 715
Cdd:cd05909   165 VVLSHKNLLaN-------------VEQITAIFDpnpeDVVFGALPFfHSFGLTGC----LWLPLLSGIKVVFHPNPLDYK 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  716 GLVQEIQQRQIDTLDLPPSFcaqMMTNGLFVENQHHPSL--ILIGGEAAPLAL---WQQLNAQPALFAhnlYGPTEytvd 790
Cdd:cd05909   228 KIPELIYDKKATILLGTPTF---LRGYARAAHPEDFSSLrlVVAGAEKLKDTLrqeFQEKFGIRILEG---YGTTE---- 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  791 tfraelkqtARPVI--------------GNPIGNTQAYVLDRH-LQRCPTGVIGELYISGFGIANGYLGRADLSAarfva 855
Cdd:cd05909   298 ---------CSPVIsvntpqspnkegtvGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS----- 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  856 npFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALS-ILTNVESAVVIAEPinnsHRLLGYCVVk 934
Cdd:cd05909   364 --FAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSeILPEDNEVAVVSVP----DGRKGEKIV- 436
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490930577  935 dIELDEKTSEQLS-QQYLSQlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05909   437 -LLTTTTDTDPSSlNDILKN--AGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
501-989 8.63e-11

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: 67.00  E-value: 8.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  501 QHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLT 580
Cdd:cd17640     4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  581 tqalaqqlpqniqqlhldqegvqtqirkqdasdipaENRKfdfQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptI 660
Cdd:cd17640    84 ------------------------------------ENDS---DDLATIIYTSGTTGNPKGVMLTHANLLHQIRS----L 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  661 YWPVLEAVNERFpdrplraahthsFSFDSSW------LQVFWMLWGQELH-----IFDENMRR------DAFGLVQEIQQ 723
Cdd:cd17640   121 SDIVPPQPGDRF------------LSILPIWhsyersAEYFIFACGCSQAytsirTLKDDLKRvkphyiVSVPRLWESLY 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  724 RQIDTLDLPPSFCAQMMTNGLFVENQHhpSLILIGGEAAPLALWQQLNAQ--PALfahNLYGPTEYTVDTFRAELKQTAR 801
Cdd:cd17640   189 SGIQKQVSKSSPIKQFLFLFFLSGGIF--KFGISGGGALPPHVDTFFEAIgiEVL---NGYGLTETSPVVSARRLKCNVR 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  802 PVIGNPIGNTQAYVLDRHLQRC-PTGVIGELYISGFGIANGYLgrADLSAARFVANP---FEhgqrmyrTGDLVRWNSAG 877
Cdd:cd17640   264 GSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYY--KNPEATSKVLDSdgwFN-------TGDLGWLTCGG 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  878 KLEFMGRCDDQIKIR-GYRVEIGEVENALSILTNVESAVVIAEpinnSHRLLGYCVVKDIELDEKTSEQLSQQYLSQLRQ 956
Cdd:cd17640   335 ELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQ----DQKRLGALIVPNFEELEKWAKESGVKLANDRSQ 410
                         490       500       510
                  ....*....|....*....|....*....|...
gi 490930577  957 NLpeymvpSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:cd17640   411 LL------ASKKVLKLYKNEIKDEISNRPGFKS 437
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1133-1407 1.16e-10

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: 66.36  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1133 DIDPVRLQQALITVLKRHPQLGGHFDS----ELAEEPvfiyslhPTQAWPVQFCSvtpDLLEQTIQEALQQpihldqpyg 1208
Cdd:cd19535    36 DLDPDRLERAWNKLIARHPMLRAVFLDdgtqQILPEV-------PWYGITVHDLR---GLSEEEAEAALEE--------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1209 lIRATLIQH--APEQSELL-IMVHH--------------LLTDGWSTPLFLQDFIKAYQQTNQQLPVLEHS---YETVIK 1268
Cdd:cd19535    97 -LRERLSHRvlDVERGPLFdIRLSLlpegrtrlhlsidlLVADALSLQILLRELAALYEDPGEPLPPLELSfrdYLLAEQ 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1269 ALSGRDHETSKVIWQRDLADLQ-----PLIlfnQAQQAVQET-----SYRLSAELGAKLQHKLRQQGITLNVFMQMIWAM 1338
Cdd:cd19535   176 ALRETAYERARAYWQERLPTLPpapqlPLA---KDPEEIKEPrftrrEHRLSAEQWQRLKERARQHGVTPSMVLLTAYAE 252
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1339 TLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQ-QLH--VEHLEHDG 1407
Cdd:cd19535   253 VLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQqQLWedLDHSSYSG 324
PLN03052 PLN03052
acetate--CoA ligase; Provisional
1558-1954 1.30e-10

acetate--CoA ligase; Provisional


Pssm-ID: 215553 [Multi-domain]  Cd Length: 728  Bit Score: 67.03  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI-DLQHPTErIKFMLQDAKSK----- 1631
Cdd:PLN03052  209 MTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIaDSFAPSE-IATRLKISKAKaiftq 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1632 -LVIGEQKDLA------------AIVHPSIATFAFNELFDEtkvDLS-----SYKTTVITPQH--PAYL--------IYT 1683
Cdd:PLN03052  288 dVIVRGGKSIPlysrvveakapkAIVLPADGKSVRVKLREG---DMSwddflARANGLRRPDEykAVEQpveaftniLFS 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1684 SGTTGQPKGvmvshqaivnrILWMQSEyPL-SATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIdAHRDPLALLS-- 1760
Cdd:PLN03052  365 SGTTGEPKA-----------IPWTQLT-PLrAAADAWAHLDIRKGDIVCWPTNLGWMMGPWLVYASL-LNGATLALYNgs 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1761 --------LIQKYQVTTLHFVPSMLAVFENaaTEILSSAQRQSLpicRVFCS-GEA---------LPTALAKSFTEhfSC 1822
Cdd:PLN03052  432 plgrgfakFVQDAKVTMLGTVPSIVKTWKN--TNCMAGLDWSSI---RCFGStGEAssvddylwlMSRAGYKPIIE--YC 504
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1823 elhnlyGPTEAAvdVSYMDATLgLHPeESCVAIGYPVWNTQLYILDQYLRPVP--VGVDGELYLAGHQL-AMGYLHRADL 1899
Cdd:PLN03052  505 ------GGTELG--GGFVTGSL-LQP-QAFAAFSTPAMGCKLFILDDSGNPYPddAPCTGELALFPLMFgASSTLLNADH 574
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1900 TASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQ 1954
Cdd:PLN03052  575 YKVYFKGMPVFNGKILRRHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIER 629
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
486-888 1.41e-10

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 66.05  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  486 YPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDR 565
Cdd:PRK09029   16 RPQAIALRLNDEV----LTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  566 MQMMCEDANPLFVLTTQALAQqlPQNIQQLHLDQEGVQTQIRkqdasdipaenrkFDFQDVAYVIFTSGSTGRPKGVMNT 645
Cdd:PRK09029   92 LEELLPSLTLDFALVLEGENT--FSALTSLHLQLVEGAHAVA-------------WQPQRLATMTLTSGSTGLPKAAVHT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  646 HgsllnlilshkptiywpvleavnerfpdrplrAAHTHS---------FSFDSSW---LQVF----------WMLWGQEL 703
Cdd:PRK09029  157 A--------------------------------QAHLASaegvlslmpFTAQDSWllsLPLFhvsgqgivwrWLYAGATL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  704 HIfdenmrRDAFGLVQEIQ------------QRqidtldlppsfcaqmmtngLFVENQHHPSL--ILIGGEAAPLALWQQ 769
Cdd:PRK09029  205 VV------RDKQPLEQALAgcthaslvptqlWR-------------------LLDNRSEPLSLkaVLLGGAAIPVELTEQ 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  770 LNAQpALFAHNLYGPTEY--TVDTFRAElkqtARPVIGNPIGNtqayvldRHLQRcptgVIGELYISGFGIANGYLGRAD 847
Cdd:PRK09029  260 AEQQ-GIRCWCGYGLTEMasTVCAKRAD----GLAGVGSPLPG-------REVKL----VDGEIWLRGASLALGYWRQGQ 323
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 490930577  848 LsaarfvaNPFEHGQRMYRTGDLVRWNSaGKLEFMGRCDDQ 888
Cdd:PRK09029  324 L-------VPLVNDEGWFATRDRGEWQN-GELTILGRLDNL 356
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
1558-2002 1.61e-10

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 66.32  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAylpidlqHP-----------TERIkfmlQ 1626
Cdd:PRK00174   99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV-------HSvvfggfsaealADRI----I 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1627 DAKSKLVI--------GEQKDLAAIV------HPSIAT------------------FAFNELFDETKVDlssykttvITP 1674
Cdd:PRK00174  168 DAGAKLVItadegvrgGKPIPLKANVdealanCPSVEKvivvrrtggdvdwvegrdLWWHELVAGASDE--------CEP 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1675 Q-----HPAYLIYTSGTTGQPKGVM-----------VSHQAIV----NRILWmqseyplsatdtilqktpCTFDVSvwef 1734
Cdd:PRK00174  240 EpmdaeDPLFILYTSGSTGKPKGVLhttggylvyaaMTMKYVFdykdGDVYW------------------CTADVG---- 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1735 fW----SYLV------GARLVI---API--DAHRdplaLLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLpic 1799
Cdd:PRK00174  298 -WvtghSYIVygplanGATTLMfegVPNypDPGR----FWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSL--- 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1800 RVFCS-GEAL-PTALaksftEHFscelHNLYG----P-------TEAAvdvSYMDATL-GLHPEE--SCvaiGYPVWNTQ 1863
Cdd:PRK00174  370 RLLGSvGEPInPEAW-----EWY----YKVVGgercPivdtwwqTETG---GIMITPLpGATPLKpgSA---TRPLPGIQ 434
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1864 LYILDQYLRPVPVGVDGelYLAghqlamgylhradLTAS-------------RFVANPFTAGQRMYRTGDIARWHADGSI 1930
Cdd:PRK00174  435 PAVVDEEGNPLEGGEGG--NLV-------------IKDPwpgmmrtiygdheRFVKTYFSTFKGMYFTGDGARRDEDGYY 499
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1931 QYIGRADDQLKIRGQRIELGEIEqqlrliSGLdvVVHAISSEqnkANV----------QLVAY--LQTTAPVDiDQLKKQ 1998
Cdd:PRK00174  500 WITGRVDDVLNVSGHRLGTAEIE------SAL--VAHPKVAE---AAVvgrpddikgqGIYAFvtLKGGEEPS-DELRKE 567

                  ....
gi 490930577 1999 LAKH 2002
Cdd:PRK00174  568 LRNW 571
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
625-992 1.81e-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: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGS------LLNLILSHKPTiywPVLeavnerFPDRPLraahthsFSFDSSWLQVFWML 698
Cdd:cd05944     3 DVAAYFHTGGTTGTPKLAQHTHSNevynawMLALNSLFDPD---DVL------LCGLPL-------FHVNGSVVTLLTPL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  699 W-GQELHIFDENMRRDAfGLVQE----IQQRQIDTLDLPPSFCAQMMTNGLfveNQHHPSL--ILIGGEAAPLALWQQLN 771
Cdd:cd05944    67 AsGAHVVLAGPAGYRNP-GLFDNfwklVERYRITSLSTVPTVYAALLQVPV---NADISSLrfAMSGAAPLPVELRARFE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  772 AQPALFAHNLYGPTEYTVDTFRAELKQTARP-VIGNPIGNTQA--YVLD---RHLQRCPTGVIGELYISGFGIANGYLgR 845
Cdd:cd05944   143 DATGLPVVEGYGLTEATCLVAVNPPDGPKRPgSVGLRLPYARVriKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYL-Y 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  846 ADLSAARFVanpfehGQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIR-GYRVEIGEVENALSILTNVESAVVIAEPinNS 924
Cdd:cd05944   222 TEGNKNAFV------ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQP--DA 292
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  925 HRllGYCVVKDIELDEKTSEQlSQQYLSQLRQNLPEY-MVPSALTVMSEFPRNVSGKVDKKALPKPQIR 992
Cdd:cd05944   293 HA--GELPVAYVQLKPGAVVE-EEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADAIH 358
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
1556-1707 2.37e-10

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 65.92  E-value: 2.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1556 HQLSFSEVRLQVCALAQQLQRAgVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI---DLQHPTERIKFMLQDAKSKL 1632
Cdd:PRK12476   67 VELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfapELPGHAERLDTALRDAEPTV 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1633 VIGEQ-------KDLAAIVH---PSIatFAFNELFDETKVDlssYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVN 1702
Cdd:PRK12476  146 VLTTTaaaeaveGFLRNLPRlrrPRV--IAIDAIPDSAGES---FVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGT 220

                  ....*
gi 490930577 1703 RILWM 1707
Cdd:PRK12476  221 NLVQM 225
PRK08315 PRK08315
AMP-binding domain protein; Validated
1530-2025 3.02e-10

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 65.60  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTAL--SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGA 1607
Cdd:PRK08315   14 LEQTIGQLLDRTAARYPDREALvyRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 -------AYLPIDLQHP-----------TERIKF-----MLQDAKSKLVIGEQKDLAAIVHPSIAT------------FA 1652
Cdd:PRK08315   94 ilvtinpAYRLSELEYAlnqsgckaliaADGFKDsdyvaMLYELAPELATCEPGQLQSARLPELRRviflgdekhpgmLN 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1653 FNELF----DETKVDLSSYKTT-----VITPQhpayliYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKT 1723
Cdd:PRK08315  174 FDELLalgrAVDDAELAARQATldpddPINIQ------YTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1724 P---CtfdvsvwefFWSYL-------VGARLVIaPIDAHrDPLALLSLIQKYQVTTLHFVPSM-LAVFENA--ATEILSS 1790
Cdd:PRK08315  248 PlyhC---------FGMVLgnlacvtHGATMVY-PGEGF-DPLATLAAVEEERCTALYGVPTMfIAELDHPdfARFDLSS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1791 ------AqrqslpicrvfcsGEALPTALAKSFTE--HFScELHNLYGPTEAAvDVSYM---DATLglhpEESCVAIGYPV 1859
Cdd:PRK08315  317 lrtgimA-------------GSPCPIEVMKRVIDkmHMS-EVTIAYGMTETS-PVSTQtrtDDPL----EKRVTTVGRAL 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1860 WNTQLYILDQYL-RPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrMyRTGDIARWHADGSIQYIGRADD 1938
Cdd:PRK08315  378 PHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW-----M-HTGDLAVMDEEGYVNIVGRIKD 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1939 QLkIR-GQRIELGEIEQQLRLISG-LDVVVHAISSEqnKANVQLVAYL-----QTTAPVDI-DQLKKQLAKhlpaYMVPT 2010
Cdd:PRK08315  452 MI-IRgGENIYPREIEEFLYTHPKiQDVQVVGVPDE--KYGEEVCAWIilrpgATLTEEDVrDFCRGKIAH----YKIPR 524
                         570
                  ....*....|....*
gi 490930577 2011 HYMLVEQFPLSHNGK 2025
Cdd:PRK08315  525 YIRFVDEFPMTVTGK 539
PRK08308 PRK08308
acyl-CoA synthetase; Validated
861-987 3.09e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 64.67  E-value: 3.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  861 GQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDe 940
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEID- 367
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 490930577  941 ktSEQLSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:PRK08308  368 --PVQLRE----WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
1680-2026 3.19e-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: 64.06  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVMVSH-QAIVNRILWMQSEyPLSATDTILQKTPctfdvsvweFFWSY----------LVGARLViaP 1748
Cdd:cd17638     5 IMFTSGTTGRSKGVMCAHrQTLRAAAAWADCA-DLTEDDRYLIINP---------FFHTFgykagivaclLTGATVV--P 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 IdAHRDPLALLSLIQKYQVTtlhFVPSMLAVFENaateILSSAQRQS--LPICRVFCSGEA-LPTALAKSFTEHFSCE-L 1824
Cdd:cd17638    73 V-AVFDVDAILEAIERERIT---VLPGPPTLFQS----LLDHPGRKKfdLSSLRAAVTGAAtVPVELVRRMRSELGFEtV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1825 HNLYGPTEAAVdvsymdATLgLHPEESCVAI----GYPVWNTQLYILDqylrpvpvgvDGELYLAGHQLAMGYLHRADLT 1900
Cdd:cd17638   145 LTAYGLTEAGV------ATM-CRPGDDAETVattcGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEAT 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1901 ASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQ----NK 1975
Cdd:cd17638   208 AEAIDADGW------LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVaQVAVIGVPDERmgevGK 281
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1976 ANVqlVAYLQTTapVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKL 2026
Cdd:cd17638   282 AFV--VARPGVT--LTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
18-352 3.25e-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: 65.03  E-value: 3.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   18 RFELASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNE---ADTVIASYSSDPSQpFIELNNQVQFQ 94
Cdd:cd20484     1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQhpiLKSVIEEEDGVPFQ-KIEPSKPLSFQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   95 IEefDFCHLTPkkaqqrlWDWMPSDRQCAK---SLKAGEtqLFRQVLFTTHDKVYWYQ-RYHHIMLDGFSMINLTKRIVE 170
Cdd:cd20484    80 EE--DISSLKE-------SEIIAYLREKAKepfVLENGP--LMRVHLFSRSEQEHFVLiTIHHIIFDGSSSLTLIHSLLD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  171 LYQQLQEGKDLSVSPFIGV-NEVISERQAYENSHQFKIDQAFWKAYCE------DLPSPislSTHHLAAKTTATfvKHQL 243
Cdd:cd20484   149 AYQALLQGKQPTLASSPASyYDFVAWEQDMLAGAEGEEHRAYWKQQLSgtlpilELPAD---RPRSSAPSFEGQ--TYTR 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  244 RFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWV 323
Cdd:cd20484   224 RLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFS 303
                         330       340
                  ....*....|....*....|....*....
gi 490930577  324 SLAQHVQEQLREIRPHQKYDAEQILRDLN 352
Cdd:cd20484   304 DFIRKLQLTVLDGLDHAAYPFPAMVRDLN 332
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
625-884 3.49e-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: 64.79  E-value: 3.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKpTIYWPVLEAVNerFPDRPLRAahthsfsfdsswlqVFWMLWGQELH 704
Cdd:cd05910    86 EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALR-QLYGIRPGEVD--LATFPLFA--------------LFGPALGLTSV 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  705 IFDENMRR----DAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLfvENQHH-PSL--ILIGGEAAPLALWQQLNA--QPA 775
Cdd:cd05910   149 IPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCA--QHGITlPSLrrVLSAGAPVPIALAARLRKmlSDE 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  776 LFAHNLYGPTE---------YTVDTFRAELKQTARPV-IGNPIGNTQAYVL-----------DRHlqRCPTGVIGELYIS 834
Cdd:cd05910   227 AEILTPYGATEalpvssigsRELLATTTAATSGGAGTcVGRPIPGVRVRIIeiddepiaewdDTL--ELPRGEIGEITVT 304
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 490930577  835 GFGIANGYLGRADlsAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGR 884
Cdd:cd05910   305 GPTVTPTYVNRPV--ATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGR 352
PLN02574 PLN02574
4-coumarate--CoA ligase-like
503-997 3.96e-10

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 65.25  E-value: 3.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFL-QENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTT 581
Cdd:PLN02574   67 ISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  582 QALAQQL-PQNIQQLHLDQEGVQTQIRKQDASDIPAENRKFDF--------QDVAYVIFTSGSTGRPKGVMNTHGsllNL 652
Cdd:PLN02574  147 PENVEKLsPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDFvpkpvikqDDVAAIMYSSGTTGASKGVVLTHR---NL 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  653 ILSHKPTIywpvleavneRFpdrplRAAHTHSFSFDSSWLQVFWMLWGQELHIFDEN----------MRR-DAFGLVQEI 721
Cdd:PLN02574  224 IAMVELFV----------RF-----EASQYEYPGSDNVYLAALPMFHIYGLSLFVVGllslgstivvMRRfDASDMVKVI 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  722 QQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGEAAPLA---LWQQLNAQPALFAHNLYGPTEYT-VDTFRAELK 797
Cdd:PLN02574  289 DRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSgkfIQDFVQTLPHVDFIQGYGMTESTaVGTRGFNTE 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  798 QTAR-PVIGNPIGNTQAYVLDRHLQRC-PTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHgqrmyrTGDLVRWNS 875
Cdd:PLN02574  369 KLSKySSVGLLAPNMQAKVVDWSTGCLlPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLR------TGDIAYFDE 442
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  876 AGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKdieldeKTSEQLSQ-QYLSQL 954
Cdd:PLN02574  443 DGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVR------RQGSTLSQeAVINYV 516
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 490930577  955 RQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP-QIRAHSRM 997
Cdd:PLN02574  517 AKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSlTNSVSSRL 560
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
479-986 4.36e-10

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 65.33  E-value: 4.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  479 FYEQVKKYPERTAIVSGERPNLQHLSFAELAVkvnQLTRFLQENGARKQTViaGAI-PRSIDSVVVMLSVLNSGAsfLPL 557
Cdd:PRK08633  621 WIDTAKRNWSRLAVADSTGGELSYGKALTGAL---ALARLLKRELKDEENV--GILlPPSVAGALANLALLLAGK--VPV 693
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  558 DLDYPI--DRMQMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQ-------EGVQTQIRKQD-------ASDIPA----- 616
Cdd:PRK08633  694 NLNYTAseAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPEnvkviylEDLKAKISKVDkltallaARLLPArllkr 773
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  617 -ENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLIlshkptiywpvlEAVNERFP----DR-----PLraahTHSFS 686
Cdd:PRK08633  774 lYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNI------------EQISDVFNlrndDVilsslPF----FHSFG 837
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  687 FDSSwlqvfwmLWGQELhifdENMR-------RDAFGLVQEIQQRQIDTLDLPPSFCaqmmtnGLFVENQH-HP------ 752
Cdd:PRK08633  838 LTVT-------LWLPLL----EGIKvvyhpdpTDALGIAKLVAKHRATILLGTPTFL------RLYLRNKKlHPlmfasl 900
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  753 SLILIGGEAAPLALWQQLNAQpalFAHNL---YGPTEYT-V------DTFRAE-LKQTA--RPVIGNPIGNTQAYVLD-R 818
Cdd:PRK08633  901 RLVVAGAEKLKPEVADAFEEK---FGIRIlegYGATETSpVasvnlpDVLAADfKRQTGskEGSVGMPLPGVAVRIVDpE 977
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  819 HLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVAnpfEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEI 898
Cdd:PRK08633  978 TFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPL 1054
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  899 GEVENALSILTNVESAVVIAEPINNSHRllGYCVVKDIELDEKTSEQLSQQYLSqlrQNLPEYMVPSALTVMSEFPRNVS 978
Cdd:PRK08633 1055 GAVEEELAKALGGEEVVFAVTAVPDEKK--GEKLVVLHTCGAEDVEELKRAIKE---SGLPNLWKPSRYFKVEALPLLGS 1129

                  ....*...
gi 490930577  979 GKVDKKAL 986
Cdd:PRK08633 1130 GKLDLKGL 1137
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
2148-2265 4.86e-10

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 61.47  E-value: 4.86e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   2148 FYPGSGsAWQYTVLNRYLHSDLPIIGLQSP--RPDGLLAnsTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVA 2225
Cdd:smart00824    6 TAAPSG-PHEYARLAAALRGRRDVSALPLPgfGPGEPLP--ASADALVEAQAEAVLRAAGGRPFVLVGHSSGGLLAHAVA 82
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 490930577   2226 AKLTEQGEKVDYLGLLDTYPAE---IHQWLDLSVEEMNAEAEQ 2265
Cdd:smart00824   83 ARLEARGIPPAAVVLLDTYPPGdpaPEGWLPELLRGVFEREDS 125
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
616-981 7.84e-10

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 64.25  E-value: 7.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  616 AENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLL-NLI--------LSHKPTIYWPVLeavnerfpdrPLraahTHSFS 686
Cdd:PRK05605  211 VSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFaNAAqgkawvpgLGDGPERVLAAL----------PM----FHAYG 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  687 FdsSWLQVFWMLWGQELHIFD--------ENMRRD--AF---------GLVQEIQQRQID----------TLDLPPSFCA 737
Cdd:PRK05605  277 L--TLCLTLAVSIGGELVLLPapdidlilDAMKKHppTWlpgvpplyeKIAEAAEERGVDlsgvrnafsgAMALPVSTVE 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  738 --QMMTNGLFVEnqhhpsliligG----EAAPLALWQQLNAqpalfahnlygpteytvdtfraelkqTARP-VIGNPIGN 810
Cdd:PRK05605  355 lwEKLTGGLLVE-----------GygltETSPIIVGNPMSD--------------------------DRRPgYVGVPFPD 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  811 TQAYVLDRH-LQRC-PTGVIGELYISGFGIANGYLGRADLSAARFvanpfeHGQrMYRTGDLVRWNSAGKLEFMGRCDDQ 888
Cdd:PRK05605  398 TEVRIVDPEdPDETmPDGEEGELLVRGPQVFKGYWNRPEETAKSF------LDG-WFRTGDVVVMEEDGFIRIVDRIKEL 470
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  889 IKIRGYRVEIGEVENALSILTNVESAVVIAEPINNShrllGYCVVKDIELDEktSEQLSQQYLSQ-LRQNLPEYMVPSAL 967
Cdd:PRK05605  471 IITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDG----SEEVVAAVVLEP--GAALDPEGLRAyCREHLTRYKVPRRF 544
                         410
                  ....*....|....
gi 490930577  968 TVMSEFPRNVSGKV 981
Cdd:PRK05605  545 YHVDELPRDQLGKV 558
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
487-980 1.06e-09

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: 63.83  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYP---- 562
Cdd:cd05943    83 DDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGvpgv 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  563 IDRMQMMcedaNPLFVLT----------------TQALAQQLPQNIQQLHLD--QEGVQTQIRKQ-----------DASD 613
Cdd:cd05943   163 LDRFGQI----EPKVLFAvdaytyngkrhdvrekVAELVKGLPSLLAVVVVPytVAAGQPDLSKIakaltledflaTGAA 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  614 IPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLnlilshkptiywpvLEAVNErfpdrplraahtHSFSFDSSWLQ 693
Cdd:cd05943   239 GELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTL--------------LQHLKE------------HILHCDLRPGD 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  694 VF-------WMLW---------GQELHIFDEN-MRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHH-PSLI 755
Cdd:cd05943   293 RLfyyttcgWMMWnwlvsglavGATIVLYDGSpFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDlSSLR 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  756 LIGGEAAPLA----LWQQLNAQPALFAHNLYGPTEyTVDTFraelkqtarpVIGNPI-----GNTQAYVLDRHLQ----- 821
Cdd:cd05943   373 TILSTGSPLKpesfDYVYDHIKPDVLLASISGGTD-IISCF----------VGGNPLlpvyrGEIQCRGLGMAVEafdee 441
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  822 -RCPTGVIGELYI-SGF-GIANGYLGRADlsAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEI 898
Cdd:cd05943   442 gKPVWGEKGELVCtKPFpSMPVGFWNDPD--GSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGT 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  899 GEVENALSILTNVESAVVIAE--PINNSHRLLGYCVVKDIELDektsEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRN 976
Cdd:cd05943   520 AEIYRVVEKIPEVEDSLVVGQewKDGDERVILFVKLREGVELD----DELRKRIRSTIRSALSPRHVPAKIIAVPDIPRT 595

                  ....
gi 490930577  977 VSGK 980
Cdd:cd05943   596 LSGK 599
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
469-986 1.32e-09

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 63.50  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  469 PEQYNNVLDIFYEQVKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVL 548
Cdd:PRK07059   19 ASQYPSLADLLEESFRQYADRPAFICMGKA----ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  549 NSGAS-------FLPLDLDYpidrmQMMCEDANPLFVLTTQA-LAQQLPQNIQQLHL------DQEGVQTQI-----RKQ 609
Cdd:PRK07059   95 RAGYVvvnvnplYTPRELEH-----QLKDSGAEAIVVLENFAtTVQQVLAKTAVKHVvvasmgDLLGFKGHIvnfvvRRV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  610 D----ASDIP---------AENRKFDFQ-------DVAYVIFTSGSTGRPKGVMNTHGSLL-NLILSHKptiyWpvLEAV 668
Cdd:PRK07059  170 KkmvpAWSLPghvrfndalAEGARQTFKpvklgpdDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQMEA----W--LQPA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  669 NERFPDR---------PLraahTHSFSfdsswLQVFWMLwgqelhifdeNMR-----------RDAFGLVQEIQQRQIDT 728
Cdd:PRK07059  244 FEKKPRPdqlnfvcalPL----YHIFA-----LTVCGLL----------GMRtggrnilipnpRDIPGFIKELKKYQVHI 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  729 ldlppsFCAqmmTNGLFVENQHHP--------SLIL-IGGEAA---PLA-LWQQLNAQPAlfaHNLYGPTE--------- 786
Cdd:PRK07059  305 ------FPA---VNTLYNALLNNPdfdkldfsKLIVaNGGGMAvqrPVAeRWLEMTGCPI---TEGYGLSEtspvatcnp 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  787 YTVDTFRAelkqtarpVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYR 866
Cdd:PRK07059  373 VDATEFSG--------TIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FR 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  867 TGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVV-KDIELDEktseq 945
Cdd:PRK07059  439 TGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVkKDPALTE----- 513
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 490930577  946 lsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK07059  514 --EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
1676-2031 1.36e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 63.61  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1676 HPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYL-VGARLV------IAP 1748
Cdd:PTZ00237  255 HPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLsLGNTFVmfeggiIKN 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 IDAHRDplaLLSLIQKYQVTTLHFVPSMLAVFENA---ATEILSSAQRQSLPicRVFCSGEALPTALAKSFTEHFSCELH 1825
Cdd:PTZ00237  335 KHIEDD---LWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLK--EIWCGGEVIEESIPEYIENKLKIKSS 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1826 NLYGPTEAAVdvsymdatlglhpeesCVAIGYPVWNTQLYIL---DQYLRPVPVGVDG------ELYLAGHQLAM--GYl 1894
Cdd:PTZ00237  410 RGYGQTEIGI----------------TYLYCYGHINIPYNATgvpSIFIKPSILSEDGkelnvnEIGEVAFKLPMppSF- 472
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1895 hradltASRFVANP------FTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQ-LRLISGLDVVVH 1967
Cdd:PTZ00237  473 ------ATTFYKNDekfkqlFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSiLKHPLVLECCSI 546
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1968 AISSeQNKANVqLVAYL-----QTTAPVDIDQLKKQ----LAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PTZ00237  547 GIYD-PDCYNV-PIGLLvlkqdQSNQSIDLNKLKNEinniITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2052-2111 1.45e-09

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: 56.03  E-value: 1.45e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577  2052 HELTRIFQQILNTD-QNIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQ 2111
Cdd:pfam00550    1 ERLRELLAEVLGVPaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
1536-1956 1.46e-09

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: 63.44  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1536 QLLReqARITPEQTAL-SDENH---QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYL- 1610
Cdd:cd05943    75 NLLR--HADADDPAAIyAAEDGertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSs 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1611 --P-------IDLQHPTE-RIKFM---------LQDAKSKL--VIGEQKDLAAIVHpsIATFAFNELFDETK----VDLS 1665
Cdd:cd05943   153 csPdfgvpgvLDRFGQIEpKVLFAvdaytyngkRHDVREKVaeLVKGLPSLLAVVV--VPYTVAAGQPDLSKiakaLTLE 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1666 SYKTTVITPQ---------HPAYLIYTSGTTGQPKGVMVSH-----QAIVNRILwmQSEypLSATDTILQKTPCTFdvSV 1731
Cdd:cd05943   231 DFLATGAAGElefeplpfdHPLYILYSSGTTGLPKCIVHGAggtllQHLKEHIL--HCD--LRPGDRLFYYTTCGW--MM 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1732 WEFFWSYL-VGARLVI---APidAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAAteiLSSAQRQSLPICRVFCS-GE 1806
Cdd:cd05943   305 WNWLVSGLaVGATIVLydgSP--FYPDTNALWDLADEEGITVFGTSAKYLDALEKAG---LKPAETHDLSSLRTILStGS 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1807 ALPTALAKSFTEH--FSCELHNLYGPTEAAVDVSYMDATLGLHPEE-SCVAIGYPVwntqlYILDQYLRPVpVGVDGELY 1883
Cdd:cd05943   380 PLKPESFDYVYDHikPDVLLASISGGTDIISCFVGGNPLLPVYRGEiQCRGLGMAV-----EAFDEEGKPV-WGEKGELV 453
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1884 LAGHQLAM--GYLHRADltASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL 1956
Cdd:cd05943   454 CTKPFPSMpvGFWNDPD--GSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVV 526
PRK09274 PRK09274
peptide synthase; Provisional
474-884 1.69e-09

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 62.99  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  474 NVLDIFYEQVKKYPERTAIV------SGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSV 547
Cdd:PRK09274    7 NIARHLPRAAQERPDQLAVAvpggrgADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFAL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  548 LNSGAsfLPLDLDYPIDRMQMM-C-EDANPLfVLTTQALAQQL-------PQNIQQL-----HLDQEGVQ-TQIRkQDAS 612
Cdd:PRK09274   87 FKAGA--VPVLVDPGMGIKNLKqClAEAQPD-AFIGIPKAHLArrlfgwgKPSVRRLvtvggRLLWGGTTlATLL-RDGA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  613 DIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLIlshkptiywpvlEAVNERFPDRPlraahthsFSFDSSWL 692
Cdd:PRK09274  163 AAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQI------------EALREDYGIEP--------GEIDLPTF 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  693 QVFwmlwgqELH---------IFDENMRRDAFG----LVQEIQQRQIDTLdlppsFC--AQMMTNGLFVENQHH--PSL- 754
Cdd:PRK09274  223 PLF------ALFgpalgmtsvIPDMDPTRPATVdpakLFAAIERYGVTNL-----FGspALLERLGRYGEANGIklPSLr 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  755 -ILIGGEAAPLALWQQLNA---QPALFaHNLYGPTE---YTVDTFRAELKQTA------------RPVIG---------- 805
Cdd:PRK09274  292 rVISAGAPVPIAVIERFRAmlpPDAEI-LTPYGATEalpISSIESREILFATRaatdngagicvgRPVDGvevriiaisd 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  806 NPIgntqayvldRHLQ---RCPTGVIGELYISGFGIANGYLGRADLSAARFVANPfeHGQRMYRTGDLVRWNSAGKLEFM 882
Cdd:PRK09274  371 API---------PEWDdalRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFC 439

                  ..
gi 490930577  883 GR 884
Cdd:PRK09274  440 GR 441
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
482-986 2.02e-09

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 62.85  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  482 QVKKYPERTAIVSGErpnlQHLSFAELAVKVNqltrflqengARKQTVIAGAIPRSiDSVVVMLS--------VLNS--- 550
Cdd:PRK06155   30 QAERYPDRPLLVFGG----TRWTYAEAARAAA----------AAAHALAAAGVKRG-DRVALMCGnriefldvFLGCawl 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  551 GASFLPLDLDYPIDRMQMMCEDANP-LFVLTTQALA--QQLPQNIQQLH----LDQEGVQTQIRKQDASDIPAENRKFDF 623
Cdd:PRK06155   95 GAIAVPINTALRGPQLEHILRNSGArLLVVEAALLAalEAADPGDLPLPavwlLDAPASVSVPAGWSTAPLPPLDAPAPA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  624 QDV-----AYVIFTSGSTGRPKGVMNTHGSLLnlilshkptiYWPVLEA----VNER---FPDRPLraAHTHSFSfdsSW 691
Cdd:PRK06155  175 AAVqpgdtAAILYTSGTTGPSKGVCCPHAQFY----------WWGRNSAedleIGADdvlYTTLPL--FHTNALN---AF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  692 LQVfwMLWGQELHIFDenmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGeAAPLALWQQLN 771
Cdd:PRK06155  240 FQA--LLAGATYVLEP---RFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGP-GVPAALHAAFR 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  772 AQPALFAHNLYGPTEYTVDTfrAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISG---FGIANGYLGRAD 847
Cdd:PRK06155  314 ERFGVDLLDGYGSTETNFVI--AVTHGSQRPgSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPE 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  848 LSAARFvANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRL 927
Cdd:PRK06155  392 KTVEAW-RNLWFH------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVP----SEL 460
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577  928 LGYCVVKDIELDEKTS---EQLSQQYLSQlrqnLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK06155  461 GEDEVMAAVVLRDGTAlepVALVRHCEPR----LAYFAVPRYVEFVAALPKTENGKVQKFVL 518
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
490-999 2.34e-09

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 62.49  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  490 TAIVSGERPNLQHLSFAELAVKVNQLTRFLQEN-GARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQM 568
Cdd:PRK05620   26 TTVTTWGGAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVH 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  569 MCEDANPLFVLTTQALAQQLPQNIQQLhldqEGVQTQI----------RKQDASDIPAENRK---------FDFQDV--- 626
Cdd:PRK05620  106 IINHAEDEVIVADPRLAEQLGEILKEC----PCVRAVVfigpsdadsaAAHMPEGIKVYSYEalldgrstvYDWPELdet 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  627 --AYVIFTSGSTGRPKGVMNTHGSLLnlilshkptiywpvLEAVNERFPDRplrAAHTHSFSFDS--------SWLQVF- 695
Cdd:PRK05620  182 taAAICYSTGTTGAPKGVVYSHRSLY--------------LQSLSLRTTDS---LAVTHGESFLCcvpiyhvlSWGVPLa 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  696 -WM------LWGQEL------HIFDENMRRDAFGLvqeiqqrqidtldlpPSFCAQMMTNGLfvenQHHP---SL--ILI 757
Cdd:PRK05620  245 aFMsgtplvFPGPDLsaptlaKIIATAMPRVAHGV---------------PTLWIQLMVHYL----KNPPermSLqeIYV 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  758 GGEAAPLALWQQLNAQPALFAHNLYGPTEY-TVDTfraelkqTARPvignPIG-NTQAYVLDRHLQ-RCPTGV------- 827
Cdd:PRK05620  306 GGSAVPPILIKAWEERYGVDVVHVWGMTETsPVGT-------VARP----PSGvSGEARWAYRVSQgRFPASLeyrivnd 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  828 ----------IGELYISGFGIANGYL----GRADLSAARFVANPFEHGQRMY------RTGDLVRWNSAGKLEFMGRCDD 887
Cdd:PRK05620  375 gqvmestdrnEGEIQVRGNWVTASYYhsptEEGGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARD 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  888 QIKIRGYRVEIGEVENALSILTNVESAVVIAEPINN-SHRLLGYCVVKD-IELDEKTSEQLSqqylSQLRQNLPEYMVPS 965
Cdd:PRK05620  455 VIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwGERPLAVTVLAPgIEPTRETAERLR----DQLRDRLPNWMLPE 530
                         570       580       590
                  ....*....|....*....|....*....|....
gi 490930577  966 ALTVMSEFPRNVSGKVDKKALpkpqiRAHSRMAE 999
Cdd:PRK05620  531 YWTFVDEIDKTSVGKFDKKDL-----RQHLADGD 559
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
501-986 2.58e-09

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 62.23  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  501 QHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCED-------A 573
Cdd:PRK08276   10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDsgakvliV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  574 NPLFVLTTQALAQQLPQNIQQLHLDQEGVQTQIR------KQDASDIPAENRKFDFQdvayviFTSGSTGRPKGVMnthg 647
Cdd:PRK08276   90 SAALADTAAELAAELPAGVPLLLVVAGPVPGFRSyeealaAQPDTPIADETAGADML------YSSGTTGRPKGIK---- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  648 sllnlilshkptiywpvleavnerfpdRPLRAAHTHSFSFDSSWLQVFWM--------------------LWGQELH--- 704
Cdd:PRK08276  160 ---------------------------RPLPGLDPDEAPGMMLALLGFGMyggpdsvylspaplyhtaplRFGMSALalg 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  705 ---IFDEnmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQH-HPSLILIGGEAAPLAlwQQLNAQ------P 774
Cdd:PRK08276  213 gtvVVME--KFDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYdVSSLRVAIHAAAPCP--VEVKRAmidwwgP 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  775 ALfaHNLYGPTE---YTVDTFRAELKQ---TARPVIGnpigntQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADL 848
Cdd:PRK08276  289 II--HEYYASSEgggVTVITSEDWLAHpgsVGKAVLG------EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEK 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  849 SAARfvanpfEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIRGyRVEI--GEVENALSILTNVESAVVIAEPinnsHR 926
Cdd:PRK08276  361 TAAA------RNPHGWVTVGDVGYLDEDGYLYLTDRKSDMI-ISG-GVNIypQEIENLLVTHPKVADVAVFGVP----DE 428
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577  927 LLGYCVVKDIELDEKT--SEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK08276  429 EMGERVKAVVQPADGAdaGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
624-986 2.79e-09

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 62.15  E-value: 2.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  624 QDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiywpVLEAVNERFPD-------------RPLRAAHTHSFSFDSS 690
Cdd:PRK12492  207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQ--------VRACLSQLGPDgqplmkegqevmiAPLPLYHIYAFTANCM 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  691 WLqvfwMLWGQElHIFDENmRRDAFGLVQEIQQRQidtldlppsFCAQMMTNGLFVENQHHPSLILI----------GGE 760
Cdd:PRK12492  279 CM----MVSGNH-NVLITN-PRDIPGFIKELGKWR---------FSALLGLNTLFVALMDHPGFKDLdfsalkltnsGGT 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  761 A---APLALWQQLNAQPALFAhnlYGPTEYTVDTFRAELKQTAR-PVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGF 836
Cdd:PRK12492  344 AlvkATAERWEQLTGCTIVEG---YGLTETSPVASTNPYGELARlGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGP 420
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  837 GIANGYLGRADLSAARFVAnpfehgQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVV 916
Cdd:PRK12492  421 QVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAA 494
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577  917 IAEPINNSHRLLGYCVVkdieldeKTSEQLSQQYLSQL-RQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK12492  495 IGVPDERSGEAVKLFVV-------ARDPGLSVEELKAYcKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
477-983 3.27e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 62.10  E-value: 3.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  477 DIFYEQVKKYPERTAIVSgeRPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGA---- 552
Cdd:PRK12583   22 DAFDATVARFPDREALVV--RHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAilvn 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  553 ---SFLPLDLDYPI-----------------DRMQMMCEDANPLFVLTTQALA-QQLPQNIQQLHLDQE---------GV 602
Cdd:PRK12583  100 inpAYRASELEYALgqsgvrwvicadafktsDYHAMLQELLPGLAEGQPGALAcERLPELRGVVSLAPApppgflawhEL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  603 QTQIRKQDASDIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNlilshkptIYWPVLEAVNERFPDR-----PL 677
Cdd:PRK12583  180 QARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILN--------NGYFVAESLGLTEHDRlcvpvPL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  678 raahTHSFSFDSSWLQVfwMLWGQELHIFDENMrrDAFGLVQEIQQRQIDTL-DLPPSFCAQMmtnglfvenqHHP---- 752
Cdd:PRK12583  252 ----YHCFGMVLANLGC--MTVGACLVYPNEAF--DPLATLQAVEEERCTALyGVPTMFIAEL----------DHPqrgn 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  753 ----SLI--LIGGEAAPLALWQ----QLNAQPALFAhnlYGPTEYTVDTFraelkQTAR----PVIGNPIGNTQAY---- 814
Cdd:PRK12583  314 fdlsSLRtgIMAGAPCPIEVMRrvmdEMHMAEVQIA---YGMTETSPVSL-----QTTAaddlERRVETVGRTQPHlevk 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  815 VLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIkIRG- 893
Cdd:PRK12583  386 VVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMH------TGDLATMDEQGYVRIVGRSKDMI-IRGg 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  894 ---YRVEIgevENALSILTNVESAVVIAEPINNshrlLGYCVVKDIELdeKTSEQLSQQYLSQL-RQNLPEYMVPSALTV 969
Cdd:PRK12583  459 eniYPREI---EEFLFTHPAVADVQVFGVPDEK----YGEEIVAWVRL--HPGHAASEEELREFcKARIAHFKVPRYFRF 529
                         570
                  ....*....|....
gi 490930577  970 MSEFPRNVSGKVDK 983
Cdd:PRK12583  530 VDEFPMTVTGKVQK 543
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
631-983 3.71e-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: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 61.14  E-value: 3.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  631 FTSGSTGRPKGVMNTHGSLLN--------LILSHKPTIYWPVleavnerfpdrPLraahTHSFSfdsSWLQVFWML-WGQ 701
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNngyfigerLGLTEQDRLCIPV-----------PL----FHCFG---SVLGVLACLtHGA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  702 ELhIFDENMRrDAFGLVQEIQQRQIDTL-DLPPSFCAQMmtnglfvenqHHPSLI----------LIGGEAAPLALW--- 767
Cdd:cd05917    71 TM-VFPSPSF-DPLAVLEAIEKEKCTALhGVPTMFIAEL----------EHPDFDkfdlsslrtgIMAGAPCPPELMkrv 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  768 -QQLNAQPALFAhnlYGPTEYTVDTFRAELKQTARPVI---GNPIGNTQAYVLD-RHLQRCPTGVIGELYISGFGIANGY 842
Cdd:cd05917   139 iEVMNMKDVTIA---YGMTETSPVSTQTRTDDSIEKRVntvGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGY 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  843 LGRADLSAARfvanpfEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIRG----YRVEIgevENALSILTNVESAVVIA 918
Cdd:cd05917   216 WNDPEKTAEA------IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgeniYPREI---EEFLHTHPKVSDVQVVG 285
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577  919 EPinnsHRLLGYCVVKDIEL--DEKTSEQLSQQYLsqlRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:cd05917   286 VP----DERYGEEVCAWIRLkeGAELTEEDIKAYC---KGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
841-988 4.39e-09

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: 61.29  E-value: 4.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  841 GYLGRADlSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:cd05939   328 GYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVE 406
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  921 INNSHRLLGYCVVKDIEldektsEQLSQQYLSQ-LRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:cd05939   407 VPGVEGRAGMAAIVDPE------RKVDLDRFSAvLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
822-964 5.08e-09

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: 61.22  E-value: 5.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  822 RCPTGVIGEL--YISGFGIANGYLGRADlSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIG 899
Cdd:cd05940   281 KVPRGEPGLLisRINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTT 359
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577  900 EVENALSILTNVESAVVIAEPINNSHrllGYCVVKDIELDEKTSEQLSQqyLSQ-LRQNLPEYMVP 964
Cdd:cd05940   360 EVAAVLGAFPGVEEANVYGVQVPGTD---GRAGMAAIVLQPNEEFDLSA--LAAhLEKNLPGYARP 420
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
625-994 5.83e-09

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 61.35  E-value: 5.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHkptiywpvLEAVNERFPDRPLRAA---HTHSFSfdsswlQVFWMLWGQ 701
Cdd:PLN02860  173 DAVLICFTSGTTGRPKGVTISHSALIVQSLAK--------IAIVGYGEDDVYLHTAplcHIGGLS------SALAMLMVG 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  702 ELHIFDENMrrDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQH-HPSL--ILIGGEAAPLALWQ---QLNAQPA 775
Cdd:PLN02860  239 ACHVLLPKF--DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKvFPSVrkILNGGGSLSSRLLPdakKLFPNAK 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  776 LFAhnLYGPTE------------YTVDTFRAELKQTARPV-------IGNPIGNTQAYVldrHLQRCPTGV--IGELYIS 834
Cdd:PLN02860  317 LFS--AYGMTEacssltfmtlhdPTLESPKQTLQTVNQTKsssvhqpQGVCVGKPAPHV---ELKIGLDESsrVGRILTR 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  835 GFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESA 914
Cdd:PLN02860  392 GPHVMLGYWGQNSETASVLSNDGW------LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASV 465
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  915 VVIAEPinnSHRlLGYCVVKDIEL------------DEKTSEQLSQQYLSQ--LRQNLPEYMVPSALTVMSE-FPRNVSG 979
Cdd:PLN02860  466 VVVGVP---DSR-LTEMVVACVRLrdgwiwsdnekeNAKKNLTLSSETLRHhcREKNLSRFKIPKLFVQWRKpFPLTTTG 541
                         410
                  ....*....|....*
gi 490930577  980 KVdKKALPKPQIRAH 994
Cdd:PLN02860  542 KI-RRDEVRREVLSH 555
PLN03102 PLN03102
acyl-activating enzyme; Provisional
828-992 5.87e-09

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 61.19  E-value: 5.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  828 IGELYISGFGIANGYLgradlSAARFVANPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSI 907
Cdd:PLN03102  392 MGEIVIKGSSIMKGYL-----KNPKATSEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYK 464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  908 LTNVESAVVIAEPinnsHRLLGY--CVVKDIELDEKTSEQLSQQYLSQ-------LRQNLPEYMVPSALTVMSEFPRNVS 978
Cdd:PLN03102  465 YPKVLETAVVAMP----HPTWGEtpCAFVVLEKGETTKEDRVDKLVTRerdlieyCRENLPHFMCPRKVVFLQELPKNGN 540
                         170
                  ....*....|....
gi 490930577  979 GKVdkkalPKPQIR 992
Cdd:PLN03102  541 GKI-----LKPKLR 549
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1004-1062 7.89e-09

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: 53.72  E-value: 7.89e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577  1004 QLLCQITASVLKLDA--IGIDDDFFMTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAA 1062
Cdd:pfam00550    1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
805-988 7.89e-09

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: 60.79  E-value: 7.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  805 GNPIGNTQAYVLDRHLQRCPTGVIGELYISGfGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGR 884
Cdd:cd05967   414 GKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGR 492
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  885 CDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIAEPINNSHRLLGYCVVKdiELDEKTSEQLSQQYLSQLRQNLPEYMV 963
Cdd:cd05967   493 TDDVINVAGHRLSTGEMEESVLSHPAVaECAVVGVRDELKGQVPLGLVVLK--EGVKITAEELEKELVALVREQIGPVAA 570
                         170       180
                  ....*....|....*....|....*
gi 490930577  964 PSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:cd05967   571 FRLVIFVKRLPKTRSGKILRRTLRK 595
PRK03584 PRK03584
acetoacetate--CoA ligase;
1535-1772 1.68e-08

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 59.81  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1535 QQLLREQAritPEQTAL--SDENH---QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILA-------- 1601
Cdd:PRK03584   90 ENLLRHRR---DDRPAIifRGEDGprrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLAtaslgaiw 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1602 -----------VIE-----------AGAAYL----PIDLqhpTERIKFMLQDAKS--KLVIGEQKDLAAIVHPSIATFAF 1653
Cdd:PRK03584  167 sscspdfgvqgVLDrfgqiepkvliAVDGYRyggkAFDR---RAKVAELRAALPSleHVVVVPYLGPAAAAAALPGALLW 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1654 NELfdetkvdLSSYKTTVITPQ-----HPAYLIYTSGTTGQPKGVMVSHQAIV-NRILWMQSEYPLSATDTILQKTPCTf 1727
Cdd:PRK03584  244 EDF-------LAPAEAAELEFEpvpfdHPLWILYSSGTTGLPKCIVHGHGGILlEHLKELGLHCDLGPGDRFFWYTTCG- 315
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1728 dvsvWeFFWSYLV-----GARLVI---APidAHRDPLALLSLIQKYQVTtlHF 1772
Cdd:PRK03584  316 ----W-MMWNWLVsgllvGATLVLydgSP--FYPDPNVLWDLAAEEGVT--VF 359
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1678-2031 1.91e-08

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 58.90  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 AYLIYTSGTTGQPKGVMVSHQAIVNrilwmqseyplSATDT---------ILQKTPCTFDVSVWEFFWSYLVGARLVIAP 1748
Cdd:PRK07824   38 ALVVATSGTTGTPKGAMLTAAALTA-----------SADAThdrlggpgqWLLALPAHHIAGLQVLVRSVIAGSEPVELD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 IDAHRDPLALLSLIQ------KYqvTTLhfVPSML--AVFENAATEILSSaqrqslpICRVFCSGEALPTALAKSftehf 1820
Cdd:PRK07824  107 VSAGFDPTALPRAVAelgggrRY--TSL--VPMQLakALDDPAATAALAE-------LDAVLVGGGPAPAPVLDA----- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1821 scelhnlygPTEAAVDV--SY-MDATLGlhpeeSCVAIGYPVWNTQLYIldqylrpvpvgVDGELYLAGHQLAMGYLHRA 1897
Cdd:PRK07824  171 ---------AAAAGINVvrTYgMSETSG-----GCVYDGVPLDGVRVRV-----------EDGRIALGGPTLAKGYRNPV 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1898 DltasrfvaNPFTAGQRMYRTGDIARWHaDGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKA 1976
Cdd:PRK07824  226 D--------PDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVaDCAVFGLPDDRLGQ 296
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 1977 NVqLVAYLQTTAPVD-IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK07824  297 RV-VAAVVGDGGPAPtLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
997-1064 3.05e-08

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: 52.55  E-value: 3.05e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577  997 MAETPEQQLLCQITASVLKLDA--IGIDDDFFMT-GGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMA 1064
Cdd:COG0236     1 MPREELEERLAEIIAEVLGVDPeeITPDDSFFEDlGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLA 72
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
1558-2031 3.22e-08

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 58.67  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRagvQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:PRK06334   46 LSYNQVRKAVIALATKVSK---YPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSK 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 K--DLAAIVHPSIATFAFNELFDET---------KVDLSSYKTTVIT------------PQHPAYLIYTSGTTGQPKGVM 1694
Cdd:PRK06334  123 QlmQHLAQTHGEDAEYPFSLIYMEEvrkelsfweKCRIGIYMSIPFEwlmrwfgvsdkdPEDVAVILFTSGTEKLPKGVP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQA-IVNRILWMQSEYPLSaTDTILQKTP---------CTFdvsvweffWSYLVGARLVIA--PIDAHRdplaLLSLI 1762
Cdd:PRK06334  203 LTHANlLANQRACLKFFSPKE-DDVMMSFLPpfhaygfnsCTL--------FPLLSGVPVVFAynPLYPKK----IVEMI 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1763 QKYQVTTLHFVPSMLAVfenaateILSSAQRQ--SLPICR-VFCSGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVS 1838
Cdd:PRK06334  270 DEAKVTFLGSTPVFFDY-------ILKTAKKQesCLPSLRfVVIGGDAFKDSLYQEALKTFpHIQLRQGYGTTECSPVIT 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1839 YMDATLGLHpeESCVaiGYPVWNTQLYILDQYLR-PVPVGVDGELYLAGHQLAMGYLHrADLTASrFVAnpfTAGQRMYR 1917
Cdd:PRK06334  343 INTVNSPKH--ESCV--GMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLG-EDFGQG-FVE---LGGETWYV 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1918 TGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD-------VVVHAISSEQnkanVQLVayLQTTAPV 1990
Cdd:PRK06334  414 TGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNaadhagpLVVCGLPGEK----VRLC--LFTTFPT 487
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 490930577 1991 DIDQLKKQLAKHLPAYMVPTHYM-LVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06334  488 SISEVNDILKNSKTSSILKISYHhQVESIPMLGTGKPDYCSL 529
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
90-340 3.50e-08

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: 58.37  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   90 QVQFQIEEFDFCHLTPKKAQQRLWDWMPSDRQcaKSLKAGETQLFRQVLFTTHDKVYWY-QRYHHIMLDGFSMINLTKRI 168
Cdd:cd19543    74 DRKLPWRELDLSHLSEAEQEAELEALAEEDRE--RGFDLARAPLMRLTLIRLGDDRYRLvWSFHHILLDGWSLPILLKEL 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  169 VELYQQLQEGKDLS---VSPFigvneviSERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHHLA-AKTTATFVKHQLR 244
Cdd:cd19543   152 FAIYAALGEGQPPSlppVRPY-------RDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPAdADGSYEPGEVSFE 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  245 FSTGILEQIQALAAQTKLALNDMMM---SLSLHyiyKMTDKAELVNGI-----PfmrrlgskairSTLPTV--------N 308
Cdd:cd19543   225 LSAELTARLQELARQHGVTLNTVVQgawALLLS---RYSGRDDVVFGTtvsgrP-----------AELPGIetmvglfiN 290
                         250       260       270
                  ....*....|....*....|....*....|..
gi 490930577  309 VLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQ 340
Cdd:cd19543   291 TLPVRVRLDPDQTVLELLKDLQAQQLELREHE 322
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
474-981 4.03e-08

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: 58.73  E-value: 4.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  474 NVLDifyEQVKKYPERTAIV-SGERPN-LQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVML------ 545
Cdd:cd05966    57 NCLD---RHLKERGDKVAIIwEGDEPDqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLacarig 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  546 ---SVLNSGASFLPLdldypIDRMqmmcEDANPLFVLTT-----------------QALaQQLP--QNI---QQLHLD-- 598
Cdd:cd05966   134 avhSVVFAGFSAESL-----ADRI----NDAQCKLVITAdggyrggkviplkeivdEAL-EKCPsvEKVlvvKRTGGEvp 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  599 -QEGV----QTQIRKQDAsDIPAEnrKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLnlilshkptiywpvleavnerfp 673
Cdd:cd05966   204 mTEGRdlwwHDLMAKQSP-ECEPE--WMDSEDPLFILYTSGSTGKPKGVVHTTGGYL----------------------- 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  674 drpLRAAHTHSFSFDSSWLQVFW------------------MLWGQELHIFDENMRRDAFGLVQEIQQR-QIDTLDLPPS 734
Cdd:cd05966   258 ---LYAATTFKYVFDYHPDDIYWctadigwitghsyivygpLANGATTVMFEGTPTYPDPGRYWDIVEKhKVTIFYTAPT 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  735 FCAQMMTNG-LFVENQHHPSLILIG--GEaaPLalwqqlNAQPALFAHNLYGPTEYT-VDTFRaelkQT----------- 799
Cdd:cd05966   335 AIRALMKFGdEWVKKHDLSSLRVLGsvGE--PI------NPEAWMWYYEVIGKERCPiVDTWW----QTetggimitplp 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  800 ----------ARPVIGnpignTQAYVLDRHLQRCPTGVIGELYISGF--GIANGYLGradlSAARFVANPFEHGQRMYRT 867
Cdd:cd05966   403 gatplkpgsaTRPFFG-----IEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYG----DHERYEDTYFSKFPGYYFT 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  868 GDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLG-----YCVVKDielDEKT 942
Cdd:cd05966   474 GDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRP----HDIKGeaiyaFVTLKD---GEEP 546
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 490930577  943 SEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKV 981
Cdd:cd05966   547 SDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKI 585
PRK07529 PRK07529
AMP-binding domain protein; Validated
604-992 4.17e-08

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 58.81  E-value: 4.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  604 TQIRKQDASDIPAEnRKFDFQDVAYVIFTSGSTGRPKGVMNTHGS------LLNLILSHKP--TIYWPV-LEAVNerfpd 674
Cdd:PRK07529  194 AELARQPGDRLFSG-RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNevanawLGALLLGLGPgdTVFCGLpLFHVN----- 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  675 rplrAAHTHSFSFDSSWLQVfwmLWGQELHIFDENMRRDAFGLVQeiqQRQIDTLDLPPSFCAQMM---TNGLFVEnqhh 751
Cdd:PRK07529  268 ----ALLVTGLAPLARGAHV---VLATPQGYRGPGVIANFWKIVE---RYRINFLSGVPTVYAALLqvpVDGHDIS---- 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  752 pSL-ILIGGEAA-PLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARP-VIGNPIGNTQAYVL-----DRHLQRC 823
Cdd:PRK07529  334 -SLrYALCGAAPlPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIgSVGLRLPYQRVRVVilddaGRYLRDC 412
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  824 PTGVIGELYISGFGIANGYLgRADLSAARFVanpfehGQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIR-GYRVEIGEVE 902
Cdd:PRK07529  413 AVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL------EDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIE 484
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  903 NALSILTNVESAVVIAEPinNSHRllGYCVVKDIELDEKTSEQlSQQYLSQLRQNLPE-YMVPSALTVMSEFPRNVSGKV 981
Cdd:PRK07529  485 EALLRHPAVALAAAVGRP--DAHA--GELPVAYVQLKPGASAT-EAELLAFARDHIAErAAVPKHVRILDALPKTAVGKI 559
                         410
                  ....*....|.
gi 490930577  982 DKKALPKPQIR 992
Cdd:PRK07529  560 FKPALRRDAIR 570
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
2138-2232 6.20e-08

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 56.01  E-value: 6.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2138 RSGSGHPLFCFYPGSGSAWQYTVLNRYLHSDLPIIGLQSP-----RPDGLLansTDMDELVEKQLEIMRkQQPTGPYTLL 2212
Cdd:COG3208     2 RPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPgrgdrLGEPPL---TSLEELADDLAEELA-PLLDRPFALF 77
                          90       100
                  ....*....|....*....|
gi 490930577 2213 GYSLGGTVAYAVAAKLTEQG 2232
Cdd:COG3208    78 GHSMGALLAFELARRLERRG 97
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
488-655 8.22e-08

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 57.83  E-value: 8.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  488 ERTAIVSGERPNLQHLSFAE----LAVKV--NQLTRFLQENGARKQTV------IAGAIPRSIDSVVVMLSVLNSGASFL 555
Cdd:PRK12476   41 ERNIANVGDTVAYRYLDHSHsaagCAVELtwTQLGVRLRAVGARLQQVagpgdrVAILAPQGIDYVAGFFAAIKAGTIAV 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  556 PL---DLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQNIQQL-HLDQEGVQT--QIRKQDASD-IPAEnrkFDFQDVAY 628
Cdd:PRK12476  121 PLfapELPGHAERLDTALRDAEPTVVLTTTAAAEAVEGFLRNLpRLRRPRVIAidAIPDSAGESfVPVE---LDTDDVSH 197
                         170       180       190
                  ....*....|....*....|....*....|.
gi 490930577  629 VIFTSGSTGRPKGVMNTHGS----LLNLILS 655
Cdd:PRK12476  198 LQYTSGSTRPPVGVEITHRAvgtnLVQMILS 228
PLN02614 PLN02614
long-chain acyl-CoA synthetase
1667-1965 8.51e-08

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 57.72  E-value: 8.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1667 YKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRI-----LWMQSEYPLSATDTILQKTPCT--FDVSVWEFFWSyl 1739
Cdd:PLN02614  215 YDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIagvirLLKSANAALTVKDVYLSYLPLAhiFDRVIEECFIQ-- 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1740 VGARLVIAPIDAHrdplALLSLIQKYQVTTLHFVPSML-------------------AVFENAATEILSSAQR-----QS 1795
Cdd:PLN02614  293 HGAAIGFWRGDVK----LLIEDLGELKPTIFCAVPRVLdrvysglqkklsdggflkkFVFDSAFSYKFGNMKKgqshvEA 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1796 LPIC----------------RVFCSGEALPTALAKSFTEHFSCeLHNL--YGPTEAAVdvsymdATLGLHPEESCV--AI 1855
Cdd:PLN02614  369 SPLCdklvfnkvkqglggnvRIILSGAAPLASHVESFLRVVAC-CHVLqgYGLTESCA------GTFVSLPDELDMlgTV 441
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1856 GYPVWNtqlyiLDQYLRPVP-VGVD-------GELYLAGHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIARWHAD 1927
Cdd:PLN02614  442 GPPVPN-----VDIRLESVPeMEYDalastprGEICIRGKTLFSGYYKREDLTKEVLIDG-------WLHTGDVGEWQPN 509
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 490930577 1928 GSIQYIGRADDQLKI-RGQRIELGEIEQQLRLISGLDVV 1965
Cdd:PLN02614  510 GSMKIIDRKKNIFKLsQGEYVAVENIENIYGEVQAVDSV 548
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
1519-2039 8.92e-08

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 57.30  E-value: 8.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1519 IQKTNQTQYYVR----------QSTLQQLLREQARITPEQTALSDE--NHQLSFSEVRLQVCALAQQLQRAGVQAGDIVA 1586
Cdd:PLN02330    5 IQKQEDNEHIFRsrypsvpvpdKLTLPDFVLQDAELYADKVAFVEAvtGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1587 VALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVI------GEQKDLAAIV----HPSIAT-FAFNE 1655
Cdd:PLN02330   85 VVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVtndtnyGKVKGLGLPVivlgEEKIEGaVNWKE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1656 LFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILwmqSEYPLSATDTILQKTpctfDVSVWEFF 1735
Cdd:PLN02330  165 LLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLC---SSLFSVGPEMIGQVV----TLGLIPFF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1736 WSYLV-----------GARLVIAPIDAHrdplALLSLIQKYQVTTLHFVPS-MLAVFENAATEILSSAQrqsLPICRVFC 1803
Cdd:PLN02330  238 HIYGItgiccatlrnkGKVVVMSRFELR----TFLNALITQEVSFAPIVPPiILNLVKNPIVEEFDLSK---LKLQAIMT 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1804 SGEALPTALAKSFTEHF-SCELHNLYGPTE-AAVDVSYMDATLGlHPEESCVAIGYPVWNTQLYILD-QYLRPVPVGVDG 1880
Cdd:PLN02330  311 AAAPLAPELLTAFEAKFpGVQVQEAYGLTEhSCITLTHGDPEKG-HGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1881 ELYLAGHQLAMGYLHRADLTASRFVAnpftagQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLIS 1960
Cdd:PLN02330  390 ELCVRSQCVMQGYYNNKEETDRTIDE------DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHP 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1961 GL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPS 2039
Cdd:PLN02330  464 SVeDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSIN 543
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
487-986 1.44e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 56.56  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGERPnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGA-------SFLPLDL 559
Cdd:PRK13390   11 PDRPAVIVAETG--EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLyitainhHLTAPEA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  560 DYpidrmqMMCEDANPLFVLTT--QALAQQLPQNIQqLHLDQEGVQTQIRKQDASDIPAENRKFDFQDVAYVIFTSGSTG 637
Cdd:PRK13390   89 DY------IVGDSGARVLVASAalDGLAAKVGADLP-LRLSFGGEIDGFGSFEAALAGAGPRLTEQPCGAVMLYSSGTTG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  638 RPKGVMnthgsllnlilshkptiywPVLEAVNERFPDRPLRAAHTHSFSFDSSwlQVFW----------MLWGQELHIFD 707
Cdd:PRK13390  162 FPKGIQ-------------------PDLPGRDVDAPGDPIVAIARAFYDISES--DIYYssapiyhaapLRWCSMVHALG 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  708 ENM----RRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHH-PSLILIGGEAAPL------ALWQQLNaqPAL 776
Cdd:PRK13390  221 GTVvlakRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDvSSLRAVIHAAAPCpvdvkhAMIDWLG--PIV 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  777 FAHnlYGPTEY----TVDT--FRAELKQTARPVIGNpigntqAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSA 850
Cdd:PRK13390  299 YEY--YSSTEAhgmtFIDSpdWLAHPGSVGRSVLGD------LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTA 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  851 -ARFVANPFehgqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNshrlLG 929
Cdd:PRK13390  371 aAQHPAHPF-----WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPE----MG 441
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  930 YCVVKDIELDE--KTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK13390  442 EQVKAVIQLVEgiRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
1525-1942 1.63e-07

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: 56.69  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1525 TQYYVRQSTLQQLLReqaRITpeqtalsdenhqLSFSEVRLQVCALAQQLQ-RAGVQAGDIVAVALPRSVKLSIAILAVI 1603
Cdd:cd17632    50 TDPATGRTTLRLLPR---FET------------ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALT 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1604 EAGAAYLPIDLQHPTERIKFMLQDAKSKL--VIGEQKDLA------AIVHPSIATFAFNELFDETKVDLSSYKT------ 1669
Cdd:cd17632   115 RLGAVSVPLQAGASAAQLAPILAETEPRLlaVSAEHLDLAveavleGGTPPRLVVFDHRPEVDAHRAALESARErlaavg 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1670 -TVIT----------------------PQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSE---YPLSAtdTILQKT 1723
Cdd:cd17632   195 iPVTTltliavrgrdlppaplfrpepdDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIqdiRPPAS--ITLNFM 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1724 PCTfdvSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVP---SML-------------------AVFE 1781
Cdd:cd17632   273 PMS---HIAGRISLYGTLARGGTAYFAAASDMSTLFDDLALVRPTELFLVPrvcDMLfqryqaeldrrsvagadaeTLAE 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1782 NAATEIlssaqRQSLPICRV---FCSGEALpTALAKSFTEH-FSCELHNLYGPTEAAVDV--------SYMDATLGLHPE 1849
Cdd:cd17632   350 RVKAEL-----RERVLGGRLlaaVCGSAPL-SAEMKAFMESlLDLDLHDGYGSTEAGAVIldgvivrpPVLDYKLVDVPE 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 escvaIGYpvwntqlYILDqylRPVPvgvDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDI-ARWHADg 1928
Cdd:cd17632   424 -----LGY-------FRTD---RPHP---RGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVmAELGPD- 478
                         490
                  ....*....|....
gi 490930577 1929 SIQYIGRADDQLKI 1942
Cdd:cd17632   479 RLVYVDRRNNVLKL 492
PLN02654 PLN02654
acetate-CoA ligase
503-988 1.73e-07

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 56.83  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQ 582
Cdd:PLN02654  121 LTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCN 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  583 ALAQQLP----QNIQQLHLD---QEGVQTQI--RKQDASDIPAENRKF------------------------DFQDVAYV 629
Cdd:PLN02654  201 AVKRGPKtinlKDIVDAALDesaKNGVSVGIclTYENQLAMKREDTKWqegrdvwwqdvvpnyptkcevewvDAEDPLFL 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  630 IFTSGSTGRPKGVMNTHGSLLnlilshkptIYwpvleavnerfpdrplrAAHTHSFSFDSSWLQVFW------------- 696
Cdd:PLN02654  281 LYTSGSTGKPKGVLHTTGGYM---------VY-----------------TATTFKYAFDYKPTDVYWctadcgwitghsy 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  697 -----MLWGQELHIFDENMRRDAFGLVQEIQQR-QIDTLDLPPSFCAQMMTNGL-FVENQHHPSLILIGGEAAPLalwqq 769
Cdd:PLN02654  335 vtygpMLNGATVLVFEGAPNYPDSGRCWDIVDKyKVTIFYTAPTLVRSLMRDGDeYVTRHSRKSLRVLGSVGEPI----- 409
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  770 lNAQPALFAHNLYGPTEYTV-DTFRaelkQTAR------PVIGN----------PIGNTQAYVLDRHLQRCPTGVIGELY 832
Cdd:PLN02654  410 -NPSAWRWFFNVVGDSRCPIsDTWW----QTETggfmitPLPGAwpqkpgsatfPFFGVQPVIVDEKGKEIEGECSGYLC 484
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  833 ISGF--GIANGYLGRADlsaaRFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENAL-SILT 909
Cdd:PLN02654  485 VKKSwpGAFRTLYGDHE----RYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALvSHPQ 560
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  910 NVESAVVIAEpinnsHRLLGYCVVKDIELDEKT--SEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:PLN02654  561 CAEAAVVGIE-----HEVKGQGIYAFVTLVEGVpySEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635

                  .
gi 490930577  988 K 988
Cdd:PLN02654  636 K 636
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
1892-2031 1.98e-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: 56.28  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 GYLHRADlTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAIS 1970
Cdd:cd05939   328 GYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLeDVVVYGVE 406
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1971 SEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05939   407 VPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
491-996 2.22e-07

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 56.25  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  491 AIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMC 570
Cdd:PRK12406    4 TIISGDR----RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  571 EDANPLfVLTTQA-----LAQQLPQNIQQL------------------------HLDQEGVQTQIRKQDASDIPAEnrkf 621
Cdd:PRK12406   80 EDSGAR-VLIAHAdllhgLASALPAGVTVLsvptppeiaaayrispalltppagAIDWEGWLAQQEPYDGPPVPQP---- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  622 dfqdvAYVIFTSGSTGRPKGVmnthgsllnlilshkptiywpvleavnERFPDRPLRAAhthsfsfdsSWLQVFWMLWGQ 701
Cdd:PRK12406  155 -----QSMIYTSGTTGHPKGV---------------------------RRAAPTPEQAA---------AAEQMRALIYGL 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  702 ELHI----------------------FDENM----RRDAFGLVQEIQQRQIDT-----------LDLPPSFCAQMMTNGL 744
Cdd:PRK12406  194 KPGIralltgplyhsapnayglragrLGGVLvlqpRFDPEELLQLIERHRITHmhmvptmfirlLKLPEEVRAKYDVSSL 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  745 fvenqhhpSLILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRC 823
Cdd:PRK12406  274 --------RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSEDALSHPgTVGKAAPGAELRFVDEDGRPL 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  824 PTGVIGELYISGFGIAN-GYLG----RADLSAARFVAnpfehgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEI 898
Cdd:PRK12406  346 PQGEIGEIYSRIAGNPDfTYHNkpekRAEIDRGGFIT-----------SGDVGYLDADGYLFLCDRKRDMVISGGVNIYP 414
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  899 GEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIELDEKTSeqLSQQYL-SQLRQNLPEYMVPSALTVMSEFPRNV 977
Cdd:PRK12406  415 AEIEAVLHAVPGVHDCAVFGIP----DAEFGEALMAVVEPQPGAT--LDEADIrAQLKARLAGYKVPKHIEIMAELPRED 488
                         570
                  ....*....|....*....
gi 490930577  978 SGKVDKKALPKPQIRAHSR 996
Cdd:PRK12406  489 SGKIFKRRLRDPYWANAGR 507
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
502-650 2.66e-07

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: 55.53  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  502 HLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTT 581
Cdd:cd05914     7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  582 qalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGSTGRPKGVMNTHGSLL 650
Cdd:cd05914    87 ----------------------------------------DEDDVALINYTSGTTGNSKGVMLTYRNIV 115
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1674-2027 3.20e-07

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 55.87  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1674 PQHP---AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPC--TFDVSVwEFFWSYLVGARLVIAP 1748
Cdd:PRK08043  361 KQQPedaALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYP 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 IDAHrdplallsliqkYQVttlhfVPSMlaVFENAATEI------LSSAQRQSLP-----ICRVFCSGEALPTALAKSFT 1817
Cdd:PRK08043  440 SPLH------------YRI-----VPEL--VYDRNCTVLfgtstfLGNYARFANPydfarLRYVVAGAEKLQESTKQLWQ 500
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1818 EHFSCELHNLYGPTEAAvdvsymdatlglhpeeSCVAIGYPVW---NTQLYIL---DQYLRPVPvGVD--GELYLAGHQL 1889
Cdd:PRK08043  501 DKFGLRILEGYGVTECA----------------PVVSINVPMAakpGTVGRILpgmDARLLSVP-GIEqgGRLQLKGPNI 563
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1890 AMGYLHradltasrfVANPF---------TAGQR---MYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLR 1957
Cdd:PRK08043  564 MNGYLR---------VEKPGvlevptaenARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLAL 634
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1958 LISGLDvvVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKH-LPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:PRK08043  635 GVSPDK--QHATAIKSDASKGEALVLFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
1908-2033 3.55e-07

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 55.39  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1908 PFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRlISGL--DVVVHAISSEQnkANVQLVA-YL 1984
Cdd:PRK07445  318 QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAIL-ATGLvqDVCVLGLPDPH--WGEVVTAiYV 394
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 490930577 1985 QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK07445  395 PKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2051-2120 3.83e-07

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: 49.47  E-value: 3.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 2051 EHELTRIFQQILNTD-QNIGVNEDFFA-IGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQ 2120
Cdd:COG0236     7 EERLAEIIAEVLGVDpEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
483-986 3.97e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 55.08  E-value: 3.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  483 VKKYPERTAIV---SGERpnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSG------AS 553
Cdd:PRK13391    7 AQTTPDKPAVImasTGEV-----VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGlyytcvNS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  554 FL-PLDLDYPIDrmqmmceDANPLFVLTTQA-------LAQQLPQNIQQLHLDQ-------EGVQTQIRKQDASDIPAEN 618
Cdd:PRK13391   82 HLtPAEAAYIVD-------DSGARALITSAAkldvaraLLKQCPGVRHRLVLDGdgelegfVGYAEAVAGLPATPIADES 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  619 RKFDFQdvayviFTSGSTGRPKGVMnthGSLLNLILSHKPTIYWPVLEAVNERFPDRPLRAA---HTHSFSFDSSWLQVf 695
Cdd:PRK13391  155 LGTDML------YSSGTTGRPKGIK---RPLPEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAplyHSAPQRAVMLVIRL- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  696 wmlwGQELHIFDenmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGEAA---PLALWQQLNA 772
Cdd:PRK13391  225 ----GGTVIVME---HFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAapcPPQVKEQMID 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  773 QPALFAHNLYGPTEYTVDTF-RAE--LKQ---TARPVIGNPigntqaYVLDRHLQRCPTGVIGELYISGfGIANGYLGRA 846
Cdd:PRK13391  298 WWGPIIHEYYAATEGLGFTAcDSEewLAHpgtVGRAMFGDL------HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDP 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  847 DLSAARFVANPfehgqRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHR 926
Cdd:PRK13391  371 AKTAEARHPDG-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVP----NE 441
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577  927 LLG---YCVVKDIELDEKTSEqLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK13391  442 DLGeevKAVVQPVDGVDPGPA-LAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
629-920 4.03e-07

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: 54.62  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  629 VIFTSGSTGRPKGVMNTHGSLLnlilshkptiywpvLEAVNerfpdrplrAAHTHSFSFDSSWLQV-------FWMLWGQ 701
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALL--------------AQALV---------LAVLQAIDEGTVFLNSgplfhigTLMFTLA 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  702 ELHIFDEN--MRR-DAFGLVQEIQQRQIDTLDLPPSFCAQMMTnglFVENQHHPSLILIGGEAAPLalWQQL-NAQPALF 777
Cdd:cd17636    62 TFHAGGTNvfVRRvDAEEVLELIEAERCTHAFLLPPTIDQIVE---LNADGLYDLSSLRSSPAAPE--WNDMaTVDTSPW 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  778 AHNL--YGPTEYT-VDTFRAeLKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFV 854
Cdd:cd17636   137 GRKPggYGQTEVMgLATFAA-LGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577  855 AnpfehgqRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:cd17636   216 G-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVP 274
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1102-1260 4.35e-07

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: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1102 PLLPLQKgMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQL--------GGH--FDSELAEEPVFIYSL 1171
Cdd:cd19534     3 PLTPIQR-WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALrmrfrredGGWqqRIRGDVEELFRLEVV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1172 hptqawpvqfcSVTPDLLEQTIQEA---LQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIK 1247
Cdd:cd19534    82 -----------DLSSLAQAAAIEALaaeAQSSLDLEEgP--LLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEA 148
                         170
                  ....*....|....
gi 490930577 1248 AYQQ-TNQQLPVLE 1260
Cdd:cd19534   149 AYEQaLAGEPIPLP 162
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
474-918 7.79e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 54.67  E-value: 7.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  474 NVLDIFYEQVKKYPERTAIVSGERPNLQ--HLSFAELAVKVNQLTRFLQENGA---RKQTVIAGaipRSIDSVVVMLSVL 548
Cdd:PRK12582   50 SIPHLLAKWAAEAPDRPWLAQREPGHGQwrKVTYGEAKRAVDALAQALLDLGLdpgRPVMILSG---NSIEHALMTLAAM 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  549 NSGASFLPLDLDYpidrmQMMCEDANPL---FVLTTQAL--AQQLPQNIQQLH-LDQEGVQTQIRKQDASDIPAenrkFD 622
Cdd:PRK12582  127 QAGVPAAPVSPAY-----SLMSHDHAKLkhlFDLVKPRVvfAQSGAPFARALAaLDLLDVTVVHVTGPGEGIAS----IA 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  623 FQD---------------------VAYVIFTSGSTGRPKGVMNTHGSLLNLIlshkptiywPVLEAVNERFPDRPlraah 681
Cdd:PRK12582  198 FADlaatpptaavaaaiaaitpdtVAKYLFTSGSTGMPKAVINTQRMMCANI---------AMQEQLRPREPDPP----- 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  682 tHSFSFDsswlqvfWMLW----------------GQELHI---------FDENMR--RD----AFGLVQEIQQRQIDTLD 730
Cdd:PRK12582  264 -PPVSLD-------WMPWnhtmggnanfngllwgGGTLYIddgkplpgmFEETIRnlREisptVYGNVPAGYAMLAEAME 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  731 LPPSFCAQMMTNglfvenqhhPSLILIGGEAAPLALWQQLNAQP-ALFAHNL-----YGPTE---YTVDTFRAelkqTAR 801
Cdd:PRK12582  336 KDDALRRSFFKN---------LRLMAYGGATLSDDLYERMQALAvRTTGHRIpfytgYGATEtapTTTGTHWD----TER 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  802 P-VIGNPIGNTQayvldrhLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRW----NSA 876
Cdd:PRK12582  403 VgLIGLPLPGVE-------LKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFvdpdDPE 469
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 490930577  877 GKLEFMGRCDDQIKI-RGYRVEIGEVE-NALSILTNVESAVVIA 918
Cdd:PRK12582  470 KGLIFDGRVAEDFKLsTGTWVSVGTLRpDAVAACSPVIHDAVVA 513
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
829-986 9.04e-07

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 53.51  E-value: 9.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  829 GELYISGFGIANGYLGRADlsaarfvANPF-EHGqrMYRTGDLVRWNSaGKLEFMGRCDDQIKIRGYRVEIGEVENALSI 907
Cdd:PRK07824  208 GRIALGGPTLAKGYRNPVD-------PDPFaEPG--WFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALAT 277
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  908 LTNVESAVVIAEPinnsHRLLGYCVVKDIELDEKTSEQLSQqYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK07824  278 HPAVADCAVFGLP----DDRLGQRVVAAVVGDGGPAPTLEA-LRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
1570-1806 1.16e-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: 53.89  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQ-RAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLV-------IGEQKDLA 1641
Cdd:cd05905    27 IAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVAltveaclKGLPKKLL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1642 AIVHPS-IATF-AFNELFDETKVDLS-SYKTTVITPQHP------AYLIYTSGTTGQPKGVMVSHQAIVN--RILWMQSE 1710
Cdd:cd05905   107 KSKTAAeIAKKkGWPKILDFVKIPKSkRSKLKKWGPHPPtrdgdtAYIEYSFSSDGSLSGVAVSHSSLLAhcRALKEACE 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1711 YplSATDTILQKTPCTFDVSVWefFW---SYLVGAR-LVIAPIDAHRDPLALLSLIQKYQVTTLhFVPS--MLAVFENAA 1784
Cdd:cd05905   187 L--YESRPLVTVLDFKSGLGLW--HGcllSVYSGHHtILIPPELMKTNPLLWLQTLSQYKVRDA-YVKLrtLHWCLKDLS 261
                         250       260
                  ....*....|....*....|....*.
gi 490930577 1785 TEILSSAQR----QSLPICRVFCSGE 1806
Cdd:cd05905   262 STLASLKNRdvnlSSLRMCMVPCENR 287
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
476-920 1.28e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 53.75  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  476 LDIFYEQVKKYPE-----RTAI--VSGERPnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVL 548
Cdd:PRK04319   42 VNIAYEAIDRHADggrkdKVALryLDASRK--EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGAL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  549 NSGASFLPLDLDY---PI-DRMqmmcEDANPLFVLTTQAL-----AQQLPQNIQQLHLDQEG------VQTQIRKQDASD 613
Cdd:PRK04319  120 KNGAIVGPLFEAFmeeAVrDRL----EDSEAKVLITTPALlerkpADDLPSLKHVLLVGEDVeegpgtLDFNALMEQASD 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  614 ---IPAENRkfdfQDVAYVIFTSGSTGRPKGVMNTHgsllNLILSHKPTIYWpVLEavnerfpdrpLRAAhthsfsfdss 690
Cdd:PRK04319  196 efdIEWTDR----EDGAILHYTSGSTGKPKGVLHVH----NAMLQHYQTGKY-VLD----------LHED---------- 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  691 wlQVFWM-------------LWGQELH----IFDENmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHH-P 752
Cdd:PRK04319  247 --DVYWCtadpgwvtgtsygIFAPWLNgatnVIDGG-RFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDlS 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  753 SL--ILIGGEaaPL---ALW--QQLNAQPalfAHNLYGPTE---YTVDTFRAelkQTARP-VIGNPIGNTQAYVLDRHLQ 821
Cdd:PRK04319  324 SLrhILSVGE--PLnpeVVRwgMKVFGLP---IHDNWWMTEtggIMIANYPA---MDIKPgSMGKPLPGIEAAIVDDQGN 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  822 RCPTGVIGELYI-----SGFgiaNGYLGradlsaarfvaNP------FEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIK 890
Cdd:PRK04319  396 ELPPNRMGNLAIkkgwpSMM---RGIWN-----------NPekyesyFAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIK 459
                         490       500       510
                  ....*....|....*....|....*....|
gi 490930577  891 IRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:PRK04319  460 TSGERVGPFEVESKLMEHPAVAEAGVIGKP 489
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
464-986 1.63e-06

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 53.44  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  464 PRVSHPEQYNnVLDIFYEQVKKYPERTAIVsgERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVV 543
Cdd:PLN02330   20 PSVPVPDKLT-LPDFVLQDAELYADKVAFV--EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  544 MLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQ-NIQQLHLDQEGVQTQIRKQD-------ASDIP 615
Cdd:PLN02330   97 ALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGlGLPVIVLGEEKIEGAVNWKElleaadrAGDTS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  616 AeNRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLL-NLILShkptiywpvleavneRFPDRPLRAAHTHSFSfdsswLQV 694
Cdd:PLN02330  177 D-NEEILQTDLCALPFSSGTTGISKGVMLTHRNLVaNLCSS---------------LFSVGPEMIGQVVTLG-----LIP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  695 FWMLWG--------------------QELHIFDENMrrdafgLVQEIQQRQIdtldLPPSFCAqmMTNGLFVENQHHPSL 754
Cdd:PLN02330  236 FFHIYGitgiccatlrnkgkvvvmsrFELRTFLNAL------ITQEVSFAPI----VPPIILN--LVKNPIVEEFDLSKL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  755 IL--IGGEAAPLA--LWQQLNAQ-PALFAHNLYGPTEYTVDTFRAELKQTARPV-----IGNPIGNTQAYVLDRHL-QRC 823
Cdd:PLN02330  304 KLqaIMTAAAPLApeLLTAFEAKfPGVQVQEAYGLTEHSCITLTHGDPEKGHGIakknsVGFILPNLEVKFIDPDTgRSL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  824 PTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVEN 903
Cdd:PLN02330  384 PKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLH------TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEA 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  904 ALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEKtseqlSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:PLN02330  458 ILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKES-----EEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMR 532

                  ...
gi 490930577  984 KAL 986
Cdd:PLN02330  533 RLL 535
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1557-1953 1.72e-06

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. 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, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 53.20  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGE 1636
Cdd:cd05915    24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 QKDLaAIVHPSIATFAFnelFDETKVDLSSYKT------------TVITPQ---HPAYLIYTSGTTGQPKGVMVSHQ-AI 1700
Cdd:cd05915   104 PNLL-PLVEAIRGELKT---VQHFVVMDEKAPEgylayeealgeeADPVRVperAACGMAYTTGTTGLPKGVVYSHRaLV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRI-LWMQSEYPLSATDTILQKTPcTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIqKYQVTTLHFVPSMLAV 1779
Cdd:cd05915   180 LHSLaASLVDGTALSEKDVVLPVVP-MFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFD-GEGVTFTAGVPTVWLA 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1780 FENAATEIlssaqRQSLP-ICRVFCSGEALPTALAK-----SFTEHFSCELHNLYGPTEAAVDVSYMDATlglhPEESCV 1853
Cdd:cd05915   258 LADYLEST-----GHRLKtLRRLVVGGSAAPRSLIArfermGVEVRQGYGLTETSPVVVQNFVKSHLESL----SEEEKL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1854 AI----GYPVWNTQLYILDQYLRPVPvgVDGE----LYLAGHQLAMGYLHRADLTAsrfvANPFTAGqrMYRTGDIARWH 1925
Cdd:cd05915   329 TLkaktGLPIPLVRLRVADEEGRPVP--KDGKalgeVQLKGPWITGGYYGNEEATR----SALTPDG--FFRTGDIAVWD 400
                         410       420
                  ....*....|....*....|....*...
gi 490930577 1926 ADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:cd05915   401 EEGYVEIKDRLKDLIKSGGEWISSVDLE 428
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
625-919 2.38e-06

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: 52.60  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHkptiywpvLEAVNERFPDR-----PLraahTHSFSfDSSWLQVFWMLW 699
Cdd:cd05907    88 DLATIIYTSGTTGRPKGVMLSHRNILSNALAL--------AERLPATEGDRhlsflPL----AHVFE-RRAGLYVPLLAG 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  700 GQELHIFDENMRRDAFglvQEIQqrqidtldlPPSFCA-----QMMTNGLFVENQhhPSL------ILIGGE-------A 761
Cdd:cd05907   155 ARIYFASSAETLLDDL---SEVR---------PTVFLAvprvwEKVYAAIKVKAV--PGLkrklfdLAVGGRlrfaasgG 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  762 APLAlwqqlnAQPALFAHNL-------YGPTE----YTVDTFRAELKQTarpvIGNPIGNTQAYVLDRhlqrcptgviGE 830
Cdd:cd05907   221 APLP------AELLHFFRALgipvyegYGLTEtsavVTLNPPGDNRIGT----VGKPLPGVEVRIADD----------GE 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  831 LYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIR-GYRVEIGEVENALSILT 909
Cdd:cd05907   281 ILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASP 354
                         330
                  ....*....|
gi 490930577  910 NVESAVVIAE 919
Cdd:cd05907   355 LISQAVVIGD 364
PLN03052 PLN03052
acetate--CoA ligase; Provisional
828-997 4.68e-06

acetate--CoA ligase; Provisional


Pssm-ID: 215553 [Multi-domain]  Cd Length: 728  Bit Score: 52.00  E-value: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  828 IGE--LYISGFGiANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYR---VEIGEVE 902
Cdd:PLN03052  553 TGElaLFPLMFG-ASSTLLNADHYKVYFKGMPVFNGKILRRHGDIFERTSGGYYRAHGRADDTMNLGGIKvssVEIERVC 631
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  903 NAL--SILtnvESAVVIAEPINNS-HRLLGYCVVKDIELDEKTSEQLSQQYLSQLRQNL-PEYMVpSALTVMSEFPRNVS 978
Cdd:PLN03052  632 NAAdeSVL---ETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLnPLFKV-SAVVIVPSFPRTAS 707
                         170       180
                  ....*....|....*....|.
gi 490930577  979 GKVDKKALPK--PQIRAHSRM 997
Cdd:PLN03052  708 NKVMRRVLRQqlAQELSRSKL 728
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
523-646 5.97e-06

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 51.65  E-value: 5.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  523 GARKQTV------IAGAIPRSIDSVVVMLSVLNSGASFLPL-DLDYP--IDRMQMMCEDANPLFVLTTQALAQQLPQNIQ 593
Cdd:PRK07769   69 GARLQQVtkpgdrVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGVRKFFR 148
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  594 QLHLDQegvQTQIRKQDAsdIPAE------NRKFDFQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:PRK07769  149 ARPAKE---RPRVIAVDA--VPDEvgatwvPPEANEDTIAYLQYTSGSTRIPAGVQITH 202
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
829-932 7.44e-06

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 51.27  E-value: 7.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  829 GELYISGFGIANGYLGRADLSAARFVANpfEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIR-GYRVEIGEVENALSI 907
Cdd:PLN02387  503 GEIVIGGPSVTLGYFKNQEKTDEVYKVD--ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSV 580
                          90       100
                  ....*....|....*....|....*
gi 490930577  908 LTNVESAVVIAEPINNshrllgYCV 932
Cdd:PLN02387  581 SPYVDNIMVHADPFHS------YCV 599
PRK07470 PRK07470
acyl-CoA synthetase; Validated
484-656 8.07e-06

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 51.20  E-value: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  484 KKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPI 563
Cdd:PRK07470   18 RRFPDRIALVWGDR----SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  564 DRMQ----------MMCEDANPLFVLTTQALAQQLPQNIQQLHLDQE-GVQTQIRkqDASDIPAENRKFDFQDVAYVIFT 632
Cdd:PRK07470   94 DEVAylaeasgaraMICHADFPEHAAAVRAASPDLTHVVAIGGARAGlDYEALVA--RHLGARVANAAVDHDDPCWFFFT 171
                         170       180
                  ....*....|....*....|....
gi 490930577  633 SGSTGRPKGVMNTHGSLLNLILSH 656
Cdd:PRK07470  172 SGTTGRPKAAVLTHGQMAFVITNH 195
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
900-980 8.72e-06

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 45.61  E-value: 8.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   900 EVENALSILTNVESAVVIAEPINNS-HRLLGYCVVKDieldekTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVS 978
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKgEAPVAFVVLKP------GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRS 74

                   ..
gi 490930577   979 GK 980
Cdd:pfam13193   75 GK 76
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
624-655 8.94e-06

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: 51.06  E-value: 8.94e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 490930577  624 QDVAYVIFTSGSTGRPKGVMNTHGSLLNLILS 655
Cdd:cd05927   114 EDLATICYTSGTTGNPKGVMLTHGNIVSNVAG 145
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
126-352 1.08e-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: 50.53  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  126 LKAGETqlFRQVLFTTHDKVYW----YqryHHIMLDGFSMINLTKRIVELYQqlqeGKDLSVSPFIGVNEVISERQAYEn 201
Cdd:cd19532   105 LESGET--MRIVLLSLSPTEHYlifgY---HHIAMDGVSFQIFLRDLERAYN----GQPLLPPPLQYLDFAARQRQDYE- 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  202 SHQFKIDQAFWKAYCEDLPSPISL-STHHLAAKTTATFVKH---QLRFSTGILEQIQALAAQTK-------LAlndmmms 270
Cdd:cd19532   175 SGALDEDLAYWKSEFSTLPEPLPLlPFAKVKSRPPLTRYDThtaERRLDAALAARIKEASRKLRvtpfhfyLA------- 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  271 lSLH-YIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQK--YDAeqI 347
Cdd:cd19532   248 -ALQvLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRvpFDV--L 324

                  ....*
gi 490930577  348 LRDLN 352
Cdd:cd19532   325 LDELG 329
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
597-650 1.45e-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: 50.29  E-value: 1.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 490930577  597 LDQEGVQTQIRKQDASDIPAENRKfdfQDVAYVIFTSGSTGRPKGVMNTHGSLL 650
Cdd:cd17639    64 LGEDALIHSLNETECSAIFTDGKP---DDLACIMYTSGSTGNPKGVMLTHGNLV 114
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
1670-1701 1.48e-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: 50.43  E-value: 1.48e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 490930577 1670 TVITPQHP---AYLIYTSGTTGQPKGVMVSHQAIV 1701
Cdd:cd05933   142 AIISSQKPnqcCTLIYTSGTTGMPKGVMLSHDNIT 176
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
1680-1942 2.02e-05

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 49.84  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVMVSHQAIVNRIlwMQSEYPLSATDTIlqktpCTFDVSvwefFWSYLVGARLVIAPIDAH------- 1752
Cdd:PLN02861  225 IMYTSGTTGEPKGVILTNRAIIAEV--LSTDHLLKVTDRV-----ATEEDS----YFSYLPLAHVYDQVIETYciskgas 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1753 -----RDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSA------------------------QRQSLPI----- 1798
Cdd:PLN02861  294 igfwqGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGgmlrkklfdfaynyklgnlrkglkQEEASPRldrlv 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1799 -----------CRVFCSGEALPTALAKSFTEHFSCE-LHNLYGPTEAA-------VDVSYMDATLGLHPE------ESCV 1853
Cdd:PLN02861  374 fdkikeglggrVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCggcftsiANVFSMVGTVGVPMTtiearlESVP 453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1854 AIGYPVwntqlyildqyLRPVPvgvDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQYI 1933
Cdd:PLN02861  454 EMGYDA-----------LSDVP---RGEICLRGNTLFSGYHKRQDLTEEVLIDGWF-------HTGDIGEWQPNGAMKII 512

                  ....*....
gi 490930577 1934 GRADDQLKI 1942
Cdd:PLN02861  513 DRKKNIFKL 521
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
1656-1948 2.10e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 50.10  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1656 LFDE-TKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIlwmqseYPLSATDTILQKTPCT----FDVS 1730
Cdd:PTZ00342  284 LFDDmTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTV------VPLCKHSIFKKYNPKThlsyLPIS 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1731 -VWE---FFWSYLVGARLVIAPIDahrdpLALLSL-IQKYQVTTLHFVPSMLA-VFENAATEIlssaqrQSLPICRVFCS 1804
Cdd:PTZ00342  358 hIYErviAYLSFMLGGTINIWSKD-----INYFSKdIYNSKGNILAGVPKVFNrIYTNIMTEI------NNLPPLKRFLV 426
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1805 GEALptALAKS--------FTE---HFSC--------------------------ELHNL--------YGPTEAAVDVSY 1839
Cdd:PTZ00342  427 KKIL--SLRKSnnnggfskFLEgitHISSkikdkvnpnlevilngggklspkiaeELSVLlnvnyyqgYGLTETTGPIFV 504
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1840 MDATlGLHPEescvAIGYPVWNTQLYIL---DQY----LRPvpvgvDGELYLAGHQLAMGYLHRADLTASRFVANPFtag 1912
Cdd:PTZ00342  505 QHAD-DNNTE----SIGGPISPNTKYKVrtwETYkatdTLP-----KGELLIKSDSIFSGYFLEKEQTKNAFTEDGY--- 571
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 490930577 1913 qrmYRTGDIARWHADGSIQYIGRADDQLKI-RGQRIE 1948
Cdd:PTZ00342  572 ---FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
629-920 2.24e-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: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  629 VIFTSGSTGRPKGVMNTHGsllNLILSHKPTIY-WPVLEAvnerfpDR---PLRAAHTHSFSFDSSWLQVfwmlWGQELh 704
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHG---NLIAANLQLIHaMGLTEA------DVylnMLPLFHIAGLNLALATFHA----GGANV- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  705 ifdeNMRR-DAFGLVQEIQQRQIdTL--DLPPsfcaqMMTNGLFVENQHH---PSLILIGGEAAP--LALWQQLNaqPAL 776
Cdd:cd17637    71 ----VMEKfDPAEALELIEEEKV-TLmgSFPP-----ILSNLLDAAEKSGvdlSSLRHVLGLDAPetIQRFEETT--GAT 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  777 FaHNLYGPTE----YTVDTFRAelkqtaRP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAA 851
Cdd:cd17637   139 F-WSLYGQTEtsglVTLSPYRE------RPgSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAY 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577  852 RFvANPFEHgqrmyrTGDLVRWNSAGKLEFMGRC--DDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:cd17637   212 TF-RNGWHH------TGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP 275
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
625-649 3.86e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 49.20  E-value: 3.86e-05
                          10        20
                  ....*....|....*....|....*
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSL 649
Cdd:PTZ00216  265 DLALIMYTSGTTGDPKGVMHTHGSL 289
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
625-650 3.96e-05

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 48.96  E-value: 3.96e-05
                          10        20
                  ....*....|....*....|....*.
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSLL 650
Cdd:PLN02387  251 DIAVIMYTSGSTGLPKGVMMTHGNIV 276
PRK05850 PRK05850
acyl-CoA synthetase; Validated
503-646 4.23e-05

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 48.79  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAiPRSIDSVVVMLSVLNSGASFLPLDLDYP---IDRMQMMCEDANPLFVL 579
Cdd:PRK05850   36 LTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGALQAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVL 114
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577  580 TTQALAQQLPQNIQQlhlDQEGVQTQIRKQDASDIPAEN----RKFDFQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:PRK05850  115 TTSAVVDDVTEYVAP---QPGQSAPPVIEVDLLDLDSPRgsdaRPRDLPSTAYLQYTSGSTRTPAGVMVSH 182
PLN02479 PLN02479
acetate-CoA ligase
828-986 6.34e-05

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 48.30  E-value: 6.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  828 IGELYISGFGIANGYLGRADLSAARFvANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSI 907
Cdd:PLN02479  402 MGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFH------SGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYT 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  908 LTNVESAVVIAEPINN-SHRLLGYCVVKDiELDEKTSEQLSQQYLSQLRQNLPEYMVPSALtVMSEFPRNVSGKVDKKAL 986
Cdd:PLN02479  475 HPAVLEASVVARPDERwGESPCAFVTLKP-GVDKSDEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVL 552
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
626-983 6.54e-05

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: 48.25  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  626 VAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYWPVLEAVNERFPdrplraaHTHSFSFDSSWLQVFWMLWGQELHI 705
Cdd:cd05908   108 LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMP-------LTHDMGLIAFHLAPLIAGMNQYLMP 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  706 FDENMRRDAFGLVQeIQQRQIDTLDLP----PSFCAQMMTNGLFVENQHHPSLILIGGEAAPLALWQQLNAQPALFA--- 778
Cdd:cd05908   181 TRLFIRRPILWLKK-ASEHKATIVSSPnfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGlkr 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  779 ---HNLYGPTEYTVDTFRAELKQTARPVI----------------------------GNPIGNTQAYVLDRHLQRCPTGV 827
Cdd:cd05908   260 naiLPVYGLAEASVGASLPKAQSPFKTITlgrrhvthgepepevdkkdsecltfvevGKPIDETDIRICDEDNKILPDGY 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  828 IGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDL--VRwnsAGKLEFMGRCDDQIKIRGYRVEIGEVENAL 905
Cdd:cd05908   340 IGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDLgfIR---NGRLVITGREKDIIFVNGQNVYPHDIERIA 410
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  906 SILTNVESAVVIAEPINNSH----RLLGYCVVKD-----IELDEKTSEQLSQQYLSQLRQNLPeymvpsaltvMSEFPRN 976
Cdd:cd05908   411 EELEGVELGRVVACGVNNSNtrneEIFCFIEHRKseddfYPLGKKIKKHLNKRGGWQINEVLP----------IRRIPKT 480

                  ....*..
gi 490930577  977 VSGKVDK 983
Cdd:cd05908   481 TSGKVKR 487
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
1559-1957 7.29e-05

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: 48.19  E-value: 7.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1559 SFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG--- 1635
Cdd:cd17641    13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAede 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1636 EQKD----LAAIVH------------------PSIATFA----------------FNELFDETKvdlssykttvitPQHP 1677
Cdd:cd17641    93 EQVDklleIADRIPsvryviycdprgmrkyddPRLISFEdvvalgraldrrdpglYEREVAAGK------------GEDV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFdvsVWEFFwsYLVGARLVIA-PIDAHRDPL 1756
Cdd:cd17641   161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPW---IGEQM--YSVGQALVCGfIVNFPEEPE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1757 ALLSLIQKYQVttlHFVPSMLAVFENAATEILSSAQrQSLPICRVF---------------CSGEALPTALAK------- 1814
Cdd:cd17641   236 TMMEDLREIGP---TFVLLPPRVWEGIAADVRARMM-DATPFKRFMfelgmklglraldrgKRGRPVSLWLRLaswlada 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1815 ------------------------------SFTEHFSCELHNLYGPTEAAVdVSYMDATLGLHPEescvAIGYPVWNTQL 1864
Cdd:cd17641   312 llfrplrdrlgfsrlrsaatggaalgpdtfRFFHAIGVPLKQLYGQTELAG-AYTVHRDGDVDPD----TVGVPFPGTEV 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YILDQylrpvpvgvdGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKI-R 1943
Cdd:cd17641   387 RIDEV----------GEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAKDVGTTsD 450
                         490
                  ....*....|....
gi 490930577 1944 GQRIELGEIEQQLR 1957
Cdd:cd17641   451 GTRFSPQFIENKLK 464
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
1951-2025 9.52e-05

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 42.53  E-value: 9.52e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577  1951 EIEQQLRLISG-LDVVVHAISSEQnKANVqLVAY--LQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGK 2025
Cdd:pfam13193    1 EVESALVSHPAvAEAAVVGVPDEL-KGEA-PVAFvvLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PLN03051 PLN03051
acyl-activating enzyme; Provisional
861-1005 1.35e-04

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 47.12  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  861 GQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENAL--SILTNVESAVVIAEPINNSHRLLgYCVVKDIEL 938
Cdd:PLN03051  355 GMPLRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACdrAVAGIAETAAVGVAPPDGGPELL-VIFLVLGEE 433
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577  939 ----DEKTSEQLSQQYLSQLRQNL-PEYMVpSALTVMSEFPRNVSGKVDKKALpkpqiRAHSRMAETPEQQL 1005
Cdd:PLN03051  434 kkgfDQARPEALQKKFQEAIQTNLnPLFKV-SRVKIVPELPRNASNKLLRRVL-----RDQLKKELSGRSKL 499
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
625-649 1.35e-04

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 47.18  E-value: 1.35e-04
                          10        20
                  ....*....|....*....|....*
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSL 649
Cdd:PRK08180  210 TIAKFLFTSGSTGLPKAVINTHRML 234
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
487-649 1.50e-04

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: 47.04  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  487 PERTAIVSGERPN-LQHLSFAELAVKVNQLTRFLQENG---ARKQTVIAGaipRSIDSVVVMLSVLNSGASFLPLDLDYP 562
Cdd:cd05921     9 PDRTWLAEREGNGgWRRVTYAEALRQVRAIAQGLLDLGlsaERPLLILSG---NSIEHALMALAAMYAGVPAAPVSPAYS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  563 I-----DRMQMMCEDANPLFVLTT------QALAQQLPQNIQQLHL--DQEGVQTQIRKQDAS-----DIPAENRKFDFQ 624
Cdd:cd05921    86 LmsqdlAKLKHLFELLKPGLVFAQdaapfaRALAAIFPLGTPLVVSrnAVAGRGAISFAELAAtpptaAVDAAFAAVGPD 165
                         170       180
                  ....*....|....*....|....*
gi 490930577  625 DVAYVIFTSGSTGRPKGVMNTHGSL 649
Cdd:cd05921   166 TVAKFLFTSGSTGLPKAVINTQRML 190
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
19-224 1.93e-04

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: 46.54  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   19 FELASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYS-SDPSQPFIELNNQVQFQIEE 97
Cdd:cd19547     2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTwRDRAEPLQYVRDDLAPPWAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   98 FDFCHLTPKKAQQRLWDWMPSDRQCAKSLKAgeTQLFRQVLFTTHD-KVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQ 176
Cdd:cd19547    82 LDWSGEDPDRRAELLERLLADDRAAGLSLAD--CPLYRLTLVRLGGgRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 490930577  177 EGKDLSVSPFIGVNEVISERQAyeNSHQFKIDQAFWKAYCEDL-PSPIS 224
Cdd:cd19547   160 HGREPQLSPCRPYRDYVRWIRA--RTAQSEESERFWREYLRDLtPSPFS 206
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
1872-1968 2.00e-04

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 46.65  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1872 RPVPvgvDGELYLAGHQLAMGYLHRADLTASRFVANpfTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR-GQRIELG 1950
Cdd:PLN02387  498 KPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVD--ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLG 572
                          90
                  ....*....|....*....
gi 490930577 1951 EIEQQLRLISGLD-VVVHA 1968
Cdd:PLN02387  573 KVEAALSVSPYVDnIMVHA 591
PLN03051 PLN03051
acyl-activating enzyme; Provisional
1589-1954 2.39e-04

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 46.35  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1589 LPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG------------------EQKDLAAIVHPSIAT 1650
Cdd:PLN03051    1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTqdvvlrggralplyskvvEAAPAKAIVLPAAGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1651 FAFNELF--DETKVDL--SSYKTTVITPQH--PAYL--------IYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSAT 1716
Cdd:PLN03051   81 PVAVPLReqDLSWCDFlgVAAAQGSVGGNEysPVYApvesvtniLFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1717 DTILQKTPCTFDVSVWEFFWSYLVGARLVIApidaHRDPLA--LLSLIQKYQVTTLHFVPSMLAVFENAATeilSSAQRQ 1794
Cdd:PLN03051  161 DVVCWPTNLGWMMGPWLLYSAFLNGATLALY----GGAPLGrgFGKFVQDAGVTVLGLVPSIVKAWRHTGA---FAMEGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1795 SLPICRVFCS-GEA----------LPTALAKSFTEHfsCelhnlyGPTEAAVdvSYMDATLgLHPEeSCVAIGYPVWNTQ 1863
Cdd:PLN03051  234 DWSKLRVFAStGEAsavddvlwlsSVRGYYKPVIEY--C------GGTELAS--GYISSTL-LQPQ-APGAFSTASLGTR 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1864 LYILDQYLRPVPVG--VDGELYLAghQLAMGYLHR---ADLTASRFVANPF--TAGQRMYRTGDIARWHADGSIQYIGRA 1936
Cdd:PLN03051  302 FVLLNDNGVPYPDDqpCVGEVALA--PPMLGASDRllnADHDKVYYKGMPMygSKGMPLRRHGDIMKRTPGGYFCVQGRA 379
                         410
                  ....*....|....*...
gi 490930577 1937 DDQLKIRGQRIELGEIEQ 1954
Cdd:PLN03051  380 DDTMNLGGIKTSSVEIER 397
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
829-982 2.64e-04

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 46.50  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  829 GELYISGFGIANGYLgRADlsaARFVANPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSIL 908
Cdd:PRK06814  982 GRLFVRGPNVMLGYL-RAE---NPGVLEPPADG--WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAEL 1055
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  909 TNVESAVVIAEPinnshrllgycvvkdielDEKTSEQL----------SQQYLSQLRQN-LPEYMVPSALTVMSEFPRNV 977
Cdd:PRK06814 1056 WPDALHAAVSIP------------------DARKGERIillttasdatRAAFLAHAKAAgASELMVPAEIITIDEIPLLG 1117

                  ....*
gi 490930577  978 SGKVD 982
Cdd:PRK06814 1118 TGKID 1122
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
829-1004 3.60e-04

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 45.86  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  829 GELYISGFGIANGYL-----GRADLSAARFVANPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVEN 903
Cdd:PRK08043  554 GRLQLKGPNIMNGYLrvekpGVLEVPTAENARGEMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQ 631
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  904 -ALSILTNVESAVVIAEPINNSHRLLGYcvVKDIELdekTSEQLSQQYLSqlrQNLPEYMVPSALTVMSEFPRNVSGKVD 982
Cdd:PRK08043  632 lALGVSPDKQHATAIKSDASKGEALVLF--TTDSEL---TREKLQQYARE---HGVPELAVPRDIRYLKQLPLLGSGKPD 703
                         170       180
                  ....*....|....*....|..
gi 490930577  983 KKALpkpqirahSRMAETPEQQ 1004
Cdd:PRK08043  704 FVTL--------KSMVDEPEQH 717
prpE PRK10524
propionyl-CoA synthetase; Provisional
851-986 3.64e-04

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 45.71  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  851 ARFVANPFEH-GQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVV-IAEPInNSHRL 927
Cdd:PRK10524  460 DRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVaEVAVVgVKDAL-KGQVA 538
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577  928 LGYCVVKDIEL--DEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK10524  539 VAFVVPKDSDSlaDREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAI 599
PRK08315 PRK08315
AMP-binding domain protein; Validated
477-651 3.71e-04

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 45.57  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  477 DIFYEQVKKYPERTAIVSGERpNLqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLS---------- 546
Cdd:PRK08315   20 QLLDRTAARYPDREALVYRDQ-GL-RWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFAtakigailvt 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  547 ------------VLN-SGASFLPL-----DLDYpidrMQMMCEDANPLFVLTTQAL-AQQLPQNIQQLHLDQEG------ 601
Cdd:PRK08315   98 inpayrlseleyALNqSGCKALIAadgfkDSDY----VAMLYELAPELATCEPGQLqSARLPELRRVIFLGDEKhpgmln 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490930577  602 ---VQTQIRKQDASDIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLN 651
Cdd:PRK08315  174 fdeLLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILN 226
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
1672-1719 4.13e-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: 45.36  E-value: 4.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1672 ITPQHPAYLIYTSGTTGQPKGVMVSHQaivnRILWMQSEYPLS---ATDTI 1719
Cdd:cd05938   141 VTIKSPALYIYTSGTTGLPKAARISHL----RVLQCSGFLSLCgvtADDVI 187
PLN02246 PLN02246
4-coumarate--CoA ligase
480-649 7.92e-04

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 44.59  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  480 YEQVKKYPERTAIVSGerPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLsvlnsGASFLpldl 559
Cdd:PLN02246   30 FERLSEFSDRPCLIDG--ATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFL-----GASRR---- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  560 dypidrmQMMCEDANPLFvlTTQALAQQL-----------PQNIQQL--HLDQEGVQ--------------TQIRKQDAS 612
Cdd:PLN02246   99 -------GAVTTTANPFY--TPAEIAKQAkasgakliitqSCYVDKLkgLAEDDGVTvvtiddppegclhfSELTQADEN 169
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 490930577  613 DIPAEnrKFDFQDVAYVIFTSGSTGRPKGVMNTHGSL 649
Cdd:PLN02246  170 ELPEV--EISPDDVVALPYSSGTTGLPKGVMLTHKGL 204
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
496-650 1.39e-03

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 44.19  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  496 ERPNLQHLSFAELAVKVNQLTRFLQENGARKQTViaGA-IPRSIDSVVVMLSVLNSGasFLPLDLDYP--IDRMQMMCED 572
Cdd:PRK06814  652 EDPVNGPLTYRKLLTGAFVLGRKLKKNTPPGENV--GVmLPNANGAAVTFFALQSAG--RVPAMINFSagIANILSACKA 727
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  573 ANPLFVLTT---------QALAQQLPQNIQQLHLdqEGVQTQIRKQD---------ASDIPAENRKFDfqDVAYVIFTSG 634
Cdd:PRK06814  728 AQVKTVLTSrafiekarlGPLIEALEFGIRIIYL--EDVRAQIGLADkikgllagrFPLVYFCNRDPD--DPAVILFTSG 803
                         170
                  ....*....|....*.
gi 490930577  635 STGRPKGVMNTHGSLL 650
Cdd:PRK06814  804 SEGTPKGVVLSHRNLL 819
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
151-383 1.64e-03

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: 43.40  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  151 YHHIMLDGFSMINLTKRIVELYQQLQEGKDLSVSPFIGVN--EVISERQAYENSHQFKIDQAFWKAYCEDLPSPISL--- 225
Cdd:cd20483   131 SHHIAWDRGSSKSIFEQFTALYDALRAGRDLATVPPPPVQyiDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKLlpf 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  226 -STHHLAAKTTATfVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTL 304
Cdd:cd20483   211 aKAERPPVKDYER-STVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVG 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  305 PTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLN-----------SIDIHERMYGPILNYKAFDQD 373
Cdd:cd20483   290 FFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSAVPFDYIVDALDvprstshfpigQIAVNYQVHGKFPEYDTGDFK 369
                         250
                  ....*....|.
gi 490930577  374 LV-IDGEKVKT 383
Cdd:cd20483   370 FTdYDHYDIPT 380
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
305-439 1.86e-03

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: 43.06  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  305 PTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSiDIHERMYGPILNYK-AFDQDLVIDGEKVKT 383
Cdd:cd19542   265 PCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGL-WPSGTLFNTLVSYQnFEASPESELSGSSVF 343
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577  384 HHISTGPIDDFEFSFIVQDH--ELIIELRADSQRYTQDELFNHGQRLTLLLEQALIRP 439
Cdd:cd19542   344 ELSAAEDPTEYPVAVEVEPSgdSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
PLN02736 PLN02736
long-chain acyl-CoA synthetase
1674-1701 1.88e-03

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 43.55  E-value: 1.88e-03
                          10        20
                  ....*....|....*....|....*...
gi 490930577 1674 PQHPAYLIYTSGTTGQPKGVMVSHQAIV 1701
Cdd:PLN02736  220 PEDVATICYTSGTTGTPKGVVLTHGNLI 247
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
612-662 1.91e-03

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 43.59  E-value: 1.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577  612 SDIPAEnrKFDFQDVAYVIFTSGSTGRPKGVM-NTHGSLLNLILSH------KPT-IYW 662
Cdd:PRK00174  235 DECEPE--PMDAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAAMTMkyvfdyKDGdVYW 291
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
782-986 1.95e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 43.48  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  782 YGPTEYTVDTFRAElkQTARPVIGNPIGNTQAYVLDRhLQRCPTGV-------------IGELY-ISGFGIANGYLGRAD 847
Cdd:PRK13388  295 YGSSEGAVIVVREP--GTPPGSIGRGAPGVAIYNPET-LTECAVARfdahgallnadeaIGELVnTAGAGFFEGYYNNPE 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  848 LSAARFvanpfEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNShrl 927
Cdd:PRK13388  372 ATAERM-----RHG--MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERV--- 441
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577  928 lGYCVVKDIELDEKTS-------EQLSQQylsqlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK13388  442 -GDQVMAALVLRDGATfdpdafaAFLAAQ------PDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
2141-2252 2.37e-03

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 41.91  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2141 SGHPLFCF--YPGSGSAWQYTVlnRYLHSDLPIIGL------QSPRPDGllanSTDMDELVEkQLEIMRKQQPTGPYTLL 2212
Cdd:COG0596    22 DGPPVVLLhgLPGSSYEWRPLI--PALAAGYRVIAPdlrghgRSDKPAG----GYTLDDLAD-DLAALLDALGLERVVLV 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 490930577 2213 GYSLGGTVAYAVAAKlteQGEKVDYLGLLDTYPAEIHQWL 2252
Cdd:COG0596    95 GHSMGGMVALELAAR---HPERVAGLVLVDEVLAALAEPL 131
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
1122-1329 2.65e-03

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 42.77  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1122 YNAFTRLS--LNGDIDPVRLQQALITVLKRHPQLGGHFDSElaeepvfiyslhPTQAWPVQFCSVTPDLLEQTIQEALQQ 1199
Cdd:PRK09294   20 YEAFTGYTahLRGVLDIDALSDAFDALLRAHPVLAAHLEQD------------SDGGWELVADDLLHPGIVVVDGDAARP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1200 PIH--LDQPYGLIRATLIQHApEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ---TNQQLPVLEH----SYETVI--- 1267
Cdd:PRK09294   88 LPElqLDQGVSLLALDVVPDD-GGARVTLYIHHSIADAHHSASLLDELWSRYTDvvtTGDPGPIRPQpapqSLEAVLaqr 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1268 ----KALSGRDhETSKVIWQRDLADLQPLILFNQAQ--QAVQETSYRLSAELGAKLQHKLRQQGITLN 1329
Cdd:PRK09294  167 girrQALSGAE-RFMPAMYAYELPPTPTAAVLAKPGlpQAVPVTRCRLSKAQTSSLAAFGRRHRLTVN 233
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
624-650 2.73e-03

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 43.16  E-value: 2.73e-03
                          10        20
                  ....*....|....*....|....*..
gi 490930577  624 QDVAYVIFTSGSTGRPKGVMNTHGSLL 650
Cdd:PRK08043  365 EDAALILFTSGSEGHPKGVVHSHKSLL 391
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
152-352 3.17e-03

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: 42.37  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  152 HHIMLDGFSMINLTKRIVELYQQLQEGK--DLSVSPFIGVNEVISERQAYEnSHQFKIDQAFWKAYCEDLpSPISLSTHH 229
Cdd:cd19539   134 HHTAFDAWSLDVFARDLAALYAARRKGPaaPLPELRQQYKEYAAWQREALA-APRAAELLDFWRRRLRGA-EPTALPTDR 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  230 LAAKTTAtFVKHQLRFST--GILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTV 307
Cdd:cd19539   212 PRPAGFP-YPGADLRFELdaELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFV 290
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 490930577  308 NVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLN 352
Cdd:cd19539   291 NLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQLVAELP 335
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
840-972 3.89e-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: 42.28  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  840 NGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAE 919
Cdd:cd05938   363 LGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV 442
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490930577  920 PINNSHRLLGYCVVKdieLDEKTSEQLSQQYlSQLRQNLPEYMVPSALTVMSE 972
Cdd:cd05938   443 TVPGHEGRIGMAAVK---LKPGHEFDGKKLY-QHVREYLPAYARPRFLRIQDS 491
PLN02736 PLN02736
long-chain acyl-CoA synthetase
624-650 4.25e-03

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 42.39  E-value: 4.25e-03
                          10        20
                  ....*....|....*....|....*..
gi 490930577  624 QDVAYVIFTSGSTGRPKGVMNTHGSLL 650
Cdd:PLN02736  221 EDVATICYTSGTTGTPKGVVLTHGNLI 247
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
1678-1701 5.75e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 41.89  E-value: 5.75e-03
                          10        20
                  ....*....|....*....|....
gi 490930577 1678 AYLIYTSGTTGQPKGVMVSHQAIV 1701
Cdd:PTZ00216  267 ALIMYTSGTTGDPKGVMHTHGSLT 290
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
865-958 8.04e-03

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 41.29  E-value: 8.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  865 YRTGDLVRWNSA----G----KLEF-MGRCDDQIKIRG---YRVEIGEVENALSILTnvESAVVIAEPINNSHRLlgycV 932
Cdd:COG1541   297 YRTGDLTRLLPEpcpcGrthpRIGRiLGRADDMLIIRGvnvFPSQIEEVLLRIPEVG--PEYQIVVDREGGLDEL----T 370
                          90       100
                  ....*....|....*....|....*..
gi 490930577  933 VKdIELDEKTS-EQLSQQYLSQLRQNL 958
Cdd:COG1541   371 VR-VELAPGASlEALAEAIAAALKAVL 396
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
93-351 9.34e-03

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: 40.93  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577   93 FQIEEFDFCHLTPKKAQQRLWDWmpsdRQcAKS---LKAGETQLFRQVLFTTHDKVYwyqRYH----HIMLDGFSMINLT 165
Cdd:cd19535    75 YGITVHDLRGLSEEEAEAALEEL----RE-RLShrvLDVERGPLFDIRLSLLPEGRT---RLHlsidLLVADALSLQILL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  166 KRIVELYQQlqEGKDLsvsPFIGVN---EVISERQAYENSHQfkIDQAFWKAYCEDLPSPISLSthhLAAK----TTATF 238
Cdd:cd19535   147 RELAALYED--PGEPL---PPLELSfrdYLLAEQALRETAYE--RARAYWQERLPTLPPAPQLP---LAKDpeeiKEPRF 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577  239 VKHQLRFSTGILEQIQALAAQTKLALNDMMMSlslhyIYkmtdkAE-----------LVNgIP-FMRRLGSKAIRS---- 302
Cdd:cd19535   217 TRREHRLSAEQWQRLKERARQHGVTPSMVLLT-----AY-----AEvlarwsgqprfLLN-LTlFNRLPLHPDVNDvvgd 285
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 490930577  303 -TlptvNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDL 351
Cdd:cd19535   286 fT----SLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSYSGVVVVRRL 331
 
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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